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1000 results found for “Interleukin 8 (CXCL8)”

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  • View Data Sheet

    Description:

    Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3), His Tag

    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.

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    CHM-347

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    • SDS-PAGE

    Description

    MIP-1a Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 90 amino acids (24-92 a.a.) and having a molecular mass of 10.0kDa. MIP-1a is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP-1a protein solution (0.25mg/ml) containing 10mM Sodium Citrate buffer (pH 3.5) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    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.

    • 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

      MGSSHHHHHH SSGLVPRGSH MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPGV IFLTKRSRQVCADPSEEWVQ KYVSDLELSA.

    • Background

      What is the molecular weight/Mw of MIP 1A HUMAN, HIS Protein?
      MIP 1A HUMAN, HIS Protein has a total Mw of 10kDa.

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

      What is the Purity of MIP 1A HUMAN, HIS Protein?
      MIP 1A HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A HUMAN, HIS Protein?
      The biological functionality of MIP 1A HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of MIP 1A HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPGV IFLTKRSRQVCADPSEEWVQ KYVSDLELSA.

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

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

      Who supplies recombinant MIP 1A HUMAN, HIS 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 MIP 1A HUMAN, HIS?
      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.

    Mip 1A Human His
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    Description:

    RELM-Gamma Mouse Recombinant

    Resistin-like gamma, RELMgamma,RELM-γ, RELM-g. 

    Product # :

    CYT-1035

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    Description

    RELM g Mouse Recombinant produced in E.Coli is a non glycosylated, homodimeric polypeptide chain containing 2 x 89 amino acids and having a total molecular mass of 18.9kDa. The RELM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.

    • Synonyms

      Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized RELM g although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution RELM g Mouse 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 RELM g in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MEGTLESIVE KKVKELLANR DDCPSTVTKT FSCTSITASG RLASCPSGMT VTGCACGYGC GSWDIRDGNT CHCQCSTMDW ATARCCQLA.

    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.

    Mouse Relm Gamma
  • View Data Sheet

    Description:

    Interleukin-29 Human Recombinant, His Tag

    Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.

    Product # :

    CYT-864

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    Description

    IL 29 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids (20-200 a.a) and having a molecular mass of 22.7kDa.IL 29 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL 29 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL-29 is distantly related to type I interferons and the IL-10 family. Expression of IL-29 is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-29 exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
      IL-29 acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda3 are closely positioned genes on human chromosome 19.
      IL-29 induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
      IL-29 is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-29 produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
      IFN-Lambda 1 antiviral and antiproliferative activity requires Interferon-Lambda 2 receptor tyrosine residues.

    • Synonyms

      Interferon lambda-1, IL-29, IL29, IFN-lambda-1, Cytokine Zcyto21, Interleukin-29.

    • 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 MGSHMGPVPT SKPTTTGKGC HIGRFKSLSP QELASFKKAR DALEESLKLK NWSCSSPVFP GNWDLRLLQV RERPVALEAE LALTLKVLEA AAGPALEDVL DQPLHTLHHI LSQLQACIQP QPTAGPRPRG RLHHWLHRLQ EAPKKESAGC LEASVTFNLF RLLTRDLKYV ADGNLCLRTS THPEST.

    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 29 Human His
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    Description:

    Interleukin-7 Human Recombinant, sf9

    Interleukin 7, IL-7, Interleukin-7.

    Product # :

    CYT-975

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    • SDS-PAGE

    Description

    IL7 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 161 amino acids (26-177 a.a.) and having a molecular mass of 18.4kDa. IL7 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL7 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      IL-7 is a cytokine important for B and T cell development. This cytokine and the hepatocyte growth factor (HGF) form a heterodimer that functions as a pre-pro-B cell growth-stimulating factor. This cytokine is found to be a cofactor for V(D)J rearrangement of the T cell receptor beta (TCRB) during early T cell development. This cytokine can be produced locally by intestinal epithelial and epithelial goblet cells, and may serve as a regulatory factor for intestinal mucosal lymphocytes. Knockout studies in mice suggested that this cytokine plays an essential role in lymphoid cell survival.

    • Synonyms

      Interleukin 7, IL-7, Interleukin-7.

    • 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

      ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, SF9 Protein?
      IL7 HUMAN, SF9 Protein has a total Mw of 18.4kDa.

      What is the source or expression system of IL7 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL7 HUMAN, SF9 Protein?
      IL7 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL7 HUMAN, SF9 Protein?
      The biological functionality of IL7 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of IL7 HUMAN, SF9 Protein?
      ADPDCDIEGK DGKQYESVLM VSIDQLLDSM KEIGSNCLNN EFNFFKRHIC DANKEGMFLF RAARKLRQFL KMNSTGDFDL HLLKVSEGTT ILLNCTGQVK GRKPAALGEA QPTKSLEENK SLKEQKKLND LCFLKRLLQE IKTCWNKILM GTKEHHHHHH H.

      What applications can IL7 HUMAN, SF9 Protein be used in?
      IL7 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL7 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL7 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL7 HUMAN, 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 IL7 HUMAN, 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.

    Il7 Human Sf9
  • View Data Sheet

    Description:

    Interleukin-17 Receptor Beta Human Recombinant

    Interleukin 17 Receptor B, IL17RH1, IL17BR, Interleukin 17B Receptor, Cytokine, Receptor-Like 4, Interleukin-17B Receptor, IL-17 Receptor Homolog 1, IL-17 Receptor B, IL-17B Receptor, IL-17Rh1, IL-17RB, EVI27, CRL4, Interleukin 17 Receptor Homolog 1, Interleukin-17 Receptor B, Cytokine Receptor CRL4.

    Product # :

    CYT-901

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    Description

    IL17RB Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 514 amino acids (18-292a.a) and having a molecular mass of 57.2kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).IL17RB is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL17RB protein solution (0.25mg/ml) containing phosphate buffered saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.

    • Synonyms

      Interleukin 17 Receptor B, IL17RH1, IL17BR, Interleukin 17B Receptor, Cytokine, Receptor-Like 4, Interleukin-17B Receptor, IL-17 Receptor Homolog 1, IL-17 Receptor B, IL-17B Receptor, IL-17Rh1, IL-17RB, EVI27, CRL4, Interleukin 17 Receptor Homolog 1, Interleukin-17 Receptor B, Cytokine Receptor CRL4.

