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  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 3 Mouse Recombinant

    Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

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    CYT-143

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    Description

    TGF-β 3 Mouse Recombinant produced in E.Coli is a disulfide-linked homodimeric, non-glycosylated, polypeptide chain containing two 113 amino acid chains and having a total molecular mass of 25.7kDa. The TGF-β 3 is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Mouse TGFB3 protein solution contains 20% Ethanol and 10mM Acetic acid.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity is determined by the ability to induce chondrogenic differentiation.

    More Info

    • Introduction

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGF Betas have been identified in mammals. TGF Beta 1, TGF Beta 2 and TGF Beta 3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Mouse TGF-beta 3 although stable at room temperature for 3 weeks, should be stored at 4°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).

    • Amino Acid Sequence

      MALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.718 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TGF-b 3 as a Reference Standard.

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

    Tgfb3 Mouse
  • View Data Sheet

    Description:

    GM-CSF Receptor Beta Human Recombinant

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

    Product # :

    CYT-928

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    • sds-page

    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

    • Background

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

      Abstract:


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

      Introduction:


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

      Production and Characterization:


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

      Immunological Significance:


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

      Therapeutic Implications:


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

      Conclusion:


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

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

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

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

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

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

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

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

    Csf2Rb Human
  • View Data Sheet

    Description:

    TGFB-Induced Factor Homeobox 2-Like Y-Linked Human Recombinant

    TGIFLY, Homeobox protein TGIF2LY, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, Y-linked, TGIF-like on the Y, TGIF2LY.

    Product # :

    PRO-1867

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    Description

    TGIF2LY Human Recombinant produced in E. coli is. a single polypeptide chain containing 208 amino acids (1-185) and having a molecular mass of 23.2kDa. TGIF2LY is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGIF2LY solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      TGFB-Induced Factor Homeobox 2-Like Y-Linked (TGIF2LY) is a part of the TALE/TGIF homeobox family of transcription factors. TGIF2LY is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition. TGIF2LY act as a regulator of TGIF2LX due to the fact that the C-terminus of TGIF2LY is different from that of its chromosome X homolog (TGIF2LX). TGIF2LY has also a transcription role in testis.

    • Synonyms

      TGIFLY, Homeobox protein TGIF2LY, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, Y-linked, TGIF-like on the Y, TGIF2LY.

    • 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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLRI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PVVQTMYKAC PCGPCQRARC QERSNQIRSR PLARSSPE.

    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.

    Tgif2Ly Human
  • View Data Sheet

    Description:

    Stromal Cell Derived Factor-1 Beta Mouse Recombinant (CXCL12)

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-326

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    Description

    Stromal Cell-Derived Factor-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8513 Dalton. The SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL12 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 its ability to chemoattract human monocytes at 50-100ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 Stromal Cell-Derived Factor-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    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.

    Sdf 1 B Mouse
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Mouse Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-252

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    Description

    Tumor Necrosis Factor-a Mouse Recombinant produced in E. coli is a single, non glycosylated, polypeptide chain containing 157 amino acids and having a molecular mass of 17301.32 Dalton. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.2.

    Purity

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

    Biological Activity

    The ED50 as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D is < 0.1ng/ml, corresponding to a Specific Activity of 10,000,000 Units/mg.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, insulin resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MLRSSSQNSS DKPVAHVVAN HQVEEQLEWL SQRANALLAN GMDLKDNQLV VPADGLYLVY SQVLFKGQGC PDYVLLTHTV SRFAISYQEK VNLLSAVKSP CPKDTPEGAE LKPWYEPIYL GGVFQLEKGD QLSAEVNLPK YLDFAESGQV YFGVIAL

    • Background

      Tumor Necrosis Factor-alpha (TNF-α) is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. It is primarily produced by activated macrophages, but can also be secreted by other immune cells, such as T cells, natural killer cells, and mast cells. TNF-α is involved in a wide range of physiological and pathological processes, including the defense against infections, the development of autoimmune diseases, and the progression of cancer.

      TNF-α exerts its effects by binding to two distinct cell surface receptors, TNF receptor 1 (TNFR1) and TNF receptor 2 (TNFR2). Upon binding to its receptors, TNF-α activates multiple signaling pathways, including the nuclear factor-kappa B (NF-κB) pathway, the mitogen-activated protein kinase (MAPK) pathway, and the apoptotic pathway. These signaling pathways regulate various cellular processes, such as inflammation, cell proliferation, differentiation, and apoptosis.

      In the context of infections, TNF-α plays a crucial role in the body's defense against pathogens. It promotes the recruitment and activation of immune cells, enhances the production of other pro-inflammatory cytokines, and stimulates the expression of adhesion molecules on endothelial cells, facilitating the migration of immune cells to the site of infection. TNF-α also helps to induce fever, which is an important component of the body's immune response to infections.

