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Search results

1000 results found for “haptoglobin”

Name

Description

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  • View Data Sheet

    Name :

    MIP 1a Human

    Description:

    Macrophage Inflammatory Protein-1 Alpha Human Recombinant (CCL3)

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

    Product # :

    CHM-233

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    Macrophage Inflammatory Protein-1 alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 7820 Dalton. The MIP-1a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 0.55 mg/ml 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 Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Macrophage Inflammatory Proteins (MIP) belong to the family of chemotactic cytokines known as chemokines. In humans, there are two major forms, MIP-1a and MIP-1b that are now officially named CCL3 and CCL4 respectively. Both are major factors produced by macrophages after they are stimulated with bacterial endotoxins. They activate human granulocytes (neutrophils, eosinophilsand 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 White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

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

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

      What is the Purity of MIP 1A HUMAN Protein?
      MIP 1A HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of MIP 1A HUMAN Protein?
      The Activity is calculated by the ability of chemo-attraction of Human monocytes using 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

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

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

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


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

    Mip 1A Human
  • View Data Sheet

    Name :

    MIP 1a Mouse

    Description:

    Macrophage Inflammatory Protein-1 Alpha Mouse Recombinant (CCL3)

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

    Product # :

    CHM-320

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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



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

    Mip 1A Mouse
  • View Data Sheet

    Name :

    S100b Mouse, His

    Description:

    S100 Calcium Binding Protein B Mouse Recombinant, His Tag

    Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    Product # :

    PRO-853

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    S100B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-112 a.a.) and having a molecular mass of 12.8 kDa. The Mouse S100B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100B Mouse solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100B faintly binds calcium but binds zinc extremely strongly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. S100B binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction participates in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

    • Synonyms

      Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    • 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 MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVAM VTTACHEFFE HE.

    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.

    S100B Mouse
  • View Data Sheet

    Name :

    CCL20 Human

    Description:

    Macrophage Inflammatory Protein-3 alpha Human Recombinant (CCL20)

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

    Product # :

    CHM-351

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    MIP-3 Alpha Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 70 amino acids and having a molecular mass of 8 kDa. The MIP-3a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract human T lymphocytes using a concentration range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

    More Info

    • Introduction

      CCL-20 is a chemotactic factor that draws lymphocytes & neutrophils, rathar than monocytes. MIP-3 alpha inhibits proliferation of myeloid progenitors in colony formation assays. MIP3A plays a role in the formation and function of the mucosal lymphoid tissues by attracting lymphocytes and dendritic cells towards epithelial cells. C-terminal processed forms have been shown to be equally chemotactically active for leukocytes. CCL-20 holdes antibacterial activity e.coli atcc 25922 and s.aureus atcc 29213. CCL-20 gene transcription is activated by H. pylori, which activates NF-kappaB through intracellular signal pathway which involves IkappaB kinase and NF-kappaB-inducing kinase. MIP-3 alpha is invloved in chemokine-mediated lymphocyte trafficking during gastric inflammation in Helicobacter infection. CCL-20 expression is involved in the recruitment of CD45R0-positive T cell subsets into the intestinal lamina propria.
      MIP-3A is in charge of the advancement of pulpal inflammation through the recruitment of C-C motif Receptor 6-expressing lymphocytes Vaginal epithelial cells respond to factors present in semen by secreting MIP-3 alpha, which increases langerhans cells recruitment during HIV transmission.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-3a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL20 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      ASNFDCCLGY TDRILHPKFI VGFTRQLANE GCDINAIIFH TKKKLSVCAN PKQTWVKYIV RLLSKKVKNM.

    • Background

      What is the molecular weight/Mw of CCL20 HUMAN Protein?
      CCL20 HUMAN Protein has a total Mw of 8kDa.

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

      What is the Purity of CCL20 HUMAN Protein?
      CCL20 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL20 HUMAN Protein?
      Determined by its ability to chemoattract human T lymphocytes using a concentration range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

      What is the amino acid sequence of CCL20 HUMAN Protein?
      ASNFDCCLGY TDRILHPKFI VGFTRQLANE GCDINAIIFH TKKKLSVCAN PKQTWVKYIV RLLSKKVKNM.

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

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


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

    Mip 3A Human
  • View Data Sheet

    Name :

    CTGF Human

    Description:

    Connective Tissue Growth Factor Human Recombinant

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    Product # :

    CYT-541

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    Description

    CTGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 98 amino acids and having a molecular mass of 11.2 kDa. The CTGF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CTGF was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Purity of CTGF is greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

    More Info

    • Introduction

      Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane.
      CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
      Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
      The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the IGFBPs.
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
      Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to binding motifs are also found within this domain.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
      In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
      CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

    • Background

      Title: Connective Tissue Growth Factor Human Recombinant: Insights into Production, Function, and Therapeutic Potential

      Abstract:


      Connective tissue growth factor (CTGF) is a multifunctional protein that plays a critical role in tissue homeostasis and repair. This research paper provides a comprehensive analysis of human recombinant CTGF, focusing on its production, characterization, and potential therapeutic applications. The paper discusses the significance of CTGF in connective tissue development, fibrosis, and wound healing. Furthermore, it explores the ongoing research and clinical trials investigating the therapeutic potential of recombinant CTGF in various pathological conditions. The information presented in this paper aims to deepen our understanding of human recombinant CTGF and its utility as a research tool and a potential therapeutic agent.