    • 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

      REPTVQCGSE TGPSPEWMLQ HDLIPGDLRD LRVEPVTTSV ATGDYSILMN VSWVLRADAS IRLLKATKIC VTGKSNFQSY SCVRCNYTEA FQTQTRPSGG KWTFSYIGFP VELNTVYFIG AHNIPNANMN EDGPSMSVNF TSPGCLDHIM KYKKKCVKAG SLWDPNITAC KKNEETVEVN FTTTPLGNRY MALIQHSTII GFSQVFEPHQ KKQTRASVVI PVTGDSEGAT VQLTPYFPTC GSDCIRHKGT VVLCPQTGVP FPLDNNKSKP GGWLPVEPKS CDKTHTCPPC PAPELLGGPS VFLFPPKPKD TLMISRTPEV TCVVVDVSHE DPEVKFNWYV DGVEVHNAKT KPREEQYNST YRVVSVLTVL HQDWLNGKEY KCKVSNKALP APIEKTISKA KGQPREPQVY TLPPSRDELT KNQVSLTCLV KGFYPSDIAV EWESNGQPEN NYKTTPPVLD SDGSFFLYSK LTVDKSRWQQ GNVFSCSVMH EALHNHYTQK SLSLSPGKHH HHHH.

    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.

    Il17Rb Human
  • View Data Sheet

    Description:

    Lymphotactin (XCL1) Rat Recombinant

    XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    Product # :

    CHM-038

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    Description

    Lymphotactin (XCL1) Rat Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of approximately 10.0kDa.Lymphotactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.

    More Info

    • Introduction

      XCL1 is a small cytokine belongs to the XC chemokine family that is also known as lymphotactin. XCL1 is found in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.

    • Synonyms

      XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized XCL1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Lymphotactin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.

    • Background

      What is the molecular weight/Mw of LYMPHOTACTIN RAT Protein?
      LYMPHOTACTIN RAT Protein has a total Mw of 10kDa.

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

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

      What is the Biological Activity of LYMPHOTACTIN RAT Protein?
      The ED50 as determined by a chemotaxis bioassay using human XCR1 transfected murine BaF3 cells < 100 ng/ml, corresponding to a specific activity of > 1.0 × 104 IU/mg.

      What is the amino acid sequence of LYMPHOTACTIN RAT Protein?
      VGTEVLQESI CVSLRTQRLP VQKIKTYTIK EGAMRAVIFV TKRGLRICAD PQAKWVKTAI KTVDGRASAS KSKAETIPTQ AQRSASTAVT LTG.

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

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

      Who supplies recombinant LYMPHOTACTIN 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 LYMPHOTACTIN 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.

    Lymphotactin Rat
  • View Data Sheet

    Description:

    Interleukin-34 Human Recombinant

    Interleukin 34, C16orf77, MGC34647, IL34

    Product # :

    CYT-1198

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    Description

    IL34 Human Recombinant produced in CHO cells is a glycosylated homodimeric polypeptide chain containing 228 amino acids and having a total molecular mass of 26kDa.IL34 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    Lyophilized from a sterile (0.2µ) filtered solution containing phosphate buffered saline (PBS).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.

    • Synonyms

      Interleukin 34, C16orf77, MGC34647, IL34

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL34 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL34 Human 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 IL34 in sterile water at a concentration of 0.1 mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      NEPLEMWPLT QNEECTVTGF LRDKLQYRSR LQYMKHYFPI NYKISVPYEG VFRIANVTRLQRAQVSEREL RYLWVLVSLS ATESVQDVLL EGHPSWKYLQ EVETLLLNVQ QGLTDVEVSPKVESVLSLLN APGPNLKLVR PKALLDNCFR VMELLYCSCC KQSSVLNWQD CEVPSPQSCSPEPSLQYAAT QLYPPPPWSP SSPPHSTGSV RPVRAQGEGL LPHHHHHH

    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 34 Human
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    Description:

    Interleukin-6 Human Recombinant, Sf9

    BSF2, HGF, HSF, IFNB2, IL-6.

    Product # :

    CYT-1150

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    • SDS-PAGE

    Description

    IL6 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 189 amino acids (30-212aa) and having a molecular mass of 21.6kDa.(Migrates at 18-28kDa on SDS-PAGE under reducing conditions).IL6 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL6 protein (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml . 

    SDS-PAGE

    More Info

    • Introduction

      Interleukin-6 or Il-6 is a cytokine with a large assortment of biological functions. IL-6 it has a crucial part in the last differentiation of b-cells into ig-secreting cells. This cytokine also induces myeloma and plasmacytoma growth. Interleukin-6 induces nerve cells differentiation, among hepatocytes it induces acute phase reactants.

    • Synonyms

      BSF2, HGF, HSF, IFNB2, IL-6.

    • 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

      VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
      LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
      LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

    • Background

      Production and Applications of Human Recombinant Interleukin-6 in Sf9 Cells

      Abstract:

      Interleukin-6 (IL-6) holds a central role in immune regulation, inflammation, and hematopoiesis. The production of Human Recombinant IL-6 using the Sf9 insect cell system presents a versatile approach for investigating its biological functions and potential therapeutic applications. This paper outlines the methodology of producing Human Recombinant IL-6 in Sf9 cells and explores its significance in immunological research and clinical studies.

      Introduction:

      IL-6 is a multifunctional cytokine pivotal in various physiological processes, making it a target of intensive research. The expression of Human Recombinant IL-6 facilitates investigations into its intricate mechanisms and offers potential avenues for therapeutic development. The Sf9 cell system, harnessed from Spodoptera frugiperda, enables efficient recombinant protein expression through baculovirus vectors.

      Methods:

      Production of Human Recombinant IL-6 involves cloning the human IL-6 gene into a baculovirus transfer vector, which is co-transfected with linearized baculovirus DNA into Sf9 cells. The resultant recombinant baculovirus generates and secretes IL-6 into the culture medium. Purification methods, such as chromatography, ensure the protein's quality and functionality.

      Applications:

      Human Recombinant IL-6 from Sf9 cells has broad applications. It serves as a critical tool for investigating IL-6's roles in immune responses, inflammation, and hematopoiesis. Additionally, it plays a crucial role in the development of therapies targeting IL-6-associated disorders like autoimmune diseases, chronic inflammatory conditions, and cancer.