      However, excessive or prolonged production of TNF-α can contribute to the development of chronic inflammatory diseases, such as rheumatoid arthritis, inflammatory bowel disease, and psoriasis. In these conditions, elevated levels of TNF-α promote the infiltration of immune cells into the affected tissues, leading to tissue damage and the perpetuation of inflammation. The central role of TNF-α in the pathogenesis of these diseases has led to the development of anti-TNF-α therapies, which have revolutionized the treatment of chronic inflammatory diseases. These therapies include monoclonal antibodies, such as infliximab and adalimumab, and soluble TNF receptor fusion proteins, such as etanercept. Anti-TNF-α therapies have been shown to be effective in reducing inflammation, improving symptoms, and slowing disease progression in patients with chronic inflammatory diseases.

      In the context of cancer, TNF-α has complex and context-dependent effects on tumor development and progression. On one hand, TNF-α can promote anti-tumor immunity by activating immune cells and stimulating the production of other pro-inflammatory cytokines. On the other hand, chronic inflammation driven by TNF-α can promote tumor growth, angiogenesis, and metastasis. Therefore, the role of TNF-α in cancer is still an area of active research, and the development of TNF-α-targeted therapies for cancer remains a challenge.

      In conclusion, TNF-α is a pro-inflammatory cytokine that plays a critical role in the regulation of immune responses, inflammation, and cell survival. Its involvement in various physiological and pathological processes has made it an important target for the development of therapies for chronic inflammatory diseases and cancer. Anti-TNF-α therapies have revolutionized the treatment of chronic inflammatory diseases, but the complex role of TNF-α in cancer remains an area of ongoing research. Understanding the precise mechanisms by which TNF-α contributes to disease pathogenesis will be crucial for the development of more effective and targeted therapies.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.24 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of TNF-a as a Reference Standard.

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

    Tnf Alpha Mouse
  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 3 Rat Recombinant

    Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    Product # :

    CYT-1269

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    Description

    TGFB3 Rat Recombinant produced in CHO cells is a glycosylated, polypeptide homodimer chain containing 2x112 amino acids and having a total molecular mass of 25.0kDa. The TGFB3 is purified by proprietary chromatographic techniques.

    Source

    CHO cells.

    Formulation

    TGFB3 was lyophilized from a concentrated solution containing 35% (v/v) Acetonitrile and 0.1% (v/v) TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

    More Info

    • Synonyms

      Transforming Growth Factor-beta3, TGFB3, ARVD, FLJ16571, TGF-beta3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Transforming Growth Factor-Beta 3 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB3 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 TGFB3 in sterile 4mM HCl to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤-20°C which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSSDTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

    • Background

      Recombinant TGF-β3 Rat is commonly used in cell culture and biomedical research to investigate TGF-β signalling, stem cell differentiation, tissue engineering, chondrogenesis, wound healing, fibrosis, and cancer biology. TGFB3 is added to mesenchymal stem cell and chondrocyte cultures to promote cartilage formation and maintain specific cellular phenotypes under defined experimental conditions.

      What is the molecular weight / Mw of TGFB3 Rat Protein?
      TGFB3 Rat Protein has a total Mw of 25kDa.

      What is the source or expression system of TGFB3 Rat Protein?
      CHO Cells

      What is the Purity of TGFB3 Rat Protein?
      TGFB3 rat Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of TGFB3 rat Protein?
      Determined by the ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is less than 0.05 ng/ml, corresponding to a specific activity of ≥ 2.0×107 units/mg.

      What is the amino acid sequence of TGFB3 Protein?
      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHSR VLSLYNTINP EASASPCCVS QDLEPLTILY YIGKTPKIEQ LSNMIVKSCK CS

      What applications can TGFB3 rat Protein be used in?
      TGFB3 rat Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for TGFB3 rat Protein?
      The endotoxin level is minimal, TGFB3 rat Protein was purified using conventional chromatography techniques.

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

    TGFB3 Rat
  • View Data Sheet

    Description:

    Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-018

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Colorless, clear and transparent solution.

    • Stability

      G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

      What is the source or expression system of G CSF HUMAN, PEG Protein?
      Escherichia Coli.

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

      What is the Biological Activity of G CSF HUMAN, PEG Protein?
      The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

      What is the endotoxin level for G CSF HUMAN, PEG Protein?
      The endotoxin level is minimal, G CSF HUMAN, PEG 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.

