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Search results

1000 results found for “asfv”

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  • View Data Sheet

    Name :

    FGF 1 Mouse, His

    Description:

    Fibroblast Growth Factor-acidic Mouse Recombinant, His Tag

    HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    Product # :

    CYT-072

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    Description

    FGF-1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (16-155 a.a) and having a molecular mass of 18kDa (Molecular weight on SDS-PAGE will appear higher).FGF-1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FGF-1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    FGF1-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    • Physical Appearance

      Sterile Filtered colorless 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 MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

    • Background

      What is the molecular weight/Mw of FGF 1 Protein?
      FGF 1 Protein has a total Mw of 18kDa.

      What is the source or expression system of FGF 1 Protein?
      Escherichia Coli.

      What is the Purity of FGF 1 Protein?
      FGF 1 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 1 Protein?
      The biological functionality of FGF 1 Protein will be determined in the future.

      What is the amino acid sequence of FGF 1 Protein?
      MGSSHHHHHH SSGLVPRGSH MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

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

      What is the endotoxin level for FGF 1 Protein?
      The endotoxin level is minimal, FGF 1 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.

    Fgf 1 Mouse His
  • View Data Sheet

    Name :

    ACPP Human, Sf9

    Description:

    Acid Phosphatase Prostate, Human Recombinant, sf9

    Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.

    Product # :

    ENZ-968

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    Description

    ACPP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 360 amino acids (33-386 a.a.) and having a molecular mass of 41.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). ACPP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acid phosphatase, prostate (ACPP) is a non-specific tyrosine phosphatase, which dephosphorylates a varied number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. ACPP has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.

    • Synonyms

      Acid Phosphatase, Prostate, Thiamine Monophosphatase, Ecto-5-Nucleotidase, 5-Nucleotidase, EC 3.1.3.2, TMPase, 5-NT, Prostatic Acid Phosphatase, Prostatic Acid Phosphotase, EC 3.1.3.5, ACP-3 , ACP3, PAP.

    • 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

      KELKFVTLVF RHGDRSPIDT FPTDPIKESS WPQGFGQLTQ LGMEQHYELG EYIRKRYRKF LNESYKHEQV YIRSTDVDRT LMSAMTNLAA LFPPEGVSIW NPILLWQPIP VHTVPLSEDQ LLYLPFRNCP RFQELESETL KSEEFQKRLH PYKDFIATLG KLSGLHGQDL FGIWSKVYDP LYCESVHNFT LPSWATEDTM TKLRELSELS LLSLYGIHKQ KEKSRLQGGV LVNEILNHMK RATQIPSYKK LIMYSAHDTT VSGLQMALDV YNGLLPPYAS CHLTELYFEK GEYFVEMYYR NETQHEPYPL MLPGCSPSCP LERFAELVGP VIPQDWSTEC MTTNSHQGTE DSTDHHHHHH.

    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.

    Acpp Human Sf9
  • View Data Sheet

    Name :

    Adiponectin Human, Sf9

    Description:

    Adiponectin Human Recombinant, Sf9

    Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    Product # :

    CYT-1002

    Price :

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    • description
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    • sds-page
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    Description

    Acrp30 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 146 amino acids (106-242a.a.) and having a molecular mass of 16.9kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). Acrp30 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Acrp30 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

      Adiponectin, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1 Protein, Adipocyte Complement-Related 30 KDa Protein, 30 KDa Adipocyte Complement-Related Protein, ACRP30, APM-1, GBP28, ACDC, APM1, Adipocyte, C1q And Collagen Domain-Containing Protein, Adipocyte, C1Q And Collagen Domain Containing, Adipose Most Abundant Gene Transcript 1, Adipose Specific Collagen-Like Factor, Gelatin-Binding Protein 28, Gelatin-Binding Protein, Adiponectin Precursor, Adiponectin, ADIPQTL1, ADPN, 30 kDa adipocyte complement-related protein, dipocyte complement-related 30 kDa protein, ACRP30, Adipocyte, C1q and collagen domain-containing protein, Adipose most abundant gene transcript 1 protein, apM-1, Gelatin-binding protein.

    • 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

      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16.9kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      ADPEGAYVYR SAFSVGLETY VTIPNMPIRF TKIFYNQQNH YDGSTGKFHC NIPGLYYFAY HITVYMKDVK VSLFKKDKAM LFTYDQYQEN NVDQASGSVL LHLEVGDQVW LQVYGEGERN GLYADNDNDS TFTGFLLYHD HHHHHH.