      Introduction:


      Connective tissue growth factor (CTGF) is a secreted protein that belongs to the CCN (Cyr61, CTGF, Nov) family. It is involved in diverse cellular processes, including cell proliferation, extracellular matrix synthesis, and angiogenesis. Human recombinant CTGF, produced through genetic engineering techniques, enables researchers to study its biological functions and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CTGF is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and biological activity of the recombinant CTGF.

      Role in Tissue Homeostasis and Repair:


      CTGF plays a critical role in connective tissue development, maintenance, and repair. It promotes the synthesis of extracellular matrix components, such as collagen and fibronectin, and regulates the activity of various growth factors. CTGF is also involved in wound healing and tissue remodeling processes. Understanding the molecular mechanisms underlying CTGF-mediated tissue repair provides insights into potential therapeutic interventions.

      Therapeutic Implications:


      The dysregulation of CTGF expression and signaling has been implicated in several pathological conditions, including fibrosis, arthritis, and cancer. Recombinant CTGF holds promise as a potential therapeutic agent for these diseases. Preclinical and clinical studies are being conducted to evaluate the safety and efficacy of CTGF-based therapies, such as CTGF-targeting antibodies and small-molecule inhibitors.

      Conclusion:


      Human recombinant CTGF is a valuable research tool and a potential therapeutic target in various pathological conditions. Its production, characterization, and applications in connective tissue biology contribute to our understanding of tissue repair mechanisms and the development of novel therapeutic strategies. Continued research and clinical trials exploring the therapeutic potential of recombinant CTGF offer promising avenues for improving patient outcomes.

      What is the molecular weight/Mw of CTGF Protein?
      CTGF Protein has a total Mw of 11.2kDa.

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

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

      What is the Biological Activity of CTGF Protein?
      Determined by the dose-dependent stimulation of the proliferation of HUVEC cells. The expected ED50 for this effect is 1-2µg/ml, corresponding to a specific activity of 500-1000units/mg.

      What is the amino acid sequence of CTGF Protein?
      MGKKCIRTPK ISKPIKFELS GCTSMKTYRA KFCGVCTDGR CCTPHRTTTL PVEFKCPDGE VMKKNMMFIK TCACHYNCPG DNDIFESLYY RKMYGDMA.

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

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

    Ctgf Human
  • View Data Sheet

    Name :

    CTLA 4 Human

    Description:

    Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant

    GSE, CD152, IDDM12, CELIAC3, CTLA-4.

    Product # :

    CYT-366

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    Description

    CTLA 4 Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (36-161) and having a molecular mass of 15.9 kDa.CTLA 4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTLA 4 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    CTLA4-sds-page - Product image 1

    More Info

    • Introduction

      CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

    • Synonyms

      GSE, CD152, IDDM12, CELIAC3, CTLA-4.

    • 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 MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.

    • Background

      Title: Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant: A Potential Immunotherapeutic Target

      Abstract:


      Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a key immune checkpoint receptor that plays a crucial role in regulating T-cell responses. This research paper provides an in-depth analysis of human recombinant CTLA-4, focusing on its production, characterization, and potential applications in immunotherapy. The paper discusses the significance of CTLA-4 in immune regulation, tumor immunity, and autoimmune diseases. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CTLA-4 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Cytotoxic T-lymphocyte associated antigen-4 (CTLA-4) is a cell surface receptor primarily expressed on T-cells. It functions as a negative regulator of T-cell activation, dampening immune responses to prevent excessive inflammation. Human recombinant CTLA-4, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological functions and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CTLA-4 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CTLA-4.

      Role in Immune Regulation:


      CTLA-4 plays a critical role in immune regulation by downregulating T-cell activation and suppressing immune responses. It competes with the co-stimulatory receptor CD28 for binding to its ligands, CD80 and CD86, on antigen-presenting cells. This interaction inhibits T-cell activation and promotes immune tolerance. Recombinant CTLA-4 serves as a valuable tool for studying immune checkpoint mechanisms and their impact on immune responses.

      Therapeutic Implications:


      The blockade of CTLA-4 has emerged as a promising immunotherapeutic strategy in cancer treatment. Monoclonal antibodies targeting CTLA-4, such as ipilimumab, have shown significant clinical efficacy in enhancing anti-tumor immune responses. Recombinant CTLA-4-based therapies, including fusion proteins and engineered T-cell receptors, are being explored as potential immunotherapeutic interventions. Additionally, CTLA-4 plays a role in autoimmune diseases, making it a potential target for the development of novel treatments.

      Conclusion:


      Human recombinant CTLA-4 is a valuable research tool and a potential immunotherapeutic target. Its production, characterization, and applications in immune regulation contribute to our understanding of T-cell biology and the development of novel immunotherapies. Continued research and clinical trials investigating the therapeutic potential of recombinant CTLA-4 offer promising prospects for improving outcomes in cancer and autoimmune diseases.