    G Csf Human Pegylated
  • View Data Sheet

    Description:

    Stromal Cell-Derived Factor-1 beta Rat Recombinant (CXCL12)

    SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    Product # :

    CHM-248

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    Description

    SDF-1 beta Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 72 amino acids and having a molecular mass of 8.4 kDa. The Rat SDF-1b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rat SDF1B protein was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phsophate buffer pH-7.4 and 0.15M NaCl.

    Purity

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

    Biological Activity

    The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 100-150ng/ml corresponding to a Specific Activity of 6,667-10,000IU/mg.

    More Info

    • Introduction

      SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
      The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
      The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively.

    • Synonyms

      SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1B, TPAR1, SCYB12, SDF-1b, TLSF-b, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SDF-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 SDF-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KPVSLSYRCP CRFFESHVAR ANVKHLKILN TPNCALQIVA RLKSNNRQVC IDPKLKWIQE YLDKALNKRL KM.

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    Sdf 1B Rat
  • View Data Sheet

    Description:

    Tumor Necrosis Factor-Alpha Human Recombinant

    TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    Product # :

    CYT-223

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    Description

    Tumor Necrosis Factor-a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids (157 a.a. of the mature human TNF-alpha and an N-terminal methionine) and having a molecular mass of 17.5kDa. The TNF-alpha is purified by standard chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNF-a Human was lyophilized from a concentrated 1mg/ml solution containing 20mM PB, pH-7.2, and 100mM NaCl.

    Purity

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

    Biological Activity

    The Specific Activity is >5.0×107 IU/mg as determined by the cytolysis of murine L929 cells in the presence of Actinomycin D.

    More Info

    • Introduction

      Tumor necrosis factor is a cytokine involved in systemic inflammation and is a member of a group of cytokines that all stimulate the acute phase reaction. TNF is mainly secreted by macrophages.
      TNF causes apoptotic cell death, cellular proliferation, differentiation, inflammation, tumorigenesis and viral replication, TNF is also involved in lipid metabolism, and coagulation. TNF's primary role is in the regulation of immune cells.
      Dysregulation and, in particular, overproduction of TNF have been implicated in a variety of human diseases- autoimmune diseases, INS resistance, and cancer.

    • Synonyms

      TNF-alpha, Tumor necrosis factor ligand superfamily member 2, TNF-a, Cachectin, DIF, TNFA, TNFSF2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MVRSSSRTPS DKPVAHVVAN PQAEGQLQWL NRRANALLAN GVELRDNQLV VPSEGLYLIY SQVLFKGQGC PSTHVLLTHT ISRIAVSYQT KVNLLSAIKS PCQRETPEGA E AKPWYEPIY LGGVFQLEKG DRLSAEINRP DYLDFAESGQ VYFGIIAL.

    • Background

      TNF Alpha Human: An Overview of Its Role and Importance in Immunology

      TNF alpha human, also known as Tumor Necrosis Factor-alpha, is a critical cytokine in the immune system. Macrophages mainly produce this protein, and it plays a key role in inflammation and the acute phase reaction.

      This protein is involved in various cellular functions, including cell death, differentiation, proliferation, and immune regulation.

      Production and Properties

      Tumor Necrosis Factor-alpha is produced recombinantly in E. coli and consists of a single, non-glycosylated polypeptide chain. It includes 157 amino acids of the mature human TNF-alpha and an N-terminal methionine, resulting in a molecular mass of approximately 17.5 kDa.

      Furthermore, the protein is purified through standard chromatographic techniques to ensure high purity and biological activity.

      Solubility and Usage

      The lyophilized form of TNF appears as a sterile, white powder. It is recommended to reconstitute this powder in sterile water to achieve a solution of no less than 100µg/ml.

      This solution can then be further diluted for various experimental applications. TNF alpha is used extensively in research, particularly for studying its effects on cell signaling and immune response.

      Storage and Stability

      For long-term storage, TNF should be kept desiccated below -18°C. Once reconstituted, it should be used within a week if stored at 4°C or kept below -18°C for future use. Avoiding freeze-thaw cycles is crucial to maintain the protein's functionality.

      Biological Role and Implications

      TNF alpha human is involved in the regulation of immune cells and is known for its role in inflammatory processes.

      Dysregulation of TNF alpha production is linked to various diseases, such as autoimmune disorders, insulin resistance, and cancer. It is also a target for therapeutic interventions, particularly in conditions like rheumatoid arthritis and inflammatory bowel disease.

      Mechanism of Action

      TNF alpha can induce fever, apoptotic cell death, and can inhibit tumorigenesis and viral replication. Moreover, it is a potent mediator of the acute phase reaction, which influences the activity of various cells involved in systemic inflammation.

      Research and Clinical Importance

      Scientific research on TNF has provided insights into its complex role in disease mechanisms. Its interaction with receptors such as TNFRSF1A underscores its multifaceted effects across different organ systems, from liver function to brain activity.

