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1000 results found for “Other Cytokines”

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  • View Data Sheet

    Description:

    Granulocyte Chemotactic Protein 2 (CXCL6) Human Recombinant

    C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    Product # :

    CHM-025

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    Description

    GCP-2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9kDa.

    Source

    Escherichia Coli.

    Formulation

    GCP-2 protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

    More Info

    • Introduction

      Granulocyte Chemotactic Protein 2 (CXCL6), also known as GCP-2, is a Chemotactic for neutrophil granulocytes. GCP-2 signals through binding and activation of its receptors (CXCR1 and CXCR2). GCP-2 has strong antibacterial activity against Gram-positive and Gram-negative bacteria In addition to its chemotactic and angiogenic property.

    • Synonyms

      C-X-C motif chemokine 6, Chemokine alpha 3, CKA-3, Granulocyte chemotactic protein 2, GCP-2, Small-inducible cytokine B6.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GCP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCP-2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized GCP-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.

    • Background

      What is the molecular weight/Mw of CXCL6 HUMAN Protein?
      CXCL6 HUMAN Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CXCL6 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL6 HUMAN Protein?
      CXCL6 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL6 HUMAN Protein?
      Fully biologically active when compared to standard. The biological activity determined by a chemotaxis bioassay using human neutrophils is in a concentration range of 10-50 ng/ml corresponding to a specific activity of 20,000-100,000 IU/mg.

      What is the amino acid sequence of CXCL6 HUMAN Protein?
      VLTELRCTCL RVTLRVNPKT IGKLQVFPAG PQCSKVEVVA SLKNGKQVCL DPEAPFLKKV IQKILDSGNK KN.

      What applications can CXCL6 HUMAN Protein be used in?
      CXCL6 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL6 HUMAN Protein?
      The endotoxin level is minimal, CXCL6 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL6 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL6 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Gcp 2 Human
  • View Data Sheet

    Description:

    GM-CSF Receptor Beta Human Recombinant

    CSF2RB,Colony Stimulating Factor 2 Receptor, Beta, Low-Affinity (Granulocyte-Macrophage), GM-CSF/IL-3/IL-5 Receptor Common Beta Subunit, CDw131, IL3RB, SMDP5, IL5RB, Interleukin 3 Receptor/Granulocyte-Macrophage Colony Stimulating Factor 3 Receptor, Beta (High Affinity), Colony-Stimulating Factor-2 Receptor, Beta, Low-Affinity, GM-CSF/IL-3/IL-5 Receptor Common Beta-Chain, Cytokine Receptor Common Subunit Beta, CD131 Antigen, CD131.

    Product # :

    CYT-928

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    • sds-page

    Description

    CSF2RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids (17-443 a.a) and having a molecular mass of 49.7kDa. CSF2RB is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CSF2RB protein solution (0.5mg/ml) containing Phosphate Buffered Saline(pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      GM-CSF Receptor Beta, also known as CSF2RB is a member of the type I cytokine receptor family. CSF2RB is a high affinity receptor for interleukin-3, interleukin-5 as well as granulocyte-macrophage colony-stimulating factor. CSF2RB unique form of receptor assembly applies also to IL-3 and IL-5 receptors, providing a structural basis for understanding their activation mechanism which is essential for the development of therapeutics.

    • Synonyms

      CSF2RB,Colony Stimulating Factor 2 Receptor, Beta, Low-Affinity (Granulocyte-Macrophage), GM-CSF/IL-3/IL-5 Receptor Common Beta Subunit, CDw131, IL3RB, SMDP5, IL5RB, Interleukin 3 Receptor/Granulocyte-Macrophage Colony Stimulating Factor 3 Receptor, Beta (High Affinity), Colony-Stimulating Factor-2 Receptor, Beta, Low-Affinity, GM-CSF/IL-3/IL-5 Receptor Common Beta-Chain, Cytokine Receptor Common Subunit Beta, CD131 Antigen, CD131.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      WERSLAGAEE TIPLQTLRCY NDYTSHITCR WADTQDAQRL VNVTLIRRVN EDLLEPVSCD LSDDMPWSAC PHPRCVPRRC VIPCQSFVVT DVDYFSFQPD RPLGTRLTVT LTQHVQPPEP RDLQISTDQD HFLLTWSVAL GSPQSHWLSP GDLEFEVVYK RLQDSWEDAA ILLSNTSQAT LGPEHLMPSS TYVARVRTRL APGSRLSGRP SKWSPEVCWD SQPGDEAQPQ NLECFFDGAA VLSCSWEVRK EVASSVSFGL FYKPSPDAGE EECSPVLREG LGSLHTRHHC QIPVPDPATH GQYIVSVQPR RAEKHIKSSV NIQMAPPSLN VTKDGDSYSL RWETMKMRYE HIDHTFEIQY RKDTATWKDS KTETLQNAHS MALPALEPST RYWARVRVRT SRTGYNGIWS EWSEARSWDT ESVLPMWLEH HHHHH.

    • Background

      Title: GM-CSF Receptor Beta Human Recombinant: A Key Receptor in Immunological Research

      Abstract:


      Granulocyte-macrophage colony-stimulating factor receptor beta (GM-CSF Rβ) is a crucial receptor involved in immune cell development and function. This research paper provides a comprehensive analysis of human recombinant GM-CSF Rβ, focusing on its production, characterization, and applications in immunological research. The paper discusses the significance of GM-CSF Rβ in immune cell signaling and its role in various immune-related disorders. Furthermore, it elucidates the potential therapeutic implications of recombinant GM-CSF Rβ in immunotherapy and highlights ongoing research in the field. The information presented in this paper aims to enhance the understanding of human recombinant GM-CSF Rβ and its utility as a research tool in immunological studies.

      Introduction:


      Granulocyte-macrophage colony-stimulating factor receptor beta (GM-CSF Rβ) is a high-affinity receptor that binds to granulocyte-macrophage colony-stimulating factor (GM-CSF). It plays a critical role in immune cell development, differentiation, and activation. Human recombinant GM-CSF Rβ, produced through genetic engineering techniques, enables researchers to investigate its biological functions and therapeutic potential.