      What is the molecular weight/Mw of CTLA4 Protein?
      CTLA4 Protein has a total Mw of 15.9kDa.

      What is the source or expression system of CTLA4 Protein?
      Escherichia Coli.

      What is the Purity of CTLA4 Protein?
      CTLA4 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTLA4 Protein?
      The biological functionality of CTLA4 Protein will be determined in the future.

      What is the amino acid sequence of CTLA4 Protein?
      MGSSHHHHHH SSGLVPRGSH MGSKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSD.

      What applications can CTLA4 Protein be used in?
      CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTLA4 Protein?
      The endotoxin level is minimal, CTLA4 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.

    Ctla 4 Human
  • View Data Sheet

    Name :

    CTLA4 Human, Sf9

    Description:

    Cytotoxic T-Lymphocyte Associated Antigen-4 Human Recombinant, Sf9

    Cytotoxic T-Lymphocyte Associated Protein 4, Cytotoxic T-Lymphocyte-Associated Protein 4, Insulin-Dependent Diabetes Mellitus 12, Celiac Disease 3, CTLA-4, CD152, Ligand And Transmembrane Spliced Cytotoxic T Lymphocyte Associated Antigen 4, Cytotoxic T Lymphocyte Associated Antigen 4 Short Spliced Form, Cytotoxic T-Lymphocyte-Associated Serine Esterase-4, Cytotoxic T-Lymphocyte-Associated Antigen 4, CD152 Isoform, CD152 Antigen, CELIAC3, IDDM12, ALPS5, GRD4, GSE, CD, Cytotoxic T-lymphocyte protein 4, CTLA4.

    Product # :

    CYT-952

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    • sds-page

    Description

    CTLA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 135 amino acids (36-161a.a.) and having a molecular mass of 14.6kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). CTLA4 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTLA4 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Determined by IL-2 ELISA via Jurkat human acute T cell leukemia cells. The ED50 range ≤ 150 ng/ml with Human B7-1/CD80.

    sds-page

    CTLA4-sds-page - Product image 1

    More Info

    • Introduction

      CTLA-4 is a member of the immunoglobulin superfamily and encodes a protein which transmits an inhibitory signal to T cells. The protein contains a V domain, a transmembrane domain, and a cytoplasmic tail. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. The membrane-bound isoform functions as a homodimer interconnected by a disulfide bond, while the soluble isoform functions as a monomer. Mutations in this gene have been associated with insulin-dependent diabetes mellitus, Graves disease, Hashimoto thyroiditis, celiac disease, systemic lupus erythematosus, thyroid-associated orbitopathy, and other autoimmune diseases.

    • Synonyms

      Cytotoxic T-Lymphocyte Associated Protein 4, Cytotoxic T-Lymphocyte-Associated Protein 4, Insulin-Dependent Diabetes Mellitus 12, Celiac Disease 3, CTLA-4, CD152, Ligand And Transmembrane Spliced Cytotoxic T Lymphocyte Associated Antigen 4, Cytotoxic T Lymphocyte Associated Antigen 4 Short Spliced Form, Cytotoxic T-Lymphocyte-Associated Serine Esterase-4, Cytotoxic T-Lymphocyte-Associated Antigen 4, CD152 Isoform, CD152 Antigen, CELIAC3, IDDM12, ALPS5, GRD4, GSE, CD, Cytotoxic T-lymphocyte protein 4, CTLA4.

    • 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

      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDH HHHHH.

    • Background

      What is the molecular weight/Mw of CTLA4 Protein?
      CTLA4 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of CTLA4 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CTLA4 Protein?
      CTLA4 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTLA4 Protein?
      Determined by IL-2 ELISA via Jurkat human acute T cell leukemia cells. The ED50 range ≤ 150 ng/ml with Human B7-1/CD80.


      What is the amino acid sequence of CTLA4 Protein?
      ADLKAMHVAQ PAVVLASSRG IASFVCEYAS PGKATEVRVT VLRQADSQVT EVCAATYMMG NELTFLDDSI CTGTSSGNQV NLTIQGLRAM DTGLYICKVE LMYPPPYYLG IGNGTQIYVI DPEPCPDSDH HHHHH.

      What applications can CTLA4 Protein be used in?
      CTLA4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTLA4 Protein?
      The endotoxin level is minimal, CTLA4 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.

    Ctla4 Human Sf9
  • View Data Sheet

    Name :

    MLLT11 Human

    Description:

    Myeloid/Lymphoid Leukemia Translocated To 11 Human Recombinant

    AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    Product # :

    PRO-1991

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    Description

    MLLT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 113 amino acids (1-90 a.a) and having a molecular mass of 12.4kDa. MLLT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MLLT11 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myeloid/Lymphoid Leukemia Translocated To 11 (MLLT11) is a part of the Mixed-Lineage Leukemia protein family. MLLT11 which takes part in leukemogenesis and in the progression of severe monocytic leukemia (AML) is located on chromosome 11q23. MLLT11 which is also expressed in embryonic brain cortex is upregulated during neuronal differentiation and is taking part in the evolution of the central nervous system.