      Ongoing studies continue to explore its therapeutic potential, especially how it can be modulated to treat diseases without harmful side effects.

      In essence, TNF alpha human is a versatile and powerful component of the immune system, important for both health and disease. Understanding its pathways and functions helps scientists develop better treatments for various inflammatory and autoimmune diseases.



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    Tnf Alpha Human
  • View Data Sheet

    Description:

    GDNF Family Receptor Alpha 3 Human Recombinant

    GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

    Product # :

    CYT-399

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    • sds-page

    Description

    GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).

    • Synonyms

      GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.

    • 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 MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

    • Background

      What is the molecular weight/Mw of GFRA3 HUMAN Protein?
      GFRA3 HUMAN Protein has a total Mw of 40.7kDa.

      What is the source or expression system of GFRA3 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GFRA3 HUMAN Protein?
      GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA3 HUMAN Protein?
      The biological functionality of GFRA3 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GFRA3 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN

      What applications can GFRA3 HUMAN Protein be used in?
      GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA3 HUMAN Protein?
      The endotoxin level is minimal, GFRA3 HUMAN Protein was purified using conventional chromatography techniques.


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    Gfra3 Human
  • View Data Sheet

    Description:

    Pregnancy Specific Beta-1-Glycoprotein 1 Human Recombinant, Sf9

    Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.

    Product # :

    PRO-2452

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    Description

    PSG1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 394 amino acids (35-419a.a.) and having a molecular mass of 44.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PSG1 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    PSG1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pregnancy Specific Beta-1-Glycoprotein 1 (PSG1) is a member of a subgroup of transcription factors which are phosphorylated upon binding to promoter sequences. PSGs belong to the carcinoembryonic antigen (CEA) family and function as early biochemical markers of syncytiotrophoblast formation. Furthermore, PSG1 is assumed to mediate placental vascular morphogenesis by enhancing VEGF-A production and endothelial tube formation. PSG1 is a major product of the syncytiotrophoblast, reaching concentrations of 100- 290 mg/l at term in the serum of pregnant women.

    • Synonyms

      Pregnancy Specific Beta-1-Glycoprotein 1, PSBG1, B1G1, Fetal Liver Non-Specific Cross-Reactive Antigen 1/2, Pregnancy-Specific Beta-1 Glycoprotein C/D, CD66 Antigen-Like Family Member F, PS-Beta-C/D, PS-Beta-G-1, FL-NCA-1/2, PSBG-1, PSGGA, PSG95, SP1, Pregnancy-Specific Beta-1-Glycoprotein 1, Pregnancy-Specific B-1 Glycoprotein, Pregnancy-Specific Glycoprotein 1, CD66f Antigen, DHFRP2, PSGIIA, CD66f, PBG1, PSG1.

    • 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

      ADLQVTIEAE PTKVSEGKDV LLLVHNLPQN LTGYIWYKGQ MRDLYHYITS YVVDGEIIIY GPAYSGRETA YSNASLLIQN VTREDAGSYT LHIIKGDDGT RGVTGRFTFT LHLETPKPSI SSSNLNPRET MEAVSLTCDP ETPDASYLWW MNGQSLPMTH SLKLSETNRT LFLLGVTKYT AGPYECEIRN PVSASRSDPV TLNLLPKLPK PYITINNLNP RENKDVLNFT CEPKSENYTY IWWLNGQSLP VSPRVKRPIE NRILILPSVT RNETGPYQCE IRDRYGGIRS DPVTLNVLYG PDLPRIYPSF TYYRSGEVLY LSCSADSNPP AQYSWTINEK FQLPGQKLFI RHITTKHSGL YVCSVRNSAT GKESSKSMTV EVSGKWIPHH HHHH.

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    Psg1 Protein
  • View Data Sheet

    Description:

    Interleukin-1 beta Human Recombinant

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    Product # :

    CYT-208

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    Description

    Interleukin-1 beta Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 153 amino acids and having a molecular mass of 17000 Dalton.The IL-1 Beta is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL-1 Beta was lyophilized from a concentrated (1mg/ml) sterile solution containing 50mM Phosphate buffer pH=7.1 and 150mM NaCl.

    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 in the test of augmentation of lymphocyte proliferation assay using mouse thymus was found to be 200,000,000 IU/mg.

    More Info

    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1 Beta stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin from synovial cells.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-1b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1 Beta 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-1b in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.631 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IL-1 beta Recombinant as a Reference Standard.

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    Il 1 Beta Human
  • View Data Sheet

    Description:

    Nucleobindin-2 Human Recombinant

    Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    Product # :

    PRO-492

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    Description

    The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 9.7kDa containing 82 amino acid residues of the human NUCB2.