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

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

    Acrp30 Human Sf9
  • View Data Sheet

    Name :

    FGF 1 Mouse

    Description:

    Fibroblast Growth Factor-Acidic Mouse Recombinant

    HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    Product # :

    CYT-528

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    Description

    Fibroblast Growth Factor-acidic Mouse Recombinant (FGF-1) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 141 amino acids and having a molecular mass of 15.9kDa. The FGF acidic is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.0, 5% Trehalose, 0.02% Tween-80, 0.5mM DTT and 0.5mM EDTA.

    Purity

    Greater than 96.0% as determined by SDS-PAGE and HPLC analyses.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

    Citations

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    • Introduction

      Acidic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.

    • Synonyms

      HBGF-1, ECGF-beta, FIBP, FGFIBP, FIBP-1, ECGF, ECGFA, GLIO703, FGF1, FGF-a.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

    • Background

      What is the molecular weight/Mw of FGF 1 Protein?
      FGF 1 Protein has a total Mw of 15.9kDa.

      What is the source or expression system of FGF 1 Protein?
      Escherichia Coli.

      What is the Purity of FGF 1 Protein?
      FGF 1 Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF 1 Protein?
      The ED50 as determined by the dose-dependent proliferation of mouse BALB/c 3T3 cells, is less than 0.2ng/ml corresponding to a Specific Activity of 5x106IU/mg.

      What is the amino acid sequence of FGF 1 Protein?
      MFNLPLGNYK KPKLLYCSNG GHFLRILPDG TVDGTRDRSD QHIQLQLSAE SAGEVYIKGT ETGQYLAMDT EGLLYGSQTP NEECLFLERL EENHYNTYTS KKHAEKNWFV GLKKNGSCKR GPRTHYGQKA ILFLPLPVSS D.

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

      What is the endotoxin level for FGF 1 Protein?
      The endotoxin level is minimal, FGF 1 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.

    Fgf 1 Mouse
  • View Data Sheet

    Name :

    GFRA1 Rat

    Description:

    GDNF Family Receptor Alpha 1 Rat Recombinant

    GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    Product # :

    CYT-1012

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    Description

    GFRA1 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 645 amino acids (25-430a.a.) and having a molecular mass of 72.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). GFRA1 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GFRA1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GDNF family receptor alpha-1 (GFRA1) belongs to the GDNF receptor family. GFRA1 is a glycosyl-phosphatidylinositol(GPI)-linked cell surface receptor for both Glial cell line-derived growth factor (GDNF), neurturin (NTN), and mediates activation of the RET tyrosine kinase receptor. The GFRA1 protein is a potent survival factor for central and peripheral neurons, and is vital for the development of kidneys and the enteric nervous system.

    • Synonyms

      GDNF family receptor alpha-1, GDNF receptor alpha-1, GDNFR-alpha-1, GFR-alpha-1, RET ligand 1, TGF-beta-related neurotrophic factor receptor 1, Gfra1, Gdnfra, Retl1, Trnr1.

    • 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

      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

    • Background

      What is the molecular weight/Mw of GFRA1 RAT Protein?
      GFRA1 RAT Protein has a total Mw of 72.3kDa.

      What is the source or expression system of GFRA1 RAT Protein?
      Sf9, Baculovirus cells.

      What is the Purity of GFRA1 RAT Protein?
      GFRA1 RAT Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GFRA1 RAT Protein?
      The biological functionality of GFRA1 RAT Protein will be determined in the future.

      What is the amino acid sequence of GFRA1 RAT Protein?
      DRLDCVKASD QCLKEQSCST KYRTLRQCVA GKETNFSLTS GLEAKDECRS AMEALKQKSL YNCRCKRGMK KEKNCLRIYW SMYQSLQGND LLEDSPYEPV NSRLSDIFRA VPFISDVFQQ VEHISKGNNC LDAAKACNLD DTCKKYRSAY ITPCTTSMSN EVCNRRKCHK ALRQFFDKVP AKHSYGMLFC SCRDIACTER RRQTIVPVCS YEERERPNCL SLQDSCKTNY ICRSRLADFF TNCQPESRSV SNCLKENYAD CLLAYSGLIG TVMTPNYVDS SSLSVAPWCD CSNSGNDLED CLKFLNFFKD NTCLKNAIQA FGNGSDVTMW QPAPPVQTTT ATTTTAFRVK NKPLGPAGSE NEIPTHVLPP CANLQAQKLK SNVSGSTHLC LSDSDFGKDG LAGASSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.