      Sf9 Expression Advantages:

      The Sf9 system offers notable advantages, including post-translational modifications and protein folding, necessary for IL-6's biological activity. Sf9 cells provide a platform for generating properly folded and functional recombinant IL-6, reflecting its native structure and function.

      Challenges and Future Prospects:

      While Sf9-based expression of Human Recombinant IL-6 offers significant advantages, optimization of expression conditions and scale-up strategies remain challenges. Furthermore, the therapeutic potential of Human Recombinant IL-6 requires in-depth preclinical and clinical investigations.

      Conclusion:

      The production of Human Recombinant IL-6 in Sf9 cells through baculovirus expression offers a powerful tool to comprehend IL-6's multifaceted roles in health and disease. This technology is poised to expand our knowledge of IL-6-related conditions and catalyze the development of precision therapeutic interventions.

      What is the molecular weight/Mw of IL 6 HUMAN, SF9 Protein?
      IL 6 HUMAN, SF9 Protein has a total Mw of 21.6kDa.

      What is the source or expression system of IL 6 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL 6 HUMAN, SF9 Protein?
      IL 6 HUMAN, SF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 6 HUMAN, SF9 Protein?
      The ED50, determined by cell proliferation assay using TF-1 human erythroleukemic cell, is 0.2 - 0.8 ng/ml .

      What is the amino acid sequence of IL 6 HUMAN, SF9 Protein?
      VPPGEDSKDV AAPHRQPLTS SERIDKQIRY ILDGISALRK ETCNKSNMCE SSKEALAENN
      LNLPKMAEKD GCFQSGFNEE TCLVKIITGL LEFEVYLEYL QNRFESSEEQ ARAVQMSTKV
      LIQFLQKKAK NLDAITTPDP TTNASLLTKL QAQNQWLQDM TTHLILRSFK EFLQSSLRAL RQMHHHHHH.

      What applications can IL 6 HUMAN, SF9 Protein be used in?
      IL 6 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 6 HUMAN, SF9 Protein?
      The endotoxin level is minimal, IL 6 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 6 HUMAN, 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 IL 6 HUMAN, 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.

    Il6 Human
  • View Data Sheet

    Description:

    Interferon-Omega 1 Human Recombinant, HEK

    IFN omega-1, IFN alpha-II-1, IFNW1.

    Product # :

    CYT-1225

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    Description

    IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 is ≤0.07 ng/ml, measured  in a cytotoxicity assay using TF-1 human erythroleukemic cells .

    More Info

    • Synonyms

      IFN omega-1, IFN alpha-II-1, IFNW1.

    • 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

      LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

    • Background

      Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.

      Structural Insights into IFNW1:

      IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.

      Signaling Pathways and Antiviral Defense:

      IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.

      IFNW1 in Immunomodulation and Disease:

      Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.

      Therapeutic Potential and Future Prospects:

      The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.

      IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.

      What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
      IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.

      What is the source or expression system of IFNW1 HUMAN, HEK Protein?
      HEK293 Cells.

      What is the Purity of IFNW1 HUMAN, HEK Protein?
      IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
      The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

      What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
      LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

      What applications can IFNW1 HUMAN, HEK Protein be used in?
      IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
      The endotoxin level is minimal, IFNW1 HUMAN, HEK 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.

    Ifn Omega Human
  • View Data Sheet

    Description:

    Eotaxin-3 Human Recombinant (CCL26)

    C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.

    Product # :

    CHM-362

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    • SDS-PAGE

    Description

    Eotaxin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8.4kDa. The Eotaxin-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 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 BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.

    SDS-PAGE

    More Info

    • Introduction

      Eotaxin-3 (CCL26) is a small cytokine that belongs to the CC chemokine family also known as TARC (thymus and activation regulated chemokine). CCL26 is major eotaxin produced and released by alveolar epithelial cells which is involved in autoregulation of CCR3 receptors and other eotaxins. Eotaxin-3 is involved in immunoregulatory and inflammatory processes. Eotaxin-3 specifically binds and stimulates chemotaxis in T cells and elicits its effects by interacting with the chemokine receptor CCR4. CCL26 exhibits chemotactic activity for normal peripheral blood eosinophils and basophils. Eotaxin-3 may play a part in the eosinophil accumulation in atopic diseases. Eotaxin-3 is overexpressed in eosinophilic esophagitis, and the expression level correlates with disease severity. Eotaxin-3 is expressed constitutively in thymus, but only briefly in phytohemagglutinin-stimulated peripheral blood mononuclear cells. CCL26 is one of two Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 7.

    • Synonyms

      C-C motif chemokine 26, Small-inducible cytokine A26, Eotaxin-3, Macrophage inflammatory protein 4-alpha, MIP-4-alpha, Thymic stroma chemokine-1, TSC-1, CC chemokine IMAC, CCL26, SCYA26, IMAC, MIP-4a, MGC126714, MIP-4alpha.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL26 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 Eotaxin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.

    • Background

      What is the molecular weight/Mw of CCL26 HUMAN Protein?
      CCL26 HUMAN Protein has a total Mw of 8.4kDa.

      What is the source or expression system of CCL26 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL26 HUMAN Protein?
      CCL26 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL26 HUMAN Protein?
      Determined by its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect is typically 0.1-1.0 μg/ml.

      What is the amino acid sequence of CCL26 HUMAN Protein?
      TRGSDISKTC CFQYSHKPLP WTWVRSYEFT SNSCSQRAVI FTTKRGKKVC THPRKKWVQK YISLLKTPKQ L.

      What applications can CCL26 HUMAN Protein be used in?
      CCL26 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL26 HUMAN Protein?
      The endotoxin level is minimal, CCL26 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL26 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 CCL26 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.

    Eotaxin 3 Human
  • View Data Sheet

    Description:

    Interleukin-5 Mouse Recombinant, Sf9

    interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    Product # :

    CYT-1195

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    Description

    IL5 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 119 amino acids (21-133 a.a) and having a molecular mass of 13.9kDa.IL5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The IL5 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

    More Info

    • Introduction

      The protein encoded by this gene is a cytokine that acts as a growth and differentiation factor for both B cells and eosinophils. IL5is a main regulator of eosinopoiesis, eosinophil maturation and activation. The elevated production of IL5is reported to be related to asthma or hypereosinophilic syndromes. The receptor of IL5is a heterodimer, whose beta subunit is shared with the receptors for interleukine 3 (IL3) and colony stimulating factor 2 (CSF2/GM-CSF). IL5, together with those for interleukin 4 (IL4), interleukin 13 (IL13), and CSF2, form a cytokine gene cluster on chromosome 5. IL5, IL4, and IL13 are found to be regulated coordinately by long-range regulatory elements spread over 120 kilobases on chromosome 5q31.