      Production and Characterization:


      Recombinant GM-CSF Rβ is typically produced using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and binding affinity of the recombinant receptor.

      Immunological Significance:


      GM-CSF Rβ is expressed on various immune cells, including myeloid cells, dendritic cells, and macrophages. It plays a crucial role in cell signaling pathways, promoting cell proliferation, survival, and activation. The dysregulation of GM-CSF Rβ signaling has been implicated in autoimmune diseases, inflammatory disorders, and hematological malignancies. Recombinant GM-CSF Rβ provides a valuable tool for investigating these immune-related processes and deciphering the underlying mechanisms.

      Therapeutic Implications:


      The dysregulation of GM-CSF Rβ signaling in immune-related disorders has prompted the exploration of recombinant GM-CSF Rβ as a potential therapeutic target. Targeted therapies, such as monoclonal antibodies and small-molecule inhibitors, are being developed to modulate GM-CSF Rβ signaling and restore immune homeostasis. Ongoing research focuses on optimizing these therapeutic approaches and identifying novel treatment strategies.

      Conclusion:


      Human recombinant GM-CSF Rβ is a critical research tool in the field of immunology. Its production, characterization, and applications in immune cell signaling contribute to our understanding of immune responses and the development of novel therapeutics. Continued research and advancements in GM-CSF Rβ-based immunotherapy hold promise for improving treatment outcomes in various immune-related disorders.

      What is the molecular weight/Mw of CD131 Protein?
      CD131 Protein has a total Mw of 49.7kDa.

      What is the source or expression system of CD131 Protein?
      Sf9, Baculovirus cells.
      What is the Purity of CD131 Protein?
      CD131 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CD131 Protein?
      The biological functionality of CD131 Protein will be determined in the future.

      What is the amino acid sequence of CD131 Protein?
      WERSLAGAEE TIPLQTLRCY NDYTSHITCR WADTQDAQRL VNVTLIRRVN EDLLEPVSCD LSDDMPWSAC PHPRCVPRRC VIPCQSFVVT DVDYFSFQPD RPLGTRLTVT LTQHVQPPEP RDLQISTDQD HFLLTWSVAL GSPQSHWLSP GDLEFEVVYK RLQDSWEDAA ILLSNTSQAT LGPEHLMPSS TYVARVRTRL APGSRLSGRP SKWSPEVCWD SQPGDEAQPQ NLECFFDGAA VLSCSWEVRK EVASSVSFGL FYKPSPDAGE EECSPVLREG LGSLHTRHHC QIPVPDPATH GQYIVSVQPR RAEKHIKSSV NIQMAPPSLN VTKDGDSYSL RWETMKMRYE HIDHTFEIQY RKDTATWKDS KTETLQNAHS MALPALEPST RYWARVRVRT SRTGYNGIWS EWSEARSWDT ESVLPMWLEH HHHHH.

      What applications can CD131 Protein be used in?
      CD131 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CD131 Protein?
      The endotoxin level is minimal, CD131 Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Csf2Rb Human
  • View Data Sheet

    Description:

    Monocyte Chemotactic Protein-1 Human Recombinant (CCL2)

    Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    Product # :

    CHM-271

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    Description

    Monocyte Chemotactic Protein-1 Human Recombinant also known as Monocyte Chemotactic and Activating Factor (MCAF) produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 8.6kDa. The MCP-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL2 was lyophilized from a concentrated (1mg/ml) sterile solution without any additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC and SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 2 (CCL2) is a small cytokine belonging to the CC chemokine family that is also known as monocyte chemotactic protein-1 (MCP-1). It is found at the site of tooth eruption and bone degradation. In the bone, CCL2 is expressed by mature osteoclasts and osteoblasts and is under the control of nuclear factor ?B (NF?B). CCL2 recruits immune cells, such as monocytes, to sites of tissue injury and infection. This chemokine is produced as a protein precursor containing signal peptide of 23 amino acids and a mature peptide of 76 amino acids. It is a monomeric polypeptide, with a molecular weight of approximately 13kDa. As with many other CC chemokines, CCL2 is located on chromosome 17 in humans. The cell surface receptors that bind CCL2 are CCR2 and CCR5.

    • Synonyms

      Small inducible cytokine A2, CCL2, Monocyte chemotactic protein 1, MCP-1, Monocyte chemoattractant protein 1, Monocyte chemotactic and activating factor, MCAF, Monocyte secretory protein JE, HC11, chemokine (C-C motif) ligand 2, MCP1, SCYA2, GDCF-2, SMC-CF, HSMCR30, MGC9434, GDCF-2 HC11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL2 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Monocyte Chemotactic Protein-1in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

    • Background

      What is the molecular weight/Mw of CCL2 HUMAN Protein?
      CCL2 HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of CCL2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL2 HUMAN Protein?
      CCL2 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL2 HUMAN Protein?
      The specific activity as determined by the ability of MCP-1 to chemoattract human THP-1 cells is detectable starting at 1ng/ml.

      What is the amino acid sequence of CCL2 HUMAN Protein?
      QPDAINAPVT CCYNFTNRKI SVQRLASYRR ITSSKCPKEA VIFKTIVAKE ICADPKQKWV QDSMDHLDKQ TQTPKT.

      What applications can CCL2 HUMAN Protein be used in?
      CCL2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL2 HUMAN Protein?
      The endotoxin level is minimal, CCL2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL2 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL2 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mcp 1 Human
  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)

    Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

    Product # :

    CHM-320

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    Description

    Macrophage Inflammatory Protein-1 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 1mg/ml solution containing no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. They also induce the synthesis and release of other pro-inflammatory cytokines such as interleukin 1 (IL-1), IL-6 and TNF-a from fibroblasts and macrophages. The genes for CCL3 and CCL4 are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A3, CCL3, Macrophage inflammatory protein 1-alpha, MIP-1-alpha, Tonsillar lymphocyte LD78 alpha protein, G0/G1 switch regulatory protein 19-1, G0S19-1 protein, SIS-beta, PAT 464.1, chemokine (C-C motif) ligand 3, MIP1A, SCYA3, G0S19-1, LD78ALPHA, TY-5, SIS-alpha, L2G25B.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.