    Source

    Escherichia Coli.

    Formulation

    The NUCB2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NUCB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NUCB2 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 NUCB2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

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    Nucb2 Human
  • View Data Sheet

    Description:

    Neurotrophin-3 Mouse Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    Product # :

    CYT-688

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    Description

    Neurotrophin-3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids and having a molecular mass of 13.6kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.02% TFA.

    Purity

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

    Biological Activity

    The activity, as determined by the dose-dependent proliferation of BaF3 cells transfected with the TrkB receptor, is typically in the range of 1-10 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3, Neurotrophin-3, Ntf3, Ntf-3, AI316846, AI835689, Nt3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      YAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

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    Neurotrophin 3 Mouse
  • View Data Sheet

    Description:

    Transforming Growth Factor-beta 1 Human

    Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

    Product # :

    CYT-561

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    Description

    Human Transforming Growth Factor-beta 1 purified from Human Platelets having a molecular mass of 25kDa.The TGF-b 1 is purified by proprietary chromatographic techniques.

    Source

    Human Platelets.

    Formulation

    TGF-Beta1 protein was lyophilized from a solution containing 30% acetonitrile and 0.1% trifluoroacetic acid.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Stimulates the growth of NRK-1 cells in soft agar at concentrations ranging from 0.1 to 5ng/ml corresponding to a specific activity of 200,000-10,000,000IU/mg. Effective concentration ranges must be experimentally determined. Purified EGF and/or TGF- must be present for observation of the biological activity.

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    • Introduction

      Transforming growth factor betas (TGF Betas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

    • Synonyms

      Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized TGF-beta 1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGF-beta 1 should be stored at 4°C between 2-7 days and for future use below -18°C.DO NOT RECONSTITE WITH NEUTRAL BUFFERS.DO NOT USE GLASS IMPLEMENTS OR EXTENSIVE MANIPULATIONS.PREVENT FREEZE THAW CYCLES.

    • Solubility

      It is recommended to reconstitute lyophilized TGF-beta 1 in 0.5% BSA in 0.1N acetic acid, which can then be further diluted to the desired aliquot with 30% acetonitrile and 0.1% trifluoroacetic acid.

    • Background

      Title: Transforming Growth Factor-Beta 1 Human: An Insight into its Role in Cellular Regulation

      Abstract:


      Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a critical role in various cellular processes, including cell growth, differentiation, apoptosis, and immune regulation. This research paper aims to provide a comprehensive overview of the structure, synthesis, signaling pathways, and biological functions of TGF-β1 in human cells. Additionally, this article highlights the relevance of TGF-β1 in various physiological and pathological conditions, including cancer, fibrosis, and immune disorders. Furthermore, potential therapeutic strategies targeting TGF-β1 signaling are also discussed. The information presented in this paper consolidates the current understanding of TGF-β1 and its significance in cellular regulation.

      Introduction:


      Transforming Growth Factor-Beta 1 (TGF-β1) belongs to a superfamily of growth factors that regulate various cellular processes. It is synthesized as a precursor protein and undergoes proteolytic cleavage to generate the biologically active form. TGF-β1 exerts its effects by binding to specific cell surface receptors, leading to the activation of downstream signaling cascades. These signaling pathways involve Smad-dependent and Smad-independent mechanisms, which ultimately regulate gene expression and cellular responses.

      Biological Functions:


      TGF-β1 regulates cell proliferation by exerting both stimulatory and inhibitory effects, depending on the cellular context. It plays a crucial role in tissue development, wound healing, and tissue repair by promoting extracellular matrix synthesis and modulating the immune response. TGF-β1 also has immunomodulatory functions, influencing the differentiation and function of immune cells. However, dysregulation of TGF-β1 signaling is associated with various pathologies, including cancer progression, fibrosis, and autoimmune disorders.

      Role in Cancer:


      TGF-β1 acts as a tumor suppressor in early stages of cancer by inhibiting cell proliferation and inducing apoptosis. However, in advanced stages, it promotes tumor progression by enhancing tumor cell migration, invasion, and angiogenesis. The dual role of TGF-β1 in cancer highlights its complex involvement in tumorigenesis.

      Therapeutic Implications:


      Given the significant role of TGF-β1 in various diseases, targeting its signaling pathways has emerged as a potential therapeutic strategy. Several approaches, including small molecule inhibitors, antibodies, and gene therapies, are being explored to modulate TGF-β1 activity in a controlled manner. These interventions hold promise in the treatment of cancer, fibrosis, and other TGF-β1-related disorders.