    • Synonyms

      interleukin 5, Il, Il-5, B-cell growth factor II, BCGF-II, Cytotoxic T-lymphocyte inducer, Eosinophil differentiation factor, T-cell replacing factor, EDF, TRF, B cell differentiation factor I, IL5.

    • 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

      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH

    • Background

      What is the molecular weight/Mw of IL 5 MOUSE, SF9 Protein?
      IL 5 MOUSE, SF9 Protein has a total Mw of 13.9kDa.

      What is the source or expression system of IL 5 MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IL 5 MOUSE, SF9 Protein?
      IL 5 MOUSE, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 5 MOUSE, SF9 Protein?
      Measured in a cell proliferation assay using TF-1 human erythroleukemic cells. The ED50 range ≤ 1 ng/ml.

      What is the amino acid sequence of IL 5 MOUSE, SF9 Protein?
      MEIPMSTVVK ETLTQLSAHR ALLTSNETMR LPVPTHKNHQ LCIGEIFQGL DILKNQTVRG GTVEMLFQNL SLIKKYIDRQ KEKCGEERRR TRQFLDYLQE FLGVMSTEWA MEGHHHHHH.

      What applications can IL 5 MOUSE, SF9 Protein be used in?
      IL 5 MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 5 MOUSE, SF9 Protein?
      The endotoxin level is minimal, IL 5 MOUSE, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 5 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 IL 5 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.

    Il 5 Mouse
  • View Data Sheet

    Description:

    Thymus and Activation Regulated Chemokine (CCL17) Rhesus Macaque Recombinant

    C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    Product # :

    CHM-036

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    Description

    Thymus and Activation Regulated Chemokine (CCL17) Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 71 amino acid and having a molecular mass of approximately 8.1kDa.TRAC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM PB, 0.02 % Tween-20 and 300mM NaCl, pH 7.4.

    Purity

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

    Biological Activity

    Was determined by a chemotaxis bioassay using human T-lymphocytes and is 1.0-10 ng/ml.

    More Info

    • Introduction

      TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 is a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

    • Synonyms

      C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TRAC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymus and Activation Regulated Chemokine Rhesus Macaque should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      ARGTNVGREC CLKYFKGAIP LRKLKTWYQT SEDCSRDAIV FVTVQNKAIC SDPNDKKVKK ALKYLQSLER S.

    • Background

      What is the molecular weight/Mw of CCL17 RHESUS MACAQUE Protein?
      CCL17 RHESUS MACAQUE Protein has a total Mw of 8.1kDa.

      What is the source or expression system of CCL17 RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CCL17 RHESUS MACAQUE Protein?
      CCL17 RHESUS MACAQUE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL17 RHESUS MACAQUE Protein?
      Was determined by a chemotaxis bioassay using human T-lymphocytes and is 1.0-10 ng/ml.

      What is the amino acid sequence of CCL17 RHESUS MACAQUE Protein?
      ARGTNVGREC CLKYFKGAIP LRKLKTWYQT SEDCSRDAIV FVTVQNKAIC SDPNDKKVKK ALKYLQSLER S.

      What applications can CCL17 RHESUS MACAQUE Protein be used in?
      CCL17 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL17 RHESUS MACAQUE Protein?
      The endotoxin level is minimal, CCL17 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL17 RHESUS MACAQUE 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 CCL17 RHESUS MACAQUE?
      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.

    Tarc Monkey
  • View Data Sheet

    Description:

    Thymus & Activation Regulated Chemokine Human Recombinant (CCL17)

    C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    Product # :

    CHM-240

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    Description

    CCL17 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8 kDa. The TARC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (0.5mg/ml) solution containing 20mM PBS & 150mM 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-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

    • Synonyms

      C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TARC 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 CCL17 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
      AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS.

    • Background

      What is the molecular weight/Mw of CCL17 HUMAN Protein?
      CCL17 HUMAN Protein has a total Mw of 8kDa.

      What is the source or expression system of CCL17 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL17 HUMAN Protein?
      CCL17 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL17 HUMAN Protein?
      Determined by its ability to chemoattract human T-Lymphocytes using a concentration range of 1.0-10.0 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL17 HUMAN Protein?
      ARGTNVGRECCLEYFKGAIPLRKLKTWYQTSEDCSRD
      AIVFVTVQGRAICSDPNNK RVKNAVKYLQSLERS.

      What applications can CCL17 HUMAN Protein be used in?
      CCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL17 HUMAN Protein?
      The endotoxin level is minimal, CCL17 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL17 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 CCL17 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.

    Ccl17 Human
  • View Data Sheet

    Description:

    Thymic Stromal Lymphopoietin Receptor Human Recombinant

    CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    Product # :

    CYT-742

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    Description

    TSLPR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (23-231 a.a.) and having a molecular mass of 26.6kDa.TSLPR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TSLPR protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymic Stromal Lymphopoietin Receptor (TSLPR) is a member of the type I cytokine receptor family. TSLPR alongside the interleukin 7 receptor (IL7R) activate STAT3, STAT5, and JAK2 pathways, which is regulated processes such as cell proliferation and development of the hematopoietic system. Two transcript variants encoding dissimilar isoforms have been found for this gene. TSLPR is expressed in heart, skeletal muscle, kidney and adult and fetal liver.

    • Synonyms

      CRL2, CRLF2Y, Cytokine receptor-like factor 2, Cytokine receptor-like 2, IL-XR, ILXR.

    • 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 MGSQGGAAEG VQIQIIYFNL ETVQVTWNAS KYSRTNLTFH YRFNGDEAYD QCTNYLLQEG HTSGCLLDAE QRDDILYFSI RNGTHPVFTA SRWMVYYLKP SSPKHVRFSW HQDAVTVTCS DLSYGDLLYE VQYRSPFDTE WQSKQENTCN VTIEGLDAEK CYSFWVRVKA MEDVYGPDTY PSDWSEVTCW QRGEIRDACA ETPTPPKPKL SK.

    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.

    Tslpr Human
  • View Data Sheet

    Description:

    IL-6 Receptor Beta Mouse Recombinant

    IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.