      What applications can GFRA1 RAT Protein be used in?
      GFRA1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GFRA1 RAT Protein?
      The endotoxin level is minimal, GFRA1 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.

    Gfra1 Rat
  • View Data Sheet

    Name :

    TROVE2 Human

    Description:

    TROVE Domain Family Member 2 Human Recombinant

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-329

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    Description

    RO-60 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 60kDa. RO60 is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 6M Urea, 500mM NaCl, 500mM imidazole and 10mM Tris pH-6.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      RO-60 although stable at 4°C for 3 weeks, should be stored below -18°C. Please prevent freeze-thaw cycles.

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

    Trove2 Human
  • View Data Sheet

    Name :

    CNPY4 Human

    Description:

    Canopy FGF Signaling Regulator 4 Human Recombinant

    PRAT4B, Protein canopy homolog 4, CNPY4.

    Product # :

    PRO-1976

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    Description

    CNPY4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (22-248 a.a) and having a molecular mass of 28.6kDa. CNPY4 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques..

    Source

    Escherichia Coli.

    Formulation

    CNPY4 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Canopy FGF Signaling Regulator 4 (CNPY4) is a part of the canopy family which owns one saposin B-type domain. CNPY4 takes part in the regulation process of the cell surface expression of TLR4.

    • Synonyms

      PRAT4B, Protein canopy homolog 4, CNPY4.

    • 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 MGSEFGMLKE EDDDTERLPS KCEVCKLLST ELQAELSRTG RSREVLELGQ VLDTGKRKRH VPYSVSETRL EEALENLCER ILDYSVHAER KGSLRYAKGQ SQTMATLKGL VQKGVKVDLG IPLELWDEPS VEVTYLKKQC ETMLEEFEDI VGDWYFHHQE QPLQNFLCEG HVLPAAETAC LQETWTGKEI TDGEEKTEGE EEQEEEEEEE EEEGGDKMTK TGSHPKLDRE DL.

    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.

    Cnpy4 Human
  • View Data Sheet

    Name :

    VTCN1 Human, Sf9

    Description:

    V-Set Domain Containing T Cell Activation Inhibitor 1 Human Recombinant, Sf9

    V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    Product # :

    PRO-2439

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    Description

    VTCN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 244 amino acids (25-259a.a.) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). VTCN1 is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VTCN1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      V-Set Domain Containing T Cell Activation Inhibitor 1, also known as VCTN1, is part of the B7 costimulatory protein family. Proteins in this family are located on the surface of antigen-presenting cells and interact with ligand bound to receptors on the surface of T cells. High level of the encoded protein has been associated with tumor progression. VCTN1 also takes part in promoting epithelial cell transformation.

    • Synonyms

      V-set domain-containing T-cell activation inhibitor 1, B7 homolog 4, B7-H4, B7h.5, Immune costimulatory protein B7-H4, Protein B7S1, T-cell costimulatory molecule B7x, B7H4, VTCN1, B7S1, B7X, PRO1291, RP11-229A19.4.

    • 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

      ADPLIIGFGI SGRHSITVTT VASAGNIGED GILSCTFEPD IKLSDIVIQW LKEGVLGLVH EFKEGKDELS EQDEMFRGRT AVFADQVIVG NASLRLKNVQ LTDAGTYKCY IITSKGKGNA NLEYKTGAFS MPEVNVDYNA SSETLRCEAP RWFPQPTVVW ASQVDQGANF SEVSNTSFEL NSENVTMKVV SVLYNVTINN TYSCMIENDI AKATGDIKVT ESEIKRRSHL QLLNSKASHH HHHH.

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

    Vtcn1 Protein
  • View Data Sheet

    Name :

    CRKL Human

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant

    Crk-like protein, CRKL.

    Product # :

    PRO-063

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    Description

    CRKL 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 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.

    • Synonyms

      Crk-like protein, CRKL.

    • 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 MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.

    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.