    • Background

      What is the molecular weight/Mw of MIP 1A MOUSE Protein?
      MIP 1A MOUSE Protein has a total Mw of 7.82kDa.

      What is the source or expression system of MIP 1A MOUSE Protein?
      Escherichia Coli.

      What is the Purity of MIP 1A MOUSE Protein?
      MIP 1A MOUSE Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A MOUSE Protein?
      The Activity is calculated by the ability to chemoattract of Balb3/C splenocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of MIP 1A MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Tyr-Gly-Ala.

      What applications can MIP 1A MOUSE Protein be used in?
      MIP 1A MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1A MOUSE Protein?
      The endotoxin level is minimal, MIP 1A MOUSE Protein was purified using conventional chromatography techniques.



    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mip 1A Mouse
  • View Data Sheet

    Description:

    Twisted Gastrulation Protein Human Recombinant

    Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

    Product # :

    CYT-873

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    Description

    TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.

    Source

    CHO.

    Formulation

    Lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to inhibit alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.

    More Info

    • Introduction

      Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.

    • Synonyms

      Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Tsg Human
  • View Data Sheet

    Description:

    Leptin, Mouse Anti-Human

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    ANT-172

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    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Solubility

      Reconstitute with sterile H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      r.Human Leptin.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      YD-HLEP4B6.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.8 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.

    • Purification Method

      Ion exchange.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Antibody
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    Description:

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant (CXCL5)

    Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    Product # :

    CHM-331

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    • sds-page

    Description

    Epithelial Neutrophil-Activating Protein 78 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8020 Dalton. The CXCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL5 was lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg)  of recombinant human ENA-78.

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    • Introduction

      Chemokine (C-X-C motif) ligand 5 (CXCL5) is a small cytokine belonging to the CXC chemokine family that is also known as epithelial-derived neutrophil-activating peptide 78 (ENA-78). It is produced following stimulation of cells with the inflammatory cytokines interleukin-1 or tumor necrosis factor-alpha. Expression of CXCL5 has also been observed in eosinophils, and can be inhibited with the type II IFN. This chemokine stimulates the chemotaxis of neutrophils possesses angiogenic properties. It elicits these effects by interacting with the cell surface chemokine receptor CXCR2. The gene for CXCL5 is encoded on four exons and is located on human chromosome 4 amongst several other CXC chemokine genes. CXCL5 has been implicated in connective tissue remodelling.

    • Synonyms

      Small inducible cytokine B5, CXCL5, Epithelial-derived neutrophil-activating protein 78, Neutrophil-activating peptide ENA-78, ENA-78(1-78), chemokine (C-X-C motif) ligand 5, SCYB5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized ENA78 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL5 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ENA-78 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.

    • Background

      What is the molecular weight/Mw of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein has a total Mw of 8.02kDa.

      What is the source or expression system of CXCL5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL5 HUMAN Protein?
      CXCL5 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL5 HUMAN Protein?
      The biological activity was determined by measuring the dose dependent mobilization of intracellular calcium (calcium flux) with human neutrophils. Significant calcium mobilization is observed with 100ng/mL (corresponding to a Specific Activity of 10,000IU/mg) of recombinant human ENA-78.

      What is the amino acid sequence of CXCL5 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala- Ala -Val-Leu-Arg.

      What applications can CXCL5 HUMAN Protein be used in?
      CXCL5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL5 HUMAN Protein?
      The endotoxin level is minimal, CXCL5 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL5 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL5 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ena 78 Human
  • View Data Sheet

    Description:

    IP-10 Mouse Recombinant (CXCL10)

    Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    Product # :

    CHM-336

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    • sds-page

    Description

    IP-10 Mouse Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8701 Dalton. The IP-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IP-10 was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

    sds-page

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.

    • Synonyms

      Small inducible cytokine B10, CXCL10, 10 kDa, Gamma-IP10, IP-10, chemokine (C-X-C motif) ligand 10, C7, IFI10, INP10, crg-2, mob-1, SCYB10, gIP-10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

    • Background

      What is the molecular weight/Mw of CXCL10 MOUSE Protein?
      CXCL10 MOUSE Protein has a total Mw of 8.7kDa.

      What is the source or expression system of CXCL10 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL10 MOUSE Protein?
      CXCL10 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL10 MOUSE Protein?
      Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 100.0-500.0 ng/ml.

      What is the amino acid sequence of CXCL10 MOUSE Protein?
      IPLARTVRCN CIHIDDGPVR MRAIGKLEII PASLSCPRVE IIATMKKNDE QRCLNPESKT IKNLMKAFSQ KRSKRAP.

      What applications can CXCL10 MOUSE Protein be used in?
      CXCL10 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL10 MOUSE Protein?
      The endotoxin level is minimal, CXCL10 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL10 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.02 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of IP-10 as a Reference Standard.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ip 10 Mouse
  • View Data Sheet

    Description:

    IP-10 Rat Recombinant (CXCL10)

    C-X-C motif chemokine 10, Gamma-IP10, IP-10, Protein Mob-1, Small-inducible cytokine B10, Cxcl10, Inp10, Mob1, Scyb10.

    Product # :

    CHM-264

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    Description

    IP-10 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 77 amino acids and having a molecular mass of 8.6kDa.The IP-10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 10.0-50.0 ng/ml.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand 10 (CXCL10) is a small cytokine belonging to the CXC chemokine family. CXCL10 is secreted by several cell types in response to IFN-?. These cell types include monocytes, endothelial cells and fibroblasts. CXCL10 has been attributed to several roles, such as chemoattraction for monocytes and T cells, promotion of T cell adhesion to endothelial cells, antitumor activity, and inhibition of bone marrow colony formation and angiogenesis. The gene for CXCL10 is located on human chromosome 4 in a cluster among several other CXC chemokines. This chemokine elicits its effects by binding to the cell surface chemokine receptor CXCR3. The three-dimensional crystal structure of this chemokine has been determined under 3 different conditions to a resolution of up to 1.92A.

    • Synonyms

      C-X-C motif chemokine 10, Gamma-IP10, IP-10, Protein Mob-1, Small-inducible cytokine B10, Cxcl10, Inp10, Mob1, Scyb10.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IP-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized IP-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IPLARTVRCT CIDFHEQPLR PRAIGKLEII PASLSCPHVE IIATMKKNNE KRCLNPESEA IKSLLKAVSQ RRSKRAP.