    Product # :

    CYT-918

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    • SDS-PAGE

    Description

    IL6R produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 603 amino acids (23-617a.a.) and having a molecular mass of 67.7kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).IL6R is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    IL6R protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      The IL-6 receptor complex is composed of two membrane glycoproteins: the low affinity receptor and the signaltransducing component. The soluble form of IL6R is found in the urine of healthy adult humans and the serum of HIV positive individuals, as well as in the cell culture supernatants of stimulated PBMC’s. This soluble form of IL6R results from either proteolytic cleavage from the membrane, or an isoform derived splice variant.

    • Synonyms

      IL-6 receptor subunit beta, IL-6R subunit beta, IL-6R-beta, IL-6RB, Interleukin-6 signal transducer, Membrane glycoprotein 130, gp130, Oncostatin-M receptor subunit alpha,CD130.

    • 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

      QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.

    • Background

      Research Paper on IL-6 Receptor Beta Mouse Recombinant

      Abstract:

      The IL-6 Receptor Beta Mouse Recombinant stands as a pivotal player in deciphering the intricate realm of immune modulation. This research paper offers an in-depth exploration of its molecular intricacies and its profound implications in immunological research. By delving into its functions, synonyms including DIF, TNFA, and TNFSF2, and potential applications, we gain valuable insights into its role in shaping immune responses.

      Introduction:

      The IL-6 Receptor Beta Mouse Recombinant has emerged as a central focus in immunological investigations. This paper aims to provide a comprehensive understanding of its molecular attributes and its influence on immune mechanisms.

      Molecular Insights and Signaling Proficiency:

      Examining the molecular architecture of IL-6 Receptor Beta Mouse Recombinant, we uncover its critical role in transducing IL-6 signals. Its intricate interactions and signaling proficiency contribute to precise immune responses.

      Influencing Immune Responses:

      IL-6, a key cytokine, exerts remarkable effects on immune cell activation and inflammation. IL-6 Receptor Beta Mouse Recombinant serves as an essential component in the IL-6 signaling pathway, influencing immune outcomes.

      Synonyms and Network Connections:

      Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, deepens our comprehension of cytokine-mediated signaling networks. The intricate interplay between IL-6 Receptor Beta Mouse Recombinant and these molecules shapes immune dynamics.

      Potential Therapeutic and Research Applications:

      IL-6 Receptor Beta Mouse Recombinant transcends the boundaries of laboratory research. Its potential as a therapeutic target for immune-related disorders and its utility in deciphering immune responses offer promising avenues for clinical applications.

      Clinical Relevance and Future Prospects:

      The clinical relevance of IL-6 Receptor Beta Mouse Recombinant is highlighted by its role in diseases characterized by dysregulated IL-6 signaling. Exploring its therapeutic potential paves the way for novel strategies to modulate immune-related conditions.

      Conclusion:

      In the intricate tapestry of immunology, IL-6 Receptor Beta Mouse Recombinant emerges as a central player in orchestrating immune responses. Its molecular intricacies, pivotal functions, and potential therapeutic implications position it as a cornerstone in understanding immune regulation and developing innovative interventions.

      What is the molecular weight/Mw of IL6R MOUSE Protein?
      IL6R MOUSE Protein has a total Mw of 67.7kDa.

      What is the source or expression system of IL6R MOUSE Protein?
      Sf9, Insect cells.

      What is the Purity of IL6R MOUSE Protein?
      IL6R MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6R MOUSE Protein?
      QLLEPCGYIY PEFPVVQRGS NFTAICVLKE ACLQHYYVNA SYIVWKTNHA AVPREQVTVI NRTTSSVTFT DVVLPSVQLT CNILSFGQIE QNVYGVTMLS GFPPDKPTNL TCIVNEGKNM LCQWDPGRET YLETNYTLKS EWATEKFPDC QSKHGTSCMV SYMPTYYVNI EVWVEAENAL GKVSSESINF DPVDKVKPTP PYNLSVTNSE ELSSILKLSW VSSGLGGLLD LKSDIQYRTK DASTWIQVPL EDTMSPRTSF TVQDLKPFTE YVFRIRSIKD SGKGYWSDWS EEASGTTYED RPSRPPSFWY KTNPSHGQEY RSVRLIWKAL PLSEANGKIL DYEVILTQSK SVSQTYTVTG TELTVNLTND RYVASLAARN KVGKSAAAVL TIPSPHVTAA YSVVNLKAFP KDNLLWVEWT PPPKPVSKYI LEWCVLSENA PCVEDWQQED ATVNRTHLRG RLLESKCYQI TVTPVFATGP GGSESLKAYL KQAAPARGPT VRTKKVGKNE AVLAWDQIPV DDQNGFIRNY SISYRTSVGK EMVVHVDSSH TEYTLSSLSS DTLYMVRMAA YTDEGGKDGP EFTFTTPKFA QGEIELEHHH HHH.

      What is the amino acid sequence of IL6R MOUSE Protein?
      IL6R MOUSE Protein is composed from XX amino acids.

      What applications can IL6R MOUSE Protein be used in?
      IL6R MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6R MOUSE Protein?
      The endotoxin level is minimal, IL6R MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6R MOUSE 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 IL6R MOUSE?
      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.

    Il6R Mouse
  • View Data Sheet

    Description:

    CX9C Motif Containing 4 Human Recombinant

    C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.

    Product # :

    PRO-1769

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    Description

    CMC4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-68 a.a) and having a molecular mass of 10.4kDa.CMC4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CMC4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CMC4 is a downstream 8kDa protein restricts to mitochondria which was identified by participation in some t(X;14) translocations related with mature T-cell proliferations. This region has a compound gene structure, with a common promoter and 5’ exon spliced to two different groups of 3’ exons which encode 2 separate proteins.

    • Synonyms

      C-X(9)-C Motif Containing 4, C-X(9)-C Motif Containing 4 Homolog, Mature T-Cell Proliferation 1 Neighbor Protein, MTCP1NB, MTCP1, Mature T-Cell Proliferation-1 Type A, Protein P8 MTCP-1, p8MTCP1, MTCP-1 Type A, C6.1B.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFMPQKD PCQKQACEIQ KCLQANSYME SKCQAVIQEL RKCCAQYPKG RSVVCSGFEK EEEENLTRKS ASK

    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.