    • Synonyms

      AF1Q, RP11-316M1.10, Protein AF1q, MLLT11.

    • 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 MGSMRDPVSS QYSSFLFWRM PIPELDLSEL EGLGLSDTAT YKVKDSSVGK MIGQATAADQ EKNPEGDGLL EYSTFNFWRA PIASIHSFEL DLL.

    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.

    Mllt11 Human
  • View Data Sheet

    Name :

    HDHD1 Human

    Description:

    Haloacid Dehalogenase-Like Hydrolase Domain Containing 1 Human Recombinant

    Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.

    Product # :

    ENZ-028

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    Description

    HDHD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 248 amino acids (1-228 a.a.) and having a molecular mass of 27.4kDa. The HDHD1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HDHD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Haloacid dehalogenase-like hydrolase domain-containing protein 1A (HDHD1A) is a member of the adiponutrin family. HDHD1A is interesting because it is an X-linked gene that escapes X-inactivation. HDHD1A is particularly important in the perception of human X chromosome structural organization as well as the mechanism of X-inactivation.

    • Synonyms

      Pseudouridine-5'-monophosphatase, 5'-PsiMPase, Haloacid dehalogenase-like hydrolase domain-containing protein 1, Haloacid dehalogenase-like hydrolase domain-containing protein 1A, Protein GS1, HDHD1, DXF68S1E, FAM16AX, GS1, HDHD1A.

    • 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 MAAPPQPVTH LIFDMDGLLL DTERLYSVVF QEICNRYDKK YSWDVKSLVM GKKALEAAQI IIDVLQLPMS KEELVEESQT KLKEVFPTAA LMPGAEKLII HLRKHGIPFA LATSSGSASF DMKTSRHKEF FSLFSHIVLG DDPEVQHGKP DPDIFLACAK RFSPPPAMEK CLVFEDAPNG VEAALAAGMQ VVMVPDGNLS RDLTTKATLV LNSLQDFQPE LFGLPSYE.

    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.

    Hdhd1 Human
  • View Data Sheet

    Name :

    HPGDS Human

    Description:

    Hematopoietic Prostaglandin D Synthase Human Recombinant

    Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    Product # :

    ENZ-616

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    Description

    HPGDS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-199 a.a.) and having a molecular mass of 25.9kDa.HPGDS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPGDS protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hematopoietic Prostaglandin D Synthase (HPGDS) belongs to the sigma class glutathione-S-transferase family. The HPGDS enzyme catalyzes the conversion of PGH2 to PGD2 and has a role in the production of prostanoids in the immune system and mast cells. The presence of the HPGDS enzyme can be utilized to identify the differentiation stage of human megakaryocytes. Furthermore, HPGDS is a prostaglandin involved in smooth muscle contraction/relaxation and an effective inhibitor of platelet aggregation, and the conjugation of glutathione with a extensive range of aryl halides and organic isothiocyanates. In addition, HPGDS displays low glutathione-peroxidase activity towards cumene hydroperoxide. HPGDS is expressed in a number of megakaryocytic cell lines but not in platelets. HPGDS is highly expressed in the adipose tissue, macrophages and placenta; however it is expressed at lower levels in the lung, heart, lymph nodes, appendix, bone marrow and fetal liver.

    • Synonyms

      Hematopoietic prostaglandin D synthase, H-PGDS, GST class-sigma, Glutathione S-transferase, Glutathione-dependent PGD synthase, Glutathione-requiring prostaglandin D synthase, Prostaglandin-H2 D-isomerase, HPGDS, GSTS, PGDS, PTGDS2GSTS, PGD2, GSTS1-1.

    • 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 MGSHMPNYKL TYFNMRGRAE IIRYIFAYLD IQYEDHRIEQ ADWPEIKSTL PFGKIPILEV DGLTLHQSLA IARYLTKNTD LAGNTEMEQC HVDAIVDTLD DFMSCFPWAE KKQDVKEQMF NELLTYNAPH LMQDLDTYLG GREWLIGNSV TWADFYWEIC
      STTLLVFKPD LLDNHPRLVT LRKKVQAIPA VANWIKRRPQ TKL.

    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.

    Hpgds Human
  • View Data Sheet

    Name :

    ANXA13 Human

    Description:

    Annexin A13 Human Recombinant

    Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.

    Product # :

    PRO-197

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    Description

    ANXA13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 336 amino acids (1-316 a.a.) and having a molecular mass of 37.5kDa. The ANXA13 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ANXA13 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Annexin A13 (ANXA13) belongs to the annexin protein family, whose members play a role in cytoskeletal interactions, phospholipase inhibition, regulation of cellular growth, and intracellular signal transduction pathways. ANXA13 is believed to be the original originator of the 12 members of vertebrate annexins. ANXA13 expression is decidedly tissue-specific, being expressed only in intestinal and kidney epithelial cells. This expression is linked with a highly differentiated intracellular transport function.

    • Synonyms

      Annexin A13, Annexin XIII, Annexin-13, Intestine-specific annexin, ISA, ANXA13, ANX13, MGC150460.