    • Background

      What is the molecular weight/Mw of CXCL10 RAT Protein?
      CXCL10 RAT Protein has a total Mw of 8.6kDa.

      What is the source or expression system of CXCL10 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL10 RAT Protein?
      CXCL10 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL10 RAT Protein?
      Determined by its ability to chemoattract hCXCR3/HEK293 cells using a concentration range of 10.0-50.0 ng/ml.

      What is the amino acid sequence of CXCL10 RAT Protein?
      IPLARTVRCT CIDFHEQPLR PRAIGKLEII PASLSCPHVE IIATMKKNNE KRCLNPESEA IKSLLKAVSQ RRSKRAP.

      What applications can CXCL10 RAT Protein be used in?
      CXCL10 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL10 RAT Protein?
      The endotoxin level is minimal, CXCL10 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL10 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL10 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ip 10 Rat
  • View Data Sheet

    Description:

    NT-Pro-B-type Natriuretic Protein Canine Recombinant

    NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    Product # :

    CYT-1223

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    Description

    NT-proBNP Canine produced in E.coli is a single, non-glycosylated polypeptide chain (1-85 a.a) containing 101 a.a and having a molecular mass of 10,545 Dalton. NT-proBNP is fused with a 16 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT-proBNP was lyophilized from 10mM potassium phosphate, pH 7.4 and 150 mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      NPPB, Natriuretic Peptide Precursor B, BNP, B-type Natriuretic Peptide.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NT-proBNP although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NT-Pro B-type Natriuretic Protein should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NT-proBNP in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      N-terminal pro-brain natriuretic peptide, or NT-proBNP, has emerged as a significant biomarker in cardiovascular medicine, providing crucial insights into heart function and aiding in the diagnosis and management of heart-related conditions. This peptide, released in response to cardiac stress, reflects the heart's intricate signaling mechanisms and physiological responses. The study of NT-proBNP, especially in its recombinant form, has not only deepened our understanding of heart diseases but has also led to the development of advanced diagnostic tools and potential therapeutic interventions. This research delves into the world of NT-proBNP Recombinant Protein, exploring its biochemical intricacies, physiological roles, and its profound impact on cardiovascular healthcare.

      Structural and Molecular Complexity of NT-proBNP:

      NT-proBNP, derived from proBNP through enzymatic cleavage, is a stable peptide fragment. It acts as a precursor to the biologically active B-type natriuretic peptide (BNP) hormone. Understanding the molecular structure and processing of NT-proBNP is essential for unraveling the regulatory mechanisms governing its release and its significance in cardiovascular physiology.

      Physiological Significance in Heart Function:

      BNP and its precursor, NT-proBNP, play pivotal roles in cardiac homeostasis. They are secreted by ventricular myocardial cells in response to increased wall stress, primarily due to volume and pressure overload. Elevated levels of NT-proBNP serve as a sensitive indicator of heart failure, reflecting the heart's struggle to maintain effective circulation. Monitoring NT-proBNP levels aids clinicians in diagnosing heart failure, assessing its severity, and guiding therapeutic strategies, ultimately improving patient outcomes.

      Diagnostic Applications and Clinical Relevance:

      NT-proBNP assays, often utilizing recombinant NT-proBNP proteins, have become cornerstones in cardiovascular diagnostics. Elevated levels of NT-proBNP are indicative of heart failure, providing vital information for early intervention and personalized treatment plans. Moreover, the peptide's utility extends to predicting cardiovascular events, aiding in risk stratification among individuals with or at risk of heart diseases. The incorporation of NT-proBNP testing into clinical practice has significantly enhanced the accuracy and timeliness of cardiovascular disease diagnosis.

      Potential Therapeutic Implications:

      Research into NT-proBNP’s regulatory pathways has opened avenues for therapeutic interventions. Targeted therapies aimed at modulating the BNP system are under investigation, offering potential strategies for managing heart failure and related conditions. By understanding the complex interplay between NT-proBNP, its receptor systems, and cardiac function, researchers are exploring novel therapies to optimize cardiovascular health.

      NT-proBNP Recombinant Protein, with its intricate involvement in cardiac physiology and its applications in diagnostics and potential therapeutics, stands as a beacon of hope in the realm of cardiovascular medicine. Its role as a diagnostic marker not only aids in early disease detection but also empowers clinicians to tailor treatments, improving patient outcomes and quality of life. As research continues to unravel the complexities of NT-proBNP, it holds the promise of not only enhancing our understanding of heart diseases but also shaping the future of cardiovascular healthcare. This research underscores the vital role of NT-proBNP in cardiovascular medicine, emphasizing its potential to transform the landscape of heart disease diagnosis and treatment.

      What is the molecular weight / Mw of NT-proBNP Canine?
      NT-proBNP Canine has a total Mw of 10,545 Da.

      What is the source or expression system of NT-proBNP Canine?
      Escherichia Coli.

      What is the Purity of NT-proBNP Canine?
      NT-proBNP Canine is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of NT-proBNP Canine?
      The biological functionality of NT-proBNP Canine will be determined in the future.

      What is the amino acid sequence of NT-proBNP Canine?
      NT-proBNP Canine Protein is composed from 16 amino acids.

      What applications can NT-proBNP Canine be used in?
      NT-proBNP Canine can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for NT-proBNP Canine?
      The endotoxin level is minimal, NT-proBNP Canine was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Probnp Canine
  • View Data Sheet

    Description:

    RANK Ligand Soluble Human Recombinant

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-334

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    • HPLC, SDS-PAGE

    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 19.7kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution containing 10mM Sodium phosphate, pH-7.5.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The activity of RAW-Blue was measured to be 46.96 ng/ml, corresponding to a specific activity of 2.1x104 units/mg.