    Cmc4 Human
  • View Data Sheet

    Description:

    CTACK Human Recombinant (CCL27)

    ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    Product # :

    CHM-373

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    • SDS-PAGE

    Description

    CTACK Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 89 amino acids (25-112 a.a.) and having a molecular mass of 10.3kDa. CTACK protein is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CTACK Human solution containing 10mM sodium citrate pH-3.5 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      ALP, CTACK, ESKINE, ILC, PESKY, SCYA27, CCL27, C-C motif chemokine 27, Small-inducible cytokine A27, IL-11 R-alpha-locus chemokine, Skinkine, ESkine, Cutaneous T-cell-attracting chemokine.

    • 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

      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

    • Background

      What is the molecular weight/Mw of CTACK HUMAN Protein?
      CTACK HUMAN Protein has a total Mw of 10.3kDa.

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

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

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

      What is the amino acid sequence of CTACK HUMAN Protein?
      MFLLPPSTAC CTQLYRKPLS DKLLRKVIQV ELQEADGDCH LQAFVLHLAQ RSICIHPQNP SLSQWFEHQE RKLHGTLPKL NFGMLRKMG.

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

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

      Who supplies recombinant CTACK 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 CTACK 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.

    Ctack Human
  • View Data Sheet

    Description:

    Eotaxin-2 Rat Recombinant (CCL24)

    C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    Product # :

    CHM-282

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    Description

    CCL24 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids and having a molecular mass of 10.2kDa. The CCL24 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 murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

    More Info

    • Introduction

      Eotaxin-2, also called MPIF2 & Ckb6, is a novel CC chemokine produced by activated monocytes and T lymphocytes. Eotaxin-2 selectively chemoattracts cells expressing CCR3 including eosinophils, basophils, Th2 T cells, mast cells, and certain subsets of dendritic cells. Furthermore, Eotaxin-2 inhibits the proliferation of multipotential hematopoietic progenitor cells. The mature protein, which includes C-terminal truncation, contains 78 amino acids (92 amino acids for the mouse homolog, without C-terminal truncation).
      CCL24 functions as a chemotactic chemokine for resting t-lymphocytes, and eosinophils. CCL24 has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. CCL24 is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line and binds to CCR3.

    • Synonyms

      C-C motif chemokine 24, Small-inducible cytokine A24, Myeloid progenitor inhibitory factor 2, CK-beta-6, Eosinophil chemotactic protein 2, Eotaxin-2, CCL24, Ckb-6, MPIF2, MPIF-2, SCYA24, Eotaxin2, CCL-24.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL24 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 CCL24 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

    • Background

      What is the molecular weight/Mw of CCL24 RAT Protein?
      CCL24 RAT Protein has a total Mw of 10.2kDa.

      What is the source or expression system of CCL24 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL24 RAT Protein?
      CCL24 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL24 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

      What is the amino acid sequence of CCL24 RAT Protein?
      VTIPSSCCVT FISKKIPVNR VISYQLANGS ICPKAGVIFI TKKGHKICTD PKLPWVQKHI KNLDAKRNQP SEGAKALGPK FVIQKLRGNS TKV.

      What applications can CCL24 RAT Protein be used in?
      CCL24 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL24 RAT Protein?
      The endotoxin level is minimal, CCL24 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL24 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 CCL24 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.

    Eotaxin 2 Rat
  • View Data Sheet

    Description:

    Monocyte Chemotactic Protein-3 Human Recombinant (CCL7)

    Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    Product # :

    CHM-317

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    Description

    Monocyte Chemotactic Protein-3 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 76 amino acids and having a molecular mass of 9011 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

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

    Biological Activity

    The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).

    • Synonyms

      Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 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-3in 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 Gln-Pro-Val-Gly-Ile.

    • Background

      What is the molecular weight/Mw of CCL7 HUMAN Protein?
      CCL7 HUMAN Protein has a total Mw of 9.01kDa.

      What is the source or expression system of CCL7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL7 HUMAN Protein?
      CCL7 HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL7 HUMAN Protein?
      The specific activity as determined by the ability of MCP-3 to chemoattract human peripheral blood at 8 - 80ng/ml corresponding to a Specific Activity of 12,500-125,000IU/mg.

      What is the amino acid sequence of CCL7 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gln-Pro-Val-Gly-Ile.

      What applications can CCL7 HUMAN Protein be used in?
      CCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL7 HUMAN Protein?
      The endotoxin level is minimal, CCL7 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL7 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 CCL7 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 3 Human
  • View Data Sheet

    Description:

    RELM-Beta Mouse Recombinant

    Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    Product # :

    CYT-413

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    Description

    Mouse RELM-b Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 83 amino acids and having a molecular mass of 8.9kDa. The Mouse RETNLB is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) protein solution containing 10mM Acetic Acid with 2:1 mannitol to protein.

    Purity

    Greater than 97% as determined by SDS-PAGE.

    More Info

    • Introduction

      RELM-beta (Resistin-Like Molecule-beta) is a member of a recently identified family of secreted proteins containing a conserved cystein-rich C-terminus. The RELM family consists of resistin (also called FIZZ3), RELM-alfa (FIZZ1), RELM-beta (FIZZ2) and RELM-gamma. Only resisistin and RELM-beta were found in humans whereas all four RELM family members were identified in rodents.
      RELM-beta appears to be produced as a homodimer exclusively by intestinal goblet cells and can be found in high quantities in stool. Remarkably, stool of germ-free mice displaying sterile intestinal tract does not contain RELM-beta until bacterial colonization takes place after pathogen-free mice entered natural environment. Some, but not all, colon carcinoma cell lines secrete RELM-beta into the cell culture supernatant.
      The physiological function of RELM-beta is not known. High doses of recombinant RELM-beta showed hyperglycemic effects including lowered glucose disposal and increased hepatic glucose production in mice.

    • Synonyms

      Resistin-like beta, RELM beta, Cysteine-rich secreted protein FIZZ2, Colon and small intestine-specific cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 1, Colon carcinoma-related gene protein, RELM-b, XCP2, HXCP2.

    • Physical Appearance

      Brownish lyophilized powder.

    • Stability

      Lyophilized RETNLB is stable at -20°C. After reconstitution the protein should be kept at all times at -20°C. It is recommended to add a carrier protein (0.1% HSA or BSA) for long term storage.

    • Solubility

      Reconstitute at 0.1 mg/ml with sterile pyrogen free water.