    • 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 MGNRHAKASS PQGFDVDRDA KKLNKACKGM GTNEAAIIEI LSGRTSDERQ QIKQKYKATY GKELEEVLKS ELSGNFEKTA LALLDRPSEY AARQLQKAMK GLGTDESVLI EVLCTRTNKE IIAIKEAYQR LFDRSLESDV KGDTSGNLKK ILVSLLQANR NEGDDVDKDL AGQDAKDLYD AGEGRWGTDE LAFNEVLAKR SYKQLRATFQ AYQILIGKDI EEAIEEETSG DLQKAYLTLV RCAQDCEDYF AERLYKSMKG AGTDEETLIR IVVTRAEVDL QGIKAKFQEK YQKSLSDMVR SDTSGDFRKL LVALLH.

    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.

    Anxa13 Human
  • View Data Sheet

    Name :

    CXCL7 Human

    Description:

    Neutrophil Activating Protein-2 Human Recombinant (CXCL7)

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-274

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    Description

    Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7should 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 Neutrophil Activating Protein-2in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Background

      What is the molecular weight/Mw of CXCL7 HUMAN Protein?
      CXCL7 HUMAN Protein has a total Mw of 7.6kDa.

      What is the source or expression system of CXCL7 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 HUMAN Protein?
      CXCL7 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 HUMAN Protein?
      The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CXCL7 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

      What applications can CXCL7 HUMAN Protein be used in?
      CXCL7 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 HUMAN Protein?
      The endotoxin level is minimal, CXCL7 HUMAN Protein was purified using conventional chromatography techniques.


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    Nap2 Human
  • View Data Sheet

    Name :

    HSD17B11 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 11 Human Recombinant

    17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.

    Product # :

    ENZ-049

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    Description

    HSD17B11 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 287 amino acids (20-285 a.a.) and having a molecular mass of 31.4kDa. The HSD17B11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSD17B11 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 8 (HSD17B11) is a member of the HSD17B family of proteins, which regulate the availability of steroids within various tissues throughout the body. HSD17B11 is widely expressed with the highest levels found in the retina, pancreas, kidney, liver, lung, adrenal, small intestine, ovary and heart as well as in steroidogenic cells. HSD17B11 converts androstan-3-?,17-?-diol (3-?-diol) to androsterone, suggesting it may participate in androgen metabolism during steroidogenesis.

    • Synonyms

      17-beta-hydroxysteroid dehydrogenase 11, 17-beta-HSD 11, 17bHSD11, 17betaHSD11, 17-beta-hydroxysteroid dehydrogenase XI, 17-beta-HSD XI, 17betaHSDXI, Cutaneous T-cell lymphoma-associated antigen HD-CL-03, CTCL-associated antigen HD-CL-03, Dehydrogenase/reductase SDR family member 8, Retinal short-chain dehydrogenase/reductase 2, retSDR2, HSD17B11, DHRS8, PAN1B, SDR16C2, 17BHSD11.

    • 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 MESFVKLFIP KRRKSVTGEI VLITGAGHGI GRLTAYEFAK LKSKLVLWDI NKHGLEETAA KCKGLGAKVH TFVVDCSNRE DIYSSAKKVK AEIGDVSILV NNAGVVYTSD LFATQDPQIE KTFEVNVLAH FWTTKAFLPA MTKNNHGHIV TVASAAGHVS VPFLLAYCSS KFAAVGFHKT LTDELAALQI TGVKTTCLCP NFVNTGFIKN PSTSLGPTLE PEEVVNRLMH GILTEQKMIF IPSSIAFLTT LERILPERFL AVLKQKI.

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    Hsd17B11 Human
  • View Data Sheet

    Name :

    SGCB Human

    Description:

    Sarcoglycan Beta Human Recombinant

    Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.

    Product # :

    PRO-2211

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    Description

    SGCB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (87-318 a.a) and having a molecular mass of 27.8kDa.SGCB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SGCB protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer(pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sarcoglycan Beta, also known as SGCB, is a part of the sarcoglycan family. SGCB belongs to the sarcoglycan complex which is a subcomplex of the dystrophin-glycoprotein complex that connects between the F-actin cytoskeleton and the extracellular matrix.

    • Synonyms

      Beta-sarcoglycan, Beta-SG, 43 kDa dystrophin-associated glycoprotein, 43DAG, A3b, LGMD2E, Sarcoglycan, Beta (43kDa Dystrophin-Associated Glycoprotein), Limb Girdle Muscular Dystrophy 2E (Non-Linked Families), SGC.

    • 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 MGSWAVIRIG PNGCDSMEFH ESGLLRFKQV SDMGVIHPLY KSTVGGRRNE NLVITGNNQP IVFQQGTTKL SVENNKTSIT SDIGMQFFDP RTQNILFSTD YETHEFHLPS GVKSLNVQKA STERITSNAT SDLNIKVDGR AIVRGNEGVF IMGKTIEFHM GGNMELKAEN SIILNGSVMV STTRLPSSSS GDQLGSGDWV RYKLCMCADG TLFKVQVTSQ NMGCQISDNP CGNTH.