      Conclusion:


      Transforming Growth Factor-Beta 1 is a versatile cytokine with diverse functions in cellular regulation. Its role in physiological processes and disease pathogenesis underscores its importance as a therapeutic target. Further investigations into the precise mechanisms and downstream effects of TGF-β1 signaling will contribute to the development of novel therapies for various human disorders.

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    Tgf B1 Human
  • View Data Sheet

    Description:

    Glia Maturation Factor Beta Human Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    Product # :

    CYT-565

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Human Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.5 kDa. Glia Maturation Factor-Beta, GMF-Beta, Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was lyophilized after dialysis against 20mM PBS pH=7.4 and 130mM NaCl.

    Purity

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

    More Info

    • Introduction

      Glia Maturation Factor-Beta (GMF-Beta) is a 17 kDa protein nerve gorwth factor identified as a growth and differentiation factor in the vertebrate brain.
      Glia Maturation Factor-Beta stimulates differentiation of normal neurons as well as glial cells. GMFB inhibits the proliferation of the N-18 neuroblastoma line and the C6 glioma line while promoting their phenotypic expression.
      GMF-beta inhances the phenotypic expression of glia & neurons thus inhibits the proliferation of their respective tumors when added to cell culture. Although astrocytes produce GMF-b and stores it inside the cells, they don’t secrete the GMF-B into the cultured medium. Cell- surface GMFb acts on the target cells at close range when cells are in direct contact. GMF-Beta is produced by thymic epithelial cells and plays an important role in T cell development in favor of CD4+ T cells.
      GMF-Beta is a brain-specific protein which belongs to the actin-binding proteins (ADF) family. GMF-beta appears to play a role in the differentiation, maintenance, and regeneration of the nervous system. It also supports the progression of certain auto-immune diseases, possibly through its ability to induce the production and secretion of various pro-inflammatory cytokines.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

    • Background

      What is the molecular weight/Mw of GMFB HUMAN Protein?
      GMFB HUMAN Protein has a total Mw of 16.5kDa.

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

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

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

      What is the amino acid sequence of GMFB HUMAN Protein?
      SESLVVCDVAEDLVEKLRKFRFRKETNNAAIIMKIDKDKRLVVLDEELEGISPD
      ELKELPERQPRFIVYSYKYQHDDGRVSYPLCFIFSSPVGCKPEQQMMYAGSKN
      KLVQT AELTKVFEIRNTEDLTEEWLREKLGFFH.

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

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


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    Gmfb Human
  • View Data Sheet

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

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    Ncf1 Human
  • View Data Sheet

    Description:

    NF-kappa-B Inhibitor Delta Human Recombinant

    NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.

    Product # :

    PRO-1684

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    Description

    NFKBID Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 35.9 kDa.NFKBID is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NFKBID solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      NFKBID belongs to the IkB family of proteins which contains four groups (IkB-alpha, IkB-beta, IkB-gamma, IkB-epsilon). NFKBID takes part in regulating inflammatory responses and cytokine, IL-2 and IL-6 expression through NFkB activity. NFKBID has 3 known alternative spliced isoforms, and is associated with RelB, NF?B p50 and NFkB p65 in nucleus. NFKBID is involeved in thymocyte selection in response to TCR induction.

    • Synonyms

      NF-kappa-B inhibitor delta, I-kappa-B-delta, IkB-delta, IkappaBdelta, IkappaBNS, T-cell activation NFKB-like protein, TA-NFKBH, NFKBID, IKBNS.

    • 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 MGSMEAGPWR VSAPPSGPPQ FPAVVPGPSL EVARAHMLAL GPQQLLAQDE EGDTLLHLFA ARGLRWAAYA AAEVLQVYRR LDIREHKGKT PLLVAAAANQ PLIVEDLLNL GAEPNAADHQ GRSVLHVAAT YGLPGVLLAV LNSGVQVDLE ARDFEGLTPL HTAILALNVA MRPSDLCPRV LSTQARDRLD CVHMLLQMGA NHTSQEIKSN KTVLHLAVQA ANPTLVQLLL ELPRGDLRTF VNMKAHGNTA LHMAAALPPG PAQEAIVRHL LAAGADPTLR NLENEQPVHL LRPGPGPEGL RQLLKRSRVA PPGLSS.

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    Nfkbid Human
  • View Data Sheet

    Description:

    Nucleobindin-2 Human Recombinant, His Tag

    Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    Product # :

    PRO-142

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    Description

    The Recombinant Human NUCB2 (Nesfatin) produced in E.coli has a molecular mass of 10.79kDa containing 92 amino acid residues of the human NUCB2 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    NUCB2 (Nesfatin) was filtered (0.4 µm) and lyophilized from 0.5 mg/ml in 20mM Tris and 50mM NaCl, pH 7.5.