    • Amino Acid Sequence

      MQCSFESLVD QRIKEALSRQ EPKTISCTSV TSSGRLASCP AGMVVTGCAC GYGCGSWDIR NGNTCHCQCS VMDWASARCC RMA.

    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.

    Relm Beta Mouse
  • View Data Sheet

    Description:

    SNF8, ESCRT-II Complex Subunit Human Recombinant

    SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    Product # :

    PRO-1135

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    Description

    SNF8 Human Recombinant produced in E. coli is a single polypeptide chain containing 282 amino acids (1-258) and having a molecular mass of 31.4 kDa.SNF8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SNF8 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SNF8 belongs to the SNF8 family of vacuolar sorting proteins and is restricts to both the nucleus and the cytoplasm. SNF8 is a subunit of the endosomal sorting complex essential for transport II (ESCRT-II), which is necessary for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway facilitates transfer of transmembrane proteins into the lumen of the lysosome for degradation. Additionally, the ESCRT-II complex takes part in transcription regulation by contributing to derepression of transcription by RNA polymerase II, probably by its interface with ELL.

    • Synonyms

      SNF8 ESCRT-II complex subunit homolog (S. cerevisiae), ESCRT-II complex subunit VPS22, ELL-associated protein of 30 kDa, EAP30 subunit of ELL complex, vacuolar-sorting protein SNF8, EAP30, VPS22, Dot3.

    • 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 MGSHMHRRGV GAGAIAKKKL AEAKYKERGT VLAEDQLAQM SKQLDMFKTN LEEFASKHKQ EIRKNPEFRV QFQDMCATIG VDPLASGKGF WSEMLGVGDF YYELGVQIIE VCLALKHRNG GLITLEELHQ QVLKGRGKFA QDVSQDDLIR AIKKLKALGT GFGIIPVGGT YLIQSVPAEL NMDHTVVLQL AEKNGYVTVS EIKASLKWET ERARQVLEHL LKEGLAWLDL QAPGEAHYWL PALFTDLYSQ EITAEEAREA LP

    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.

    Snf8 Human
  • View Data Sheet

    Description:

    Interferon Alpha And Beta Receptor Subunit 2 Human Recombinant

    Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.

    Product # :

    CYT-1167

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    • SDS-PAGE

    Description

    IFNAR2 Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 456 amino acids (27-243 a.a.) and having a molecular mass of 51.7kDa. IFNAR2 is fused to an 239 amino acid hIgG-His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IFNAR2 protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.

    SDS-PAGE

    More Info

    • Introduction

      Interferon Alpha and Beta Receptor Subunit 2 or IFNAR2 is a protein, part of the class II cytokine receptor family. When different innate immune signaling transduction are activated, there is a rapid induction of type I IFNs because it has an intronless gene source. IFNAR2 is the main ligand and binds to the receptor. Once bind, stabilization occurs and a signaling compelx recptor is formed. IFNAR2 also takes part in the activation process of STAT proteins.

    • Synonyms

      Interferon alpha/beta receptor 2, IFNAR2, IFN-alpha binding protein, Interferon alpha binding protein, Type I interferon receptor 2, interferon alpha/beta receptor 2 isoform a, IFN-R-2, IFNABR, IFNARB, IFN-alpha-REC, IFN-R, IMD45.

    • 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

      ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.

    • Background

      What is the molecular weight/Mw of IFNAR2 HUMAN Protein?
      IFNAR2 HUMAN Protein has a total Mw of 51.7kDa.

      What is the source or expression system of IFNAR2 HUMAN Protein?
      Sf9, Baculovirus cells.

      What is the Purity of IFNAR2 HUMAN Protein?
      IFNAR2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNAR2 HUMAN Protein?
      The ED50 range ≤ 500 ng/ml and is measured by its binding ability in a functional ELISA with Human IFN-alpha 2 in the presence of Human IFN-alpha/beta R1.

      What is the amino acid sequence of IFNAR2 HUMAN Protein?
      ISYDSPDYTD ESCTFKISLR NFRSILSWEL KNHSIVPTHY TLLYTIMSKP EDLKVVKNCA NTTRSFCDLT DEWRSTHEAY VTVLEGFSGN TTLFSCSHNF WLAIDMSFEP PEFEIVGFTN HINVMVKFPS IVEEELQFDL SLVIEEQSEG IVKKHKPEIK GNMSGNFTYI IDKLIPNTNY CVSVYLEHSD EQAVIKSPLK CTLLPPGQES ESAESAKLEP KSCDKTHTCP PCPAPELLGG PSVFLFPPKP KDTLMISRTP EVTCVVVDVS HEDPEVKFNW YVDGVEVHNA KTKPREEQYN STYRVVSVLT VLHQDWLNGK EYKCKVSNKA LPAPIEKTIS KAKGQPREPQ VYTLPPSRDE LTKNQVSLTC LVKGFYPSDI AVEWESNGQP ENNYKTTPPV LDSDGSFFLY SKLTVDKSRW QQGNVFSCSV MHEALHNHYT QKSLSLSPGK HHHHHH.
      What applications can IFNAR2 HUMAN Protein be used in?
      IFNAR2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNAR2 HUMAN Protein?
      The endotoxin level is minimal, IFNAR2 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.

    Ifnar2 Human
  • View Data Sheet

    Description:

    Interleukin-17A/F Heterodimer Human Recombinant

    IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

    Product # :

    CYT-623

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    Description

    IL-17A/F Human Recombinant produced in E.Coli is a heterodimeric, non-glycosylated polypeptide chain containing 1 monomeric subunit of each IL-17A & IL-17F. The active dimer contains 271 amino acids and having a total molecular mass of 30.7 kDa. The IL-17A/F Human is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-17A/F was lyophilized from a (0.2µm) filtered protein solution containing 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity as determined by production of IL-6 from mouse 3T3 cells is 3.2ng/ml (3.1x105units/mg).