    CRKL Human
  • View Data Sheet

    Name :

    DHFR Human

    Description:

    Dihydrofolate Reductase Human Recombinant

    Dihydrofolate reductase, DHFR, DHFRP1.

    Product # :

    ENZ-443

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    Description

    DHFR Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6kDa.The DHFR is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHFR solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2000 pmol/min/ug  is defined as the amount of enzyme that converts 1.0 pmole of dihydrofolic acid to tetrahydrofolic acid per minute at pH 6.5 at 25C.

    sds-page

    dhfr-human-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on separate chromosomes.
      DHFR deficiency is associated with megaloblastic anemia.
      DHFR knockdown plays a role in the anticancer activity of 2-hydroxyoleic acid.
      DHFR gene insertion/deletion polymorphism is linked to variation in serum and red blood cell folate concentrations in women.

    • Synonyms

      Dihydrofolate reductase, DHFR, DHFRP1.

    • 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 MVGSLNCIVA VSQNMGIGKN GDLPWPPLRN EFRYFQRMTT TSSVEGKQNL VIMGKKTWFS IPEKNRPLKG RINLVLSREL KEPPQGAHFL SRSLDDALKL TEQPELANKV DMVWIVGGSS VYKEAMNHPG HLKLFVTRIM QDFESDTFFP EIDLEKYKLL PEYPGVLSDV QEEKGIKYKF EVYEKND.

    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.

    Dhfr Human
  • View Data Sheet

    Name :

    EG VEGF Mouse

    Description:

    Endocrine Gland Vascular Endothelial Growth Factor Mouse Recombinant

    PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    Product # :

    CYT-825

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    Description

    EG-VEGF Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 86 amino acids and having a molecular mass of 9.6kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS pH7.4 and 3% Trehalose.

    Purity

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

    Citations

    More Info

    • Introduction

      Endocrine gland-derived vascular endothelial growth factor (EG-VEGF) induces proliferation, migration, and fenestration in capillary endothelial cells derived from endocrine glands. Its expression is induced by hypoxia and is restricted to the steroidogenic glands (ovary, testis, adrenal, and placenta). Its expression is often complementary to the expression of VEGF (MIM 192240), suggesting that these molecules function in a coordinated manner. EG-VEGF potently contracts gastrointestinal (gi) smooth muscle. Induces proliferation, migration and fenestration (the formation of membrane discontinuities) in capillary endothelial cells derived from endocrine glands. Has little or no effect on a variety of other endothelial and non-endothelial cell types.

    • Synonyms

      PK1, Prokineticin 1, EG-VEGF, Prok1, Endocrine-gland-derived vascular endothelial growth factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized EG-VEGF Human Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EG-VEGF 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 Endocrine Gland Vascular Endothelial Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

    • Background

      What is the molecular weight/Mw of EG-VEGF Protein?
      EG-VEGF Protein has a total Mw of 9.6kDa.

      What is the source or expression system of EG-VEGF Protein?
      Escherichia Coli.

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

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

      What is the amino acid sequence of EG-VEGF Protein?
      AVITGACERD IQCGAGTCCA ISLWLRGLRL CTPLGREGEE CHPGSHKIPF LRKRQHHTCP CSPSLLCSRF PDGRYRCFRD LKNANF.

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

      What is the endotoxin level for EG-VEGF Protein?
      The endotoxin level is minimal, EG-VEGF 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.

    Eg Vegf Mouse
  • View Data Sheet

    Name :

    BLyS Human, His

    Description:

    B cell Activating Factor Human Recombinant, His Tag

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-545

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    Description

    BLyS Human Recombinant fused to His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (134-285 a.a.) and having a molecular mass of 21 kDa. BAFF is fused to a 38 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Recombinant His Tag BAFF contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BLyS-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      Binds to tnfrsf13b/taci and tnfrsf17/bcma. tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity. a third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • 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 KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 21kDa.

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

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

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

      What is the amino acid sequence of BLYS Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMAV QGPEETVTQD CLQLIADSET PTIQKGSYTF VPWLLSFKRG SALEEKENKI LVKETGYFFI YGQVLYTDKT YAMGHLIQRK KVHVFGDELS LVTLFRCIQN MPETLPNNSC YSAGIAKLEE GDELQLAIPR ENAQISLDGD VTFFGALKLL

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

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

    Blys Human His
  • View Data Sheet

    Name :

    ELAVL2 Human

    Description:

    ELAV Like Neuron-Specific RNA Binding Protein 2 Human Recombinant

    ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.