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    Sgcb Human
  • View Data Sheet

    Name :

    SHH Mouse

    Description:

    Sonic Hedgehog Mouse Recombinant

    SHH, HHG-1, HHG1, Sonic hedgehog protein.

    Product # :

    CYT-597

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    Description

    Sonic Hedgehog Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The Mouse Sonic Hedgehog is 99% homologous to the human gene.Cysteine at position 25 has been substituted with Ile.The Sonic HedgeHog is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM Na2PO4 pH-7.5.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by the dose-dependent induction of alkaline phosphatase production by C3H/10T1/2 (CCL-226) fibroblasts and is typically 0.48-0.72 µg/ml.

    More Info

    • Introduction

      Recombinant Mouse Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Mouse Sonic Hedgehog is 99% homologous to the human gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.

    • Synonyms

      SHH, HHG-1, HHG1, Sonic hedgehog protein.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG.

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    Sonic Hedgehog Mouse
  • View Data Sheet

    Name :

    HSPB2 Human

    Description:

    Heat Shock 27kDa Protein 2 Human Recombinant

    Heat shock 27kDa protein 2, DMPK-binding protein, MKBP, HSP27, LOH11CR1K.

    Product # :

    HSP-052

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    Description

    HSPB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 206 amino acids (1-182) and having a molecular mass of 22.8kDa.HSPB2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HSPB2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Heat shock protein beta-2 (HSPB2) is a member of the small heat shock protein (HSP20) family. HSPB2 is a regulator of DMPK kinase.

    • Synonyms

      Heat shock 27kDa protein 2, DMPK-binding protein, MKBP, HSP27, LOH11CR1K.

    • 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 MGSHMSGRSV PHAHPATAEY EFANPSRLGE QRFGEGLLPE EILTPTLYHG YYVRPRAAPA GEGSRAGASE LRLSEGKFQA FLDVSHFTPD EVTVRTVDNL LEVSARHPQR LDRHGFVSRE FCRTYVLPAD VDPWRVRAAL SHDGILNLEA PRGGRHLDTE VNEVYISLLP APPDPEEEEE AAIVEP.

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    Hspb2 Human
  • View Data Sheet

    Name :

    DnaK E.coli

    Description:

    DnaK (HSP70) E.Coli Recombinant

    HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    Product # :

    HSP-006

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    Description

    Recombinant Dnak produced in E.Coli is a single, non-glycosylated polypeptide chain containing 638 amino acids and having a molecular mass of 69 kDa.

    Source

    Escherichia Coli.

    Formulation

    The DnaK protein contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DnaK, originally identified for its DNA replication by bacteriophage l in E. coli is the bacterial HSP70 chaperone. This protein is involved in the folding and assembly of newly synthesized polypeptide chains and in preventing the aggregation of stress-denatured proteins.

    • Synonyms

      HSP-70, HSP70, DnaK, , Chaperone protein dnaK, Heat shock protein 70, Heat shock 70 kDa protein, groP, grpF, seg, b0014, JW0013.

    • 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

      MGKIIGIDLG TTNSCVAIMD GTTPRVLENA EGDRTTPSII AYTQDGETLV GQPAKRQAVTNPQNTLFAIK RLIGRRFQDE EVQRDVSIMP FKIIAADNGD AWVEVKGQKM APPQISAEVLKKMKKTAEDY LGEPVTEAVI TVPAYFNDAQ RQATKDAGRI AGLEVKRIINEPTAAALAYGLDKGTGNRTI AVYDLGGGTFDISIIEIDEV DGEKTFEVLA TNGDTHLGGE DFDSRLINYLVEEFKKDQGI DLRNDPLAMQ RLKEAAEKAK IELSSAQQTD VNLPYITADA TGPKHMNIKVTRAKLESLVE DLVNRSIEPL KVALQDAGLS VSDIDDVILV GGQTRMPMVQ KKVAEFFGKEPRKDVNPDEA VAIGAAVQGG VLTGDVKDVL LLDVTPLSLG IETMGGVMTT LIAKNTTIPTKHSQVFSTAE DNQSAVTIHV LQGERKRAAD NKSLGQFNLD GINPAPRGMPQIEVTFDIDADGILHVSAKD KNSGKEQKITIKASSGLNED EIQKMVRDAE ANAEADRKFE ELVQTRNQGDHLLHSTRKQV EEAGDKLPAD DKTAIESALT ALETALKGED KAAIEAKMQE LAQVSQKLMEIAQQQHAQQQ TAGADASANN AKDDDVVDAE FEEVKDKK.

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    Dnak Ecoli
  • View Data Sheet

    Name :

    DSTN Human

    Description:

    Destrin Human Recombinant

    Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    Product # :

    PRO-1137

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    Description

    DSTN Human Recombinant produced in E. coli is a single polypeptide chain containing 173 amino acids (1-165) and having a molecular mass of 19.5 kDa.DSTN is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DSTN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Actin depolymerizing factor (Destrin/DSTN) belongs to the ADF/Cofilin/destrin superfamily which has the ability to swiftly depolymerize F-Actin in a stoichiometric mode. The ADF family of proteins is responsible for enhancing the turnover rate of actin in vivo. Destrin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. DSTN functions in a pH-independent manner. DSTN is found in a variety of epithelial and endothelial cells, however it is virtually nonexistent in adult mouse heart and skeletal muscle cells. Destrin shares a 71% sequence homology with Cofilin, however the 2 proteins vary in their interaction with Actin.