    HPLC, SDS-PAGE

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TNFSF11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution sRANKL should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized sRANKL in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EKAMVDGSW LDLAKRSKLE AQPFAHLTIN ATDIPSGSHK VSLSSWYHDR GWAKISNMTF SNGKLIVNQD GFYYLYANIC FRHHETSGDL ATEYLQLMVY VTKTSIKIPS SHTLMKGGST KYWSGNSEFH FYSINVGGFF KLRSGEEISI EVSNPSLLDP DQDATYFGAF KVRDID.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Rankl Human
  • View Data Sheet

    Description:

    Exodus-2 (CCL21) Mouse Recombinant, Sf9

    Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    Product # :

    CHM-043

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    Description

    Exodus-2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (24-133aa) and having a molecular mass of 13.1kDa.Exodus-2 is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Exodus-2 solution (0.5mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Exodus-2 protein or CCL21 is a cytokine, part of the CC chemokines subgroup. Because of its 6 conserved residues of the cysteine amino acid (instead of the 4 residues we usually see in chemokines), the protein is also named 6Ckine and SLC (secondary lymphoid-tissue chemokine). The gene that codes for this protein is located on chromosome 9 in humans. The Exodus-2 is binding to the CCR7 receptor, which is a chemokine receptor located to the cell’s surface.

    • Synonyms

      Ccl21a, C-C motif chemokine 21a, 6Ckine, Beta-chemokine exodus-2, Small-inducible cytokine A21a,Thymus-derived chemotactic agent 4, TCA4, Ccl21a, Scya21, Scya21a, 6CKBAC2, 6Ckine, ALP,AW987545, CKb9, plt, Scya21b, SLC.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

    • Background

      What is the molecular weight/Mw of CCL21 MOUSE, SF9 Protein?
      CCL21 MOUSE, SF9 Protein has a total Mw of 13.1kDa.

      What is the source or expression system of CCL21 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CCL21 MOUSE, SF9 Protein?
      CCL21 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL21 MOUSE, SF9 Protein?
      The biological functionality of CCL21 MOUSE, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CCL21 MOUSE, SF9 Protein?
      ADPSDGGGQD CCLKYSQKKI PYSIVRGYRK QEPSLGCPIP AILFSPRKHS KPELCANPEE GWVQNLMRRL DQPPAPGKQS PGCRKNRGTS KSGKKGKGSK GCKRTEQTQP SRGHHHHHH

      What applications can CCL21 MOUSE, SF9 Protein be used in?
      CCL21 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL21 MOUSE, SF9 Protein?
      The endotoxin level is minimal, CCL21 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL21 MOUSE, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL21 MOUSE, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Exodus 2 Mouse
  • View Data Sheet

    Description:

    Mucosae-Associated Epithelial Chemokine (CCL28) Rat Recombinant

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-278

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    Description

    MEC Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13.1kDa. The Rat MEC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and150mM NaCl.

    Purity

    Greater than 95.0% as determined by
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MEC although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution MEC should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized MEC in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

    • Background

      What is the molecular weight/Mw of CCL28 RAT Protein?
      CCL28 RAT Protein has a total Mw of 13.1kDa.

      What is the source or expression system of CCL28 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL28 RAT Protein?
      CCL28 RAT Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CCL28 RAT Protein?
      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

      What applications can CCL28 RAT Protein be used in?
      CCL28 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 RAT Protein?
      The endotoxin level is minimal, CCL28 RAT Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ccl28 Rat
  • View Data Sheet

    Description:

    Interleukin-8 (1-72 a.a) Porcine Recombinant (CXCL8)

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.

    Product # :

    CHM-340

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    Description

    Interleukin-8 Porcine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 9.1kDa. The IL8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP, Alveolar macrophage chemotactic factor I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.

    • Background

      What is the molecular weight/Mw of CXCL8 PORCINE (1-72) Protein?
      CXCL8 PORCINE (1-72) Protein has a total Mw of 9.1kDa.

      What is the source or expression system of CXCL8 PORCINE (1-72) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 PORCINE (1-72) Protein?
      CXCL8 PORCINE (1-72) Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 PORCINE (1-72) Protein?
      The biological activity was determined by a chemotaxis bioassay using human peripheral blood neutrophils is in a concentration range of 20-200 ng/ml.

      What is the amino acid sequence of CXCL8 PORCINE (1-72) Protein?
      ARVSAELRCQ CINTHSTPFH PKFIKELRVI ESGPHCENSE IIVKLVNGKE VCLDPKEKWV QKVVQIFLKR TEKQQQQQ.

      What applications can CXCL8 PORCINE (1-72) Protein be used in?
      CXCL8 PORCINE (1-72) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 PORCINE (1-72) Protein?
      The endotoxin level is minimal, CXCL8 PORCINE (1-72) Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 PORCINE (1-72) that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL8 PORCINE (1-72)?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 8 72 Porcine
  • View Data Sheet

    Description:

    Apolipoprotein-M Human Recombinant

    G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    Product # :

    CYT-715

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    • sds-page

    Description

    APOM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (23-188 a.a.) and having a molecular mass of 20.9 kDa. APOM protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    APOM Human solution containing 20mM Tris-HCl pH-8 1mM DTT & 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      APOM is belongs to the lipocalin protein family and is associated with high density lipoproteins and to a lesser extent with low density lipoproteins and triglyceride-rich lipoproteins. APOM is secreted through the plasma membrane but remains membrane-bound, where it takes part in lipid transport. .

    • Synonyms

      G3a, HSPC336, NG20, Apolipoprotein M, APOM, Apo-M, MGC22400.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

    • Background

      Apolipoprotein-M Human Recombinant: Insights into its Role in Lipid Metabolism and Cardiovascular Health

      Abstract:


      Apolipoprotein-M (ApoM), a unique member of the apolipoprotein family, has gained significant attention in the field of lipid metabolism and cardiovascular health. This research paper provides a comprehensive analysis of ApoM human recombinant, exploring its structure, function, and potential implications in cardiovascular diseases. Understanding the intricate nature of ApoM sheds light on its significance as a potential biomarker and therapeutic target in cardiovascular disorders. This article presents a concise yet comprehensive examination of ApoM, highlighting its impact on human health.

      Introduction:


      Cardiovascular diseases remain a leading cause of global morbidity and mortality, underscoring the importance of understanding lipid metabolism and its association with cardiovascular health. ApoM, an intriguing apolipoprotein, has emerged as a key player in lipid metabolism and cardiovascular function. This paper delves into the intricate nature of ApoM, elucidating its structure, molecular interactions, and potential roles in cardiovascular diseases.