    Product # :

    PRO-2155

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    Description

    ELAVL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (1-346 a.a) and having a molecular mass of 40.4kDa. ELAVL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ELAVL2 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ELAV Like Neuron-Specific RNA Binding Protein 2, also known as ELAVL2 is a neural-specific RNA-binding protein which is recognized with his ability to bind to several 3' UTRs, as well as its own and in addition those of FOS and ID. ELAVL2 identify a GAAA motif in the RNA. One of the diseases associated with ELAVL2 is contagious pustular dermatitis.

    • Synonyms

      ELAV Like Neuron-Specific RNA Binding Protein 2, HUB, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2 (Hu Antigen B), Nervous System-Specific RNA-Binding Protein Hel-N1, Hu-Antigen B, HELN1, ELAV (Embryonic Lethal, Abnormal Vision, Drosophila)-Like 2, ELAV-Like Neuronal Protein 1 Isoform Hel-N2, ELAV-Like Neuronal Protein 1, ELAV-Like Protein 2, Hu Antigen B, HEL-N1, ELAV-like protein 2, ELAV-like neuronal protein 1, Hu-antigen B.

    • 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 MGSMETQLSN GPTCNNTANG PTTINNNCSS PVDSGNTEDS KTNLIVNYLP QNMTQEELKS LFGSIGEIES CKLVRDKITG QSLGYGFVNY IDPKDAEKAI NTLNGLRLQT KTIKVSYARP SSASIRDANL YVSGLPKTMT QKELEQLFSQ YGRIITSRIL VDQVTGISRG VGFIRFDKRI EAEEAIKGLN GQKPPGATEP ITVKFANNPS QKTNQAILSQ LYQSPNRRYP GPLAQQAQRF RFSPMTIDGM TSLAGINIPG HPGTGWCIFV YNLAPDADES ILWQMFGPFG AVTNVKVIRD FNTNKCKGFG FVTMTNYDEA AMAIASLNGY RLGDRVLQVS FKTNKTHKA.

    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.

    Elavl2 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.

    Citations

    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
  • View Data Sheet

    Name :

    ESM1 Human

    Description:

    Endothelial Cell-Specific Molecule 1 Human Recombinant

    Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

    Product # :

    PRO-1328

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    Description

    ESM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (20-184 a.a.) and having a molecular mass of 20.5kDa.ESM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ESM1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Endothelial cell-specific molecule 1 (ESM1) is a proteoglycan secreted by endothelial cells (mostly in the human lung and kidney tissues) and its mRNA expression is regulated by inflammatory cytokines. ESM1 has potent implications in lung endothelial cell-leukocyte interactions. In addition, ESM1 expression is detected in various epithelia and in adipocytes. ESM1 is involved in angiogenesis and it also promotes angiogenic sprouting. ESM1 expression is upregulated by TNF alpha, IL1 beta, or lipopolysaccharide and downregulated by IFN gamma. Genetically engineered cells overexpressing ESM1 induce tumor formation, implying that ESM1 might be involved in the pathophysiology of tumor growth in vivo.

    • Synonyms

      Endothelial cell-specific molecule 1, ESM-1, ESM1, endocan.

    • 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 MGSWSNNYAV DCPQHCDSSE CKSSPRCKRT VLDDCGCCRV CAAGRGETCY RTVSGMDGMK CGPGLRCQPS NGEDPFGEEF GICKDCPYGT FGMDCRETCN CQSGICDRGT GKCLKFPFFQ YSVTKSSNRF VSLTEHDMAS GDGNIVREEV VKENAAGSPV MRKWLNPR.

    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.

    Esm1 Human
  • View Data Sheet

    Name :

    PDGF AA Rat

    Description:

    Platelet-Derived Growth Factor AA Rat Recombinant

    Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.

    Product # :

    CYT-776

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    Description

    Platelet-derived Growth Factor AA Human Recombinant is a disulfide-linked homodimer Consists of two A chains containing 111 amino acids each and having a total molecular mass of 25.3KDa. PDGF-AA is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PDGF-AA was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH7.0.

    Purity

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

    Biological Activity

    The ED50, as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 5.0 ng/ml, corresponding to a specific activity of > 2.0 × 105 IU/mg.

    Citations

    