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    • Introduction

      Nucleobindin-2 (also known as NUCB2 or Nesfatin) is a EF-hand calcium-binding protein. Nucleobindin-2 takes part in calcium homeostasis and is a multifunctional protein that interacts with Ca(2+) nucleic acids & various regulatory proteins in different signaling pathways. NUCB2 (Nesfatin) is localized in neuronal perikarya and dendrites of mouse brain.

    • Synonyms

      Nucleobindin-2, DNA-binding protein NEFA, Gastric cancer antigen Zg4, NUCB2, NEFA, Nesfatin.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VPIDIDKTKV QNIHPVESAK IEPPDTGLYY DEYLKQVIDV LETDKHFREK LQKADIEEIK SGRLSKELDL VSHHVRTKLD EL.

    • Applications

      Western blotting.

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    Nucb2 Human His
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    Description:

    TGFB-Induced Factor Homeobox 2-Like, X-Linked Human Recombinant

    Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein, TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.

    Product # :

    PRO-1902

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    Description

    TGIF2LX Human Recombinant produced in E. coli is. a single polypeptide chain containing 264 amino acids (1-241) and having a molecular mass of 29.1kDa.TGIF2LX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TGIF2LX solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

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    • Introduction

      TGFB-Induced Factor Homeobox 2-Like, X-Linked (TGIF2LX) belongs to the TALE/TGIF homeobox family of transcription factors and takes part in spermatogenesis. A homolog of TGIF2LX is located in the male specific region of chromosome Y, in a block of sequence which is the outcome of a large X-to-Y transposition.

    • Synonyms

      Homeobox protein TGIF2LX, TGF-beta-induced transcription factor 2-like protein,
      TGFB-induced factor 2-like protein, X-linked, TGIF-like on the X, TGIF2LX, TGIFLX, TGFB-Induced Factor Homeobox 2-Like, X-Linked.

    • 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 MGSMEAAADG PAETQSPVEK DSPAKTQSPA QDTSIMSRNN ADTGRVLALP EHKKKRKGNL PAESVKILRD WMYKHRFKAY PSEEEKQMLS EKTNLSLLQI SNWFINARRR ILPDMLQQRR NDPIIGHKTG KDAHATHLQS TEASVPAKSG PSGPDNVQSL PLWPLPKGQM SREKQPDPES APSQKLTGIA QPKKKVKVSV TSPSSPELVS PEEHADFSSF LLLVDAAVQR AAELELEKKQ EPNP.

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    Tgif2Lx Human
  • View Data Sheet

    Description:

    Transforming Growth Factor Beta Receptor II, His Tag Human Recombinant

    AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.

    Product # :

    PKA-088

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    Description

    TGFBR2 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 383 amino acids (23-166a.a) and having a molecular mass of 43.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TGFBR2 is expressed with a 239aa hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The TGFBR2 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      TGFBR2 is part of the Ser/Thr protein kinase family and the TGFB receptor subfamily. TGFBR2 is a transmembrane protein that has a protein kinase domain, forms a heterodimeric complex with another receptor protein, and binds TGF-beta. This receptor/ligand complex phosphorylates proteins, which then enter the nucleus and regulate the transcription of a subset of genes related to cell proliferation. Mutations in TGFBR2 gene have been associated with Marfan syndrome, Loeys-Deitz Aortic Aneurysm Syndrome, and the development of various types of tumors. TGFBR2 expression is increased in oral squamous cell carcinoma cells. TGFBR2 attenuates the biological activities of TGF-beta in colorectal cancer. TGFBR2 expression is decreased by IL-1beta while inducing Sp3 via NFkappaB. TGFB2 and TGFBR2 are involved in the antiestrogenic activity of tamoxifen metabolites in breast cancer.

    • Synonyms

      AAT3, FAA3, MFS2, RIIC, LDS1B, LDS2B, TAAD2, TGFR-2, TGFbeta-RII, TGFBR-2, TGF-beta receptor type-2, Transforming growth factor-beta receptor type II, TGF-beta receptor type II, TGF-beta type II receptor, TbetaR-II, TGFBR2.

    • 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

      TIPPHVQKSV NNDMIVTDNN GAVKFPQLCK FCDVRFSTCD NQKSCMSNCS ITSICEKPQE VCVAVWRKND ENITLETVCH DPKLPYHDFI LEDAASPKCI MKEKKKPGET FFMCSCSSDE CNDNIIFSEE YNTSNPDLLL VIFQLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH.

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    Tgfbr2 Human His
  • View Data Sheet

    Description:

    Interleukin-1 beta Mouse Recombinant, His Tag

    Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta, Interleukin-1 beta.