    • Synonyms

      Destrin (actin depolymerizing factor), ACTDP, ADF, bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)), destrin, DSN.

    • 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

      MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPVLEHHH HHH

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    Dstn Human
  • View Data Sheet

    Name :

    ATG10 Human

    Description:

    Autophagy Related 10 Human Recombinant

    Autophagy Related Protein 10, ATG10 Autophagy Related 10 Homolog (S. Cerevisiae), Ubiquitin-Like-Conjugating Enzyme ATG10, APG10 Autophagy 10-Like (S. Cerevisiae), APG10-Like, APG10L, Pp12616, DKFZP586I0418, FLJ13954, EC 6.3.2.-.

    Product # :

    PRO-1234

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    Description

    ATG10 Human Recombinant produced in E. coli is a single polypeptide chain containing 243 amino acids (1-220) and having a molecular mass of 27.7 kDa.ATG10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ATG10 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-like-conjugating enzyme ATG10 (ATG10) is a 220 amino acid protein which localizes to the cytoplasm and has a role in autophagy, specifically acting as an E2-like enzyme providing Atg recognition sites during autophagosome synthesis. ATG10 functions as an E2-like enzyme which catalyzes the conjugation of ATG12 to ATG5, which is required for autophagy. In addition, ATG10 interacts with ATG12 in human embryonic kidney cells in the presence of ATG7. ATG10 probably serves as an ATG5-recognition molecule. Furthermore, ATG10 has a role in adenovirus-mediated cell lysis.

    • Synonyms

      Autophagy Related Protein 10, ATG10 Autophagy Related 10 Homolog (S. Cerevisiae), Ubiquitin-Like-Conjugating Enzyme ATG10, APG10 Autophagy 10-Like (S. Cerevisiae), APG10-Like, APG10L, Pp12616, DKFZP586I0418, FLJ13954, EC 6.3.2.-.

    • 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 MGSMEEDEFI GEKTFQRYCA EFIKHSQQIG DSWEWRPSKD CSDGYMCKIH FQIKNGSVMS HLGASTHGQT CLPMEEAFEL PLDDCEVIET AAASEVIKYE YHVLYSCSYQ VPVLYFRASF LDGRPLTLKD IWEGVHECYK MRLLQGPWDT ITQQEHPILG QPFFVLHPCK TNEFMTPVLK NSQKINKNVN YITSWLSIVG PVVGLNLPLS YAKATSQDER NVP

    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.

    Atg10 Human
  • View Data Sheet

    Name :

    ATG3 Human

    Description:

    Autophagy Related 3 Human Recombinant

    APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.

    Product # :

    PRO-1987

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    Description

    ATG3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 337 amino acids (1-314 a.a) and having a molecular mass of 38.3kDa. ATG3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ATG3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Autophagy Related 3 (ATG3) is a conjugating enzyme essential for the cytoplasm to vacuole transport (Cvt), autophagy, and mitochondrial homeostasis. ATG3 is localizes to the cytoplasm and is expressed in tissues with predominant levels found in kidney, placenta, liver, heart and skeletal muscle. ATG3 catalyzes a reaction which is necessary for autophagy. That reaction is the formation of the Atg8-phosphatidylethanolamine (ATG-PE) conjugate.

    • Synonyms

      APG3, APG3-LIKE, APG3L, PC3-96, Ubiquitin-like-conjugating enzyme ATG3, Autophagy-related protein 3, hApg3, PC3-96, ATG3.

    • 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 MGSMQNVINT VKGKALEVAE YLTPVLKESK FKETGVITPE EFVAAGDHLV HHCPTWQWAT GEELKVKAYL PTGKQFLVTK NVPCYKRCKQ MEYSDELEAI IEEDDGDGGW VDTYHNTGIT GITEAVKEIT LENKDNIRLQ DCSALCEEEE DEDEGEAADM EEYEESGLLE TDEATLDTRK IVEACKAKTD AGGEDAILQT RTYDLYITYD KYYQTPRLWL FGYDEQRQPL TVEHMYEDIS QDHVKKTVTI ENHPHLPPPP MCSVHPCRHA EVMKKIIETV AEGGGELGVH MYLLIFLKFV QAVIPTIEYD YTRHFTM.

    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.

    Atg3 Human
  • View Data Sheet

    Name :

    EFNA1 Human

    Description:

    Ephrin A1 Human Recombinant

    Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    Product # :

    PRO-971

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    Description

    EFNA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 185 amino acids (19-182) and having a molecular mass of 21.6 kDa.EFNA1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EFNA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EFNA1 belongs to the ephrin (EPH) family. The EPH subfamily is the biggest group of receptor protein kinases and they take part in vital nervous system function and development.