      Structure and Function of Apolipoprotein-M:


      ApoM exhibits a unique structural configuration, comprising a single membrane-bound alpha-helix and a lipocalin-like domain. It predominantly associates with high-density lipoproteins (HDL) and plays a critical role in HDL metabolism and cholesterol transport. Additionally, ApoM has been implicated in endothelial function, inflammation, and modulation of sphingolipid metabolism.

      Apolipoprotein-M and Cardiovascular Diseases:


      Studies have highlighted the potential involvement of ApoM in cardiovascular diseases, such as atherosclerosis and coronary artery disease. Genetic variations in the ApoM gene and alterations in ApoM levels have been associated with disease development and progression. Understanding the role of ApoM in cardiovascular diseases offers insights into potential therapeutic interventions and diagnostic strategies.

      Apolipoprotein-M Human Recombinant Production:


      The production of ApoM human recombinant is made possible through advanced biotechnological techniques, including recombinant DNA technology and protein expression systems. These methods facilitate large-scale production, purification, and characterization of ApoM, providing opportunities for further research and potential therapeutic applications.

      Therapeutic Potential of Apolipoprotein-M Human Recombinant:


      Exploring the therapeutic potential of ApoM holds promise in the field of cardiovascular disorders. Strategies aimed at modulating ApoM expression or function may contribute to the prevention or treatment of lipid metabolism-related diseases. Furthermore, ApoM may serve as a potential biomarker for risk assessment and monitoring of cardiovascular conditions.

      Conclusion:


      Apolipoprotein-M human recombinant represents a fascinating area of research, shedding light on the role of this protein in lipid metabolism and cardiovascular health. Understanding the structure, function, and genetic implications of ApoM is pivotal in advancing our knowledge and exploring its potential as a therapeutic target. Continued investigation into the mechanisms and signaling pathways involving ApoM will likely pave the way for innovative strategies in the diagnosis, prevention, and treatment of cardiovascular diseases.

      What is the molecular weight/Mw of APOM Protein?
      APOM Protein has a total Mw of 20.9kDa.

      What is the source or expression system of APOM Protein?
      Escherichia Coli.

      What is the Purity of APOM Protein?
      APOM Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of APOM Protein?
      The biological functionality of APOM Protein will be determined in the future.

      What is the amino acid sequence of APOM Protein?
      MGSSHHHHHH SSGLVPRGSH MCPEHSQLTT LGVDGKEFPE VHLGQWYFIA GAAPTKEELA TFDPVDNIVF NMAAGSAPMQ LHLRATIRMK DGLCVPRKWI YHLTEGSTDL RTEGRPDMKT ELFSSSCPGG IMLNETGQGY QRFLLYNRSP HPPEKCVEEF KSLTSCLDSK AFLLTPRNQE ACELSNN.

      What applications can APOM Protein be used in?
      APOM Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for APOM Protein?
      The endotoxin level is minimal, APOM Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Apom Human
  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-1 Beta Human Recombinant (CCL4)

    Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.

    Product # :

    CHM-276

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    Description

    Macrophage Inflammatory Protein-1 beta Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7620 Dalton. The CCL4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now also named CCL3 and CCL4. Both factors are produced by macrophages after they are stimulated with bacterial endotoxins. MIP-1a and MIP-1b activate human granulocytes (neutrophils, eosinophils and basophils) which can lead to acute neutrophilic inflammation. MIP-1a and MIP-1b induce synthesis and release of other pro-inflammatory cytokines such as interleukin-1 (IL-1), IL-6 and TNF-alpha from fibroblasts and macrophages. CCL3 and CCL4 genes are both located on human chromosome 17.

    • Synonyms

      Small inducible cytokine A4, CCL4, Macrophage inflammatory protein 1-beta, MIP-1- beta, MIP-1-beta(1-69), T-cell activation protein 2, ACT-2, PAT 744, H400, SIS-gamma, Lymphocyte activation gene 1 protein, LAG-1, HC21, G-26 T-lymphocyte-secreted protein, chemokine (C-C motif) ligand 4, ACT2, G-26, LAG1, MIP1B, SCYA4, AT744.1, MGC104418, MGC126025, MGC126026.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL4 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Macrophage Inflammatory Protein-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.

    • Background

      What is the molecular weight/Mw of MIP 1B HUMAN Protein?
      MIP 1B HUMAN Protein has a total Mw of 7.62kDa.

      What is the source or expression system of MIP 1B HUMAN Protein?
      Escherichia Coli.

      What is the Purity of MIP 1B HUMAN Protein?
      MIP 1B HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1B HUMAN Protein?
      The Activity is calculated by the ability to chemoattract Human blood monocytes using a concentration of 5-20ng/ml corresponding to a Specific Activity of 50,000-200,000IU/mg.

      What is the amino acid sequence of MIP 1B HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be, Ala-Pro-Met-Gly-Ser.

      What applications can MIP 1B HUMAN Protein be used in?
      MIP 1B HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for MIP 1B HUMAN Protein?
      The endotoxin level is minimal, MIP 1B HUMAN Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mip 1B Human
  • View Data Sheet

    Description:

    Interleukin-8 (1-72) (CXCL8) Human Recombinant, GST Tag

    Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    Product # :

    CHM-047

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    Description

    Recombinant Human Interleukin-8 produced in E. coli containing 72 amino acids.Recombinant Human Interleukin-8 is fused to GST tag at its N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    IL8 GST solution contains 25mM Tris-Base/ 25mM K2CO3.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining).

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      Interleukin-8, IL-8, C-X-C motif chemokine 8, IL8, CXCL8

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Applications

      Immunoassay.

    • Background

      What is the source or expression system of CXCL8 HUMAN, GST Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, GST Protein?
      The biological functionality of CXCL8 HUMAN, GST Protein will be determined in the future.

      What is the amino acid sequence of CXCL8 HUMAN, GST Protein?
      CXCL8 HUMAN, GST Protein is composed from 72 amino acids.