    Product # :

    CYT-578

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    Description

    Interleukin-1 beta Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 189 amino acids and having a molecular mass of 21 kDa. The IL-1b is fused to His-Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IL-1B protein contains 20mM Tris pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Interleukin-1b is produced by activated macrophages, IL-1B stimulates thymocyte proliferation by inducing il-2 release, b-cell maturation and proliferation, and fibroblast growth factor activity. IL1B proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the release of prostaglandin and collagenase from synovial cells. IL-1b is an inflammatory cytokine which modulates angiogenesis by interacting directly with vascular endothelial cells & increasing the production of proangiogenic factors through paracrine control. IL-1 beta stimulates endothelial cell migration and proliferation, adhesion-molecule expression, inflammatory mediator production, and leukocyte recruitment. IL1B is essential for tumor growth, metastasis, and angiogenesis in quite a few animal models.

    • Synonyms

      Catabolin, Lymphocyte-activating factor (LAF), Endogenous Pyrogen (EP), Leukocyte Endogenous Mediator (LEM), Mononuclear Cell Factor (MCF), IL1F2, IL-1 beta, Interleukin-1 beta.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMVPI RQLHYRLRDE QQKSLVLSDP YELKALHLNG QNINQQVIFS MSFVQGEPSN DKIPVALGLK GKNLYLSCVM KDGTPTLQLE SVDPKQYPKK KMEKRFVFNK IEVKSKVEFE SAEFPNWYIS TSQAEHKPVF LGNNSGQDII DFTMESVSS.

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    Il 1 Beta Mouse His
  • View Data Sheet

    Description:

    Glia Maturation Factor Beta Mouse Recombinant

    Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    Product # :

    CYT-006

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    Description

    Glia Maturation Factor-Beta (GMF-Beta) Mouse Recombinant produced in E.Coli is a signle, non-glycosylated, polypeptide chain containing 141 amino acids and having a total molecular mass of 16.6kDa. GMF-Beta, Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMF-beta protein was 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.

    More Info

    • Introduction

      GMFB is part of the GMF subfamily of the larger actin-binding protein ADF family. GMFB is phosphorylated after phorbol ester stimulation, and is crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

    • Synonyms

      Glia maturation factor beta, GMFB, GMF-B, GMF-beta, GMF, C79176, AI851627, D14Ertd630e, 3110001H22Rik, 3110001O16Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

    • Background

      What is the molecular weight/Mw of GMFB MOUSE Protein?
      GMFB MOUSE Protein has a total Mw of 16.6kDa.

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

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

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

      What is the amino acid sequence of GMFB MOUSE Protein?
      SESLVVCDVA EDLVEKLRKF RFRKETHNAA IIMKIDKDER LVVLDEELEG
      VSPDELKDEL PERQPRFIVY SYKYQHDDGR VSYPLCFIFS SPVGCKPEQQ
      MMYAGSKNKL VQTAELTKVF EIRNTEDLTE EWLREKLGFF H.

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

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

    Gmfb Mouse
  • View Data Sheet

    Description:

    Transforming Growth Factor-Beta 2 Mouse Recombinant

    Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

    Product # :

    CYT-1266

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    Shipped at Room temp

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    More Info

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

    Description

    Transforming Growth Factor-Beta 2 Mouse Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
    TGFB2 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    CHO Cells.

    Formulation

    The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

    Purity

    Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

    Biological Activity

    The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

    More Info

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 should be stored at 4°C between 2-7 days and for future use below -18°C.
      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
      Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

    • Background

      TGFB2 differ from TGFB1 in the tissue distribution, receptor interactions, and several biological roles.
      TGFB2 requires TGFBR3 for its binding to TGFBR2 while TGFB1 binds directly to the receptor TGFBR2.
      TGFB2 is crucial for embryonic development ocular biology, neural development, and tissue morphogenesis while TGFB1 is crucial for immune regulation and fibrosis.
      TGFB2 exhibits more tissue-specific developmental expression Vs TGFB1.


      What is the source or expression system of Mouse TGFB2 Protein?
      CHO Cells

      What is the Purity of Mouse TGFB2 Protein?
      Mouse TGFB2 Protein is >97% pure as determined by SDS-PAGE.

      What is the molecular weight / Mw of Mouse TGFB2 Protein?
      Mouse TGFB2 Protein having a total Mw of 25.6kDa.

      What is the Biological Activity of Mouse TGFB2 Protein?
      The biological functionality of Mouse TGFB2 Protein is determined by mouse HT-2 cells.

      What is the endotoxin level for Mouse TGFB2 Protein?
      The endotoxin level is minimal, Mouse TGFB2 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of Mouse TGFB2 Protein?
      ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.

      Is TGFB2 a homodimer / homodimeric protein?
      Yes, TGFB2 is homo dimer consisting of 2 identical chains.

    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.

    tgfb2 mouse