    More Info

    • Introduction

      Human IL-17A/F is a 40kDa glycoprotein which is secreted as a disulfide-linked heterodimer. IL-17A/F consists of two proteins of the IL-17 family, IL-17A and IL17F. Proteins of the 6 homodimeric IL17 family show a cysteine knot motif that contains two disulfide-bonds. Human IL17A is produced as a 155 a.a precursor that includes a 23 amino acids signal sequence and a 132 amino acid chain that includes an N-linked glycosylation site. Human IL17F is produced as a 153 amino acid precursor with a 20 amino acid signal sequence and a 133 amino acid region. Similar to IL17A, IL17F also has an N-linked glycosylation site. Both proteins (IL17A & IL17F) share 50% amino acid sequence identity. Human IL17A & IL17F show approximately 60% homology in their amino acid sequence to mouse IL-17A and IL-17F. Interleukin-17A/F and IL17A, IL17F homodimers are manufactured by activted CD4+ T cells, called Th17. IL-23 causes Th17 lymphocytes to manufacture IL-17A/F. IL17RA and IL17RC form a heterodimer for the binding of IL17A and IL17F. IL-17A/F binds IL-17RA. Interleukin-17A/F induces chemokine production and airway neutrophilia with intermediate potency between IL17A (most potent) and IL17F (least potent).

    • Synonyms

      IL17A/F, IL17 A/F, IL-17A/F, IL-17 A/F, IL17AF, IL-17 AF, Interleukin-17 A/F, Interleukin-17 AF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human IL-17A/F although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human IL-17A/F 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 Human IL-17A/F in sterile water at 0.1mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MIVKAGITIP RNPGCPNSED KNFPRTVMVN LNIHNRNTNT NPKRSSDYYN RSTSPWNLHR NEDPERYPSV IWEAKCRHLG CINADGNVDY HMNSVPIQQE ILVLRREPPH CPNSFRLEKI LVSVGCTCVT PIVHHVA.

      MRKIPKVGHT FFQKPESCPP VPGGSMKLDI GIINENQRVS MSRNIESRST SPWNYTVTWD PNRYPSEVVQ AQCRNLGCIN AQGKEDISMN SVPIQQETLV VRRKHQGCSV SFQLEKVLVT VGCTCVTPVI HHVQ.

    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 17 A F Human
  • View Data Sheet

    Description:

    Interleukin-2 Human Recombinant

    T-cell growth factor (TCGF), Lymphokine, IL-2.

    Product # :

    CYT-209

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    Description

    Interleukin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 15.4kDa. The IL-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2μm filtered concentrated solution (1.0mg/ml) in PBS, pH 5.0.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

    More Info

    • Introduction

      IL2 is a secreted cytokine that is important for the proliferation of T and B lymphocytes. The receptor of this cytokine is a heterotrimeric protein complex whose gamma chain is also shared by interleukin 4 (IL4) and interleukin 7 (IL7). The expression of this gene in mature thymocytes is monoallelic, which represents an unusual regulatory mode for controlling the precise expression of a single gene. The targeted disruption of a similar gene in mice leads to ulcerative colitis-like disease, which suggests an essential role of this gene in the immune response to antigenic stimuli.

    • Synonyms

      T-cell growth factor (TCGF), Lymphokine, IL-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL2 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-2 in sterile distilled water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

    • Background

      IL 2 HUMAN: A Vital Tool for Advancing Immunotherapy Research

      IL 2 HUMAN refers to the human form of Interleukin-2, a critical cytokine in the immune system. This protein is crucial for the growth and activity of T and B lymphocytes, the cells responsible for the body's immune defense against infections.

      By promoting the growth of these cells, IL 2 plays a vital role in maintaining and activating the immune response.

      Production and Characteristics

      Typically, IL 2 is produced through recombinant DNA technology using E. coli bacteria. This method allows for creating large quantities of pure and functional IL 2 protein.

      The product appears as a sterile, white lyophilized powder that is non-glycosylated and consists of 133 amino acids with a molecular mass of approximately 15.4 kDa.

      Reconstituting IL-2 Human for Laboratory Use

      To dissolve the lyophilized IL-2 effectively, it should be reconstituted with sterile distilled water to achieve a minimum 100µg/ml concentration. This makes the protein readily usable for further experimental procedures.

      Moreover, the concentration allows for easy adjustment in solubility and ensures optimal conditions for the protein's activity in various research setups. Proper dissolution and storage are crucial to maintain the protein's functionality and stability.

      Storage and Stability

      The stability of IL 2 is dependent on its storage conditions. When lyophilized, it can remain stable at room temperature for up to three weeks, but for long-term storage, it should be kept desiccated below -18°C.

      Once reconstituted, IL 2 should be used within a week if kept at 4°C, or it can be stored at below -18°C for future use. It's important to avoid freeze-thaw cycles, which can degrade the protein.

      Purity and Biological Activity

      IL 2 HUMAN's purity is generally greater than 97%, confirmed by reverse-phase high-performance liquid chromatography (RP-HPLC) and SDS-PAGE analyses.

      Its biological activity is evaluated by its ability to stimulate the proliferation of murine CTLL-2 cells, with an effective dose (ED50) typically less than 0.1 ng/ml. This indicates a very high specific activity, making it highly potent and effective in research settings.

      Applications in Research

      IL 2 is used extensively in research, particularly in studies focusing on the immune system, autoimmune diseases, and cancer. Furthermore, its role in T-cell growth and function makes it invaluable for developing new therapeutic strategies and understanding immune response mechanisms.

      Important Considerations

      It is important to remember that IL 2, like all cytokines used in research, is intended for laboratory use only. This protein is not suitable for drug, food, or cosmetic applications. Proper handling and usage instructions must be followed to ensure safety and efficacy in research environments.

      Essentially, IL 2 HUMAN is a vital tool in immunological research, offering insights into the complex workings of the immune system and providing avenues for potential therapeutic developments. The careful production, handling, and storage of IL 2 are crucial for its effective use in laboratory settings.

      What is the molecular weight/Mw of IL 2 HUMAN Protein?
      IL 2 HUMAN Protein has a total Mw of 15.4kDa.

      What is the source or expression system of IL 2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL 2 HUMAN Protein?
      IL 2 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL 2 HUMAN Protein?
      The ED50 as determined by the dose-dependent stimulation of murine CTLL-2 cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 1x107IU/mg.

      What is the amino acid sequence of IL 2 HUMAN Protein?
      APTSSSTKK TQLQLEHLLL DLQMILNGIN NYKNPKLTRM LTFKFYMPKK ATELKHLQCL EEELKPLEEV LNLAQSKNFH LRPRDLISNI NVIVLELKGS ETTFMCEYAD ETATIVEFLN RWITFCQSII STLT.

      What applications can IL 2 HUMAN Protein be used in?
      IL 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL 2 HUMAN Protein?
      The endotoxin level is minimal, IL 2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL 2 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 IL 2 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.

    Il 2 Human