      What applications can CXCL8 HUMAN, GST Protein be used in?
      CXCL8 HUMAN, GST Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN, GST Protein?
      The endotoxin level is minimal, CXCL8 HUMAN, GST Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 HUMAN, GST that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL8 HUMAN, GST?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 8 Human
  • View Data Sheet

    Description:

    Bone Morphogenetic Protein Receptor Type IA Human Recombinant

    BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    Product # :

    CYT-380

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    Description

    BMPR1A Human Recombinant extracellular domain produced in baculovirus is a monomeric, glycosylated, Polypeptide chain fused with 6xHis tag at C-terminus and having a molecular mass of 23 kDa. The BMR1A is purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    CD292 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1X PBS.

    Purity

    Greater than 90.0% as determined by
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.

    More Info

    • Introduction

      The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.

    • Synonyms

      BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein Receptor 1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized ALK-3 in sterile PBS not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Bone Morphogenetic Protein Receptor Type IA Human Recombinant: Exploring the Potential of a Key Regulator in Bone Development

      Abstract:

      Bone Morphogenetic Protein Receptor Type IA (BMPR1A) human recombinant is a crucial regulator in bone development and homeostasis. This research paper provides a comprehensive analysis of BMPR1A, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMPR1A human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Bone development and maintenance rely on intricate signaling pathways, with BMPR1A playing a pivotal role in bone morphogenesis. This paper explores the unique features of BMPR1A and presents novel approaches for its production and optimization, aiming to uncover its therapeutic potential in bone-related disorders.

      Characteristics and Signaling Pathways:

      BMPR1A belongs to the serine/threonine kinase receptor family and is expressed predominantly in skeletal tissues. It binds bone morphogenetic proteins (BMPs), initiating intracellular signaling cascades that regulate osteoblast differentiation and bone formation. BMPR1A activates the Smad-dependent and Smad-independent pathways, leading to the activation of transcription factors involved in bone-specific gene expression.

      Production of BMPR1A Human Recombinant:

      Efficient production methodologies are critical for harnessing the therapeutic potential of BMPR1A human recombinant. Mammalian cell-based expression systems, such as Chinese hamster ovary (CHO) cells, have been utilized to ensure proper folding and post-translational modifications. Optimization strategies, including codon optimization and vector engineering, have been employed to enhance production efficiency. Purification techniques, such as affinity chromatography and size exclusion chromatography, have been optimized to obtain high-quality BMPR1A recombinant protein.

      Potential Therapeutic Applications:

      BMPR1A human recombinant holds significant promise in regenerative medicine. Disruption of BMP signaling has been implicated in skeletal disorders, including bone fractures, osteoporosis, and skeletal dysplasias. Modulating BMPR1A activity using BMPR1A human recombinant may provide a targeted therapeutic approach for promoting bone regeneration, fracture healing, and bone tissue engineering. Furthermore, BMPR1A signaling plays a role in other tissues, such as the cardiovascular system and nervous system, suggesting broader therapeutic applications.

      Conclusion:

      BMPR1A human recombinant represents a crucial regulator in bone development and holds immense potential in regenerative medicine. Optimizing production methodologies and further understanding its signaling pathways will enhance its clinical utility. With its implications in skeletal disorders and potential applications in other tissues, BMPR1A human recombinant stands as a promising tool for promoting bone regeneration and tissue engineering.

      What is the molecular weight/Mw of BMPR1A Protein?
      BMPR1A Protein has a total Mw of 23kDa.

      What is the source or expression system of BMPR1A Protein?
      Insect Cells.

      What is the Purity of BMPR1A Protein?
      BMPR1A Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMPR1A Protein?
      Measured by its ability to inhibit recombinant human BMP-2 induced alkaline phosphatase production by C2C12 myogenic cells. The ED50 for this effect is typically 1-3 µg/ml in the presence of 500 ng/ml of recombinant human BMP-2 corresponding to a Specific Activity of 2,000 units/mg.

      What applications can BMPR1A Protein be used in?
      BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMPR1A Protein?
      The endotoxin level is minimal, BMPR1A Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Bmpr1A Human
  • View Data Sheet

    Description:

    Leptin Clone PAT7E10AT, Mouse Anti Human

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    ANT-690

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human Leptin mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human Leptin amino acids 22-167 purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and k light chain.

    • Clone

      PAT7E10AT.

    • Applications

      Leptin antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      Leptin antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Leptin Pat7E10At Antibody
  • View Data Sheet

    Description:

    Macrophage-Derived Chemokine Human Recombinant (CCL22)

    C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    Product # :

    CHM-250

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    Description

    MDC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 69 amino acids and having a molecular mass of 8.1 kDa. The MDC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CCL22 filtered (0.4µm) and lyophilized from a concentrated solution containing 20mM phosphate buffer & 500mM NaCl pH-7.4.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      MDC (CCL22) is a small cytokine that belongs to the CC chemokine family. CCL22 is one of several Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16.
      MDC shows chemotactic activity for natural killer cells, chronically activated T lymphocytes, monocytes and dendritic cells. On the other hand, MDC shows a mild activity for primary activated T lymphocytes and has no chemoattractant activity for neutrophils, eosinophils and resting T lymphocytes. MDC may also have a role in the trafficking of activated T lymphocytes to inflammatory sites and other aspects of activated T lymphocyte physiology. MDC interacts with cell surface chemokine receptors CCR4.
      CCL22 is vastly expressed in macrophage and in monocyte-derived dendritic cells, and thymus. CCL22 is also found in the lymph node, appendix, activated monocytes, resting and activated macrophages. Lower expression of CCL22 can be seen in the lung and the spleen and very weak expression in the small intestine. In the lymph node CCL22 is expressed in a mature subset of Langerhans' cells (CD1a+ and CD83+).
      Furthermore, CCL22 is expressed in atopic dermatitis, allergic contact dermatitis skin, and psoriasis, in both the epidermis and dermis. In addition, MDC has a role in hindering progression of lung cancer. Moreover, significantly higher CCL22 expression is linked to gastric cancer.

    • Synonyms

      C-C motif chemokine 22, Small-inducible cytokine A22, Macrophage-derived chemokine, MDC(1-69), Stimulated T-cell chemotactic protein 1, CC chemokine STCP-1, CCL22, MDC, SCYA22, ABCD-1, DC/B-CK, MGC34554, A-152E5.1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CCL22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL22 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized CCL22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

    • Background

      What is the molecular weight/Mw of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein has a total Mw of 8.1kDa.