    • Synonyms

      Ephrin-A1, EPLG1, TNFAIP4, LERK1, EFL1, ECKLG, EPH-related receptor tyrosine kinase ligand 1, Immediate early response protein B61, Tumor necrosis factor alpha-induced protein 4, TNF alpha-induced protein 4, ligand of eph-related kinase 1, tumor necrosis factor, alpha-induced protein 4.

    • 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 MDRHTVFWNS SNPKFRNEDY TIHVQLNDYV DIICPHYEDH SVADAAMEQY ILYLVEHEEY QLCQPQSKDQ VRWQCNRPSA KHGPEKLSEK FQRFTPFTLG KEFKEGHSYY YISKPIHQHE DRCLRLKVTV SGKITHSPQA HVNPQEKRLA ADDPEVRVLH SIGHS

    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.

    Efna1 Human
  • View Data Sheet

    Name :

    IFNG Mouse, His

    Description:

    Interferon-gamma Mouse Recombinant, His Tag

    Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-1001

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    • SDS-PAGE

    Description

    Interferon-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (23-155a.a.) and having a molecular mass of 18.2kDa.IFNG is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IFNG protein solution (0.5mg/ml) containing 20mM MES buffer (pH5.0), 1mM DTT, 0.2M NaCl & 40% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    IFNG Mouse, His - Product image 1

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I interferons.

    • Synonyms

      Immune Interferon, type II interferon, T cell interferon, MAF, IFNG, IFG, IFI, IFN-gamma.

    • 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 MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.

    • Background

      What is the molecular weight/Mw of IFNG MOUSE, HIS Protein?
      IFNG MOUSE, HIS Protein has a total Mw of 18.2kDa.

      What is the source or expression system of IFNG MOUSE, HIS Protein?
      Escherichia Coli.

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

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

      What is the amino acid sequence of IFNG MOUSE, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMHGTVI ESLESLNNYF NSSGIDVEEK SLFLDIWRNW QKDGDMKILQ SQIISFYLRL FEVLKDNQAI SNNISVIESH LITTFFSNSK AKKDAFMSIA KFEVNNPQVQ RQAFNELIRV VHQLLPESSL RKRKRSRC.

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

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


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    Ifng Mouse His
  • View Data Sheet

    Name :

    BMF Human

    Description:

    Bcl2 Modifying Factor, Isoform 3 Human Recombinant

    Bcl-2-modifying factor, FLJ00065, BMF.

    Product # :

    PRO-700

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    Description

    Bcl2 modifying factor Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 144 amino acids (1-129 a.a.) and having a molecular mass of 15.6 kDa.The Bcl2 modifying factor is fused to 15 amino acid His Tag at Nterminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Bcl2 modifying factor solution contains 20mM Tris pH-7.5, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Bcl2 modifying factor, is a member of the Bcl2 protein family of apoptosis mediators. Bcl2 modifying factor is widely expressed in many tissues.
      Bcl2 modifying factor contains a single Bcl2 homology domain 3 (BH3), and binds Bcl2 proteins and functions as an apoptotic activator. Also, Bcl2 modifying factor is important for histone deacetylase (HDAC) inhibitors which alters the balance between acetylation and deacetylation, significantly increasing histone acetylation, while strongly inducing apoptosis in a variety of cancer cell types. Bcl2 modifying factor supports Bim in regulating cell death processes in response to many stimuli. A synergistic role for bim and Bcl2 modifying factor in an apoptotic pathway leading to the clearance of Neisseria gonorrhoeae -infected cells.

    • Synonyms

      Bcl-2-modifying factor, FLJ00065, BMF.

    • 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

      MASMTGGQQM GRGSHMEPSQ CVEELEDDVF QPEDGEPVTQ PGSLLSADLF AQSLLDCPLS RLQLFPLTHC CGPGLRPTSQ EDKATQTLSPASPSQGVMLP CGVTEEPQRL FYAPAEPKSC VVADPPLPAQ PCFEWRREQE RGRP.

    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.

    Bcl2 Modifying Factor Human
  • View Data Sheet

    Name :

    OSR2 Human

    Description:

    Odd-Skipped Related Transcription Factor 2 Human Recombinant

    Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.

    Product # :

    PRO-2067

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    Description

    OSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a) and having a molecular mass of 33kDa. OSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    OSR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Odd-Skipped Related Transcription Factor 2, also know as OSR2 belongs to the Odd C2H2-type zinc-finger protein family. OSR2 is a mammalian homolog of the Drosophila odd-skipped family of transcription factors.

    • Synonyms

      Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.

    • 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 MGSMGSKALP APIPLHPSLQ LTNYSFLQAV NTFPATVDHL QGLYGLSAVQ TMHMNHWTLG YPNVHEITRS TITEMAAAQG LVDARFPFPA LPFTTHLFHP KQGAIAHVLP ALHKDRPRFD FANLAVAATQ EDPPKMGDLS KLSPGLGSPI SGLSKLTPDR KPSRGRLPSK TKKEFICKFC GRHFTKSYNL LIHERTHTDE RPYTCDICHK AFRRQDHLRD HRYIHSKEKP FKCQECGKGF CQSRTLAVHK TLHMQTSSPT AASSAAKCSG ETVICGGTA.

    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.

    Osr2 Human
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