      What is the source or expression system of CCL22 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL22 HUMAN Protein?
      CCL22 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL22 HUMAN Protein?
      Determined by its ability to chemoattract human T cells using a concentration range of 10ng-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL22 HUMAN Protein?
      GPYGANMEDS VCCRDYVRYR LPLRVVKHFY WTSDSCPRPG VVLLTFRDKE ICADPRVPWV KMILNKLSQ.

      What applications can CCL22 HUMAN Protein be used in?
      CCL22 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL22 HUMAN Protein?
      The endotoxin level is minimal, CCL22 HUMAN Protein was purified using conventional chromatography techniques.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mdc Human
  • View Data Sheet

    Description:

    Interleukin-8 (1-77 a.a) Human Recombinant (CXCL8)

    IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    Product # :

    CHM-327

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    • sds-page

    Description

    Interleukin-8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8904 Dalton. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

    sds-page

    More Info

    • Introduction

      Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies. When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.

    • Synonyms

      IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL8 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Interleukin 8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein has a total Mw of 8.9kDa.

      What is the source or expression system of CXCL8 HUMAN (1-77) Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 HUMAN (1-77) Protein?
      CXCL8 HUMAN (1-77) Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN (1-77) Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 25-150 ng/ml.

      What is the amino acid sequence of CXCL8 HUMAN (1-77) Protein?
      AVLPRSAKEL RCQCIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE NWVQRVVEKF LKRAENS.

      What applications can CXCL8 HUMAN (1-77) Protein be used in?
      CXCL8 HUMAN (1-77) Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL8 HUMAN (1-77) Protein?
      The endotoxin level is minimal, CXCL8 HUMAN (1-77) Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CXCL8 HUMAN (1-77) that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL8 HUMAN (1-77)?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Il 8 77 Human
  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-3 alpha Mouse Recombinant (CCL20)

    Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

    Product # :

    CHM-236

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    Description

    Macrophage Inflammatory Protein-3 alpha Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7.9 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

    Purity

    Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

    More Info

    • Introduction

      CCL20 is a chemotactic factor that draws lymphocytes & neutrophils, rather than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
      MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.

    • Synonyms

      Small inducible cytokine A20 precursor, CCL20, Macrophage inflammatory protein 3 alpha, MIP-3-alpha, Liver and activation- regulated chemokine, CC chemokine LARC, Beta chemokine exodus-1, CKb4, LARC, ST38, MIP3A, MIP-3a, SCYA20, C-C motif chemokine 20, CC chemokine ST38, exodus-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL-20 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized MIP-3a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.

    • Background

      What is the molecular weight/Mw of CCL20 MOUSE Protein?
      CCL20 MOUSE Protein has a total Mw of 7.9kDa.

      What is the source or expression system of CCL20 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CCL20 MOUSE Protein?
      CCL20 MOUSE Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL20 MOUSE Protein?
      The Activity is calculated by its ability to chemoattract primary human T cells at 2-20ng/ml, corresponding to a specific activity of 50,000-500,000 units/mg.

      What is the amino acid sequence of CCL20 MOUSE Protein?
      ASNYDCCLSY IQTPLPSRAI VGFTRQMADE ACDINAIIFH TKKRKSVCAD PKQNWVKRAV NLLSLRVKKM.

      What applications can CCL20 MOUSE Protein be used in?
      CCL20 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL20 MOUSE Protein?
      The endotoxin level is minimal, CCL20 MOUSE Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Mip 3A Mouse
  • View Data Sheet

    Description:

    Exodus-2 Human Recombinant (CCL21)

    Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

    Product # :

    CHM-332

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    Description

    Exodus-2 Human Recombinant produced in E.Coli as a single, non-glycosylated, polypeptide chain containing 111 amino acids and having a molecular mass of 12219 Dalton. The CCL21 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Phosphate Buffer, pH 7.4 and 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human total lymphocyte population using a concentration range of 10-100ng/ml.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.

    • Synonyms

      Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Exodus2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.

    • Background

      What is the molecular weight/Mw of CCL21 HUMAN Protein?
      CCL21 HUMAN Protein has a total Mw of 12.21kDa.

      What is the source or expression system of CCL21 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL21 HUMAN Protein?
      CCL21 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL21 HUMAN Protein?
      Determined by its ability to chemoattract human total lymphocyte population using a concentration range of 10-100ng/ml.

      What is the amino acid sequence of CCL21 HUMAN Protein?
      SDGGAQDCCL KYSQRKIPAK VVRSYRKQEP SLGCSIPAIL FLPRKRSQAE LCADPKELWV QQLMQHLDKT PSPQKPAQGC RKDRGASKTG KKGKGSKGCR KTERSQTPKG P.

      What applications can CCL21 HUMAN Protein be used in?
      CCL21 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL21 HUMAN Protein?
      The endotoxin level is minimal, CCL21 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL21 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL21 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ccl21 Human
  • View Data Sheet

    Description:

    Interferon Induced With Helicase C Domain 1 Human Recombinant

    Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    Product # :

    PRO-1505

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    Description

    IFIH1 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 152,000 Dalton. IFIH1 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    IFIH1 is supplied in 20mM HEPES buffer pH-7.9, 550mM NaCl and 6M Urea.

    Purity

    Greater than 93.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IFIH1 is a DEAD box protein which is upregulated in response to treatment with beta-interferon and a protein kinase C-activating compound, mezerein. Irreversible reprogramming of melanomas can be attained by therapy with both these agents; treatment with either agent alone only achieves reversible differentiation. DEAD box proteins are implicated in several cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly.

    • Synonyms

      Interferon-induced helicase C domain-containing protein 1, Clinically amyopathic dermatomyositis autoantigen 140 kDa, CADM-140 autoantigen, Helicase with 2 CARD domains, Helicard, Interferon-induced with helicase C domain protein 1, Melanoma differentiation-associated protein 5, MDA-5, Murabutide down-regulated protein, RIG-I-like receptor 2, RLR-2, RNA helicase-DEAD box protein 116, IFIH1, MDA5, RH116, Hlcd, IDDM19.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Ifih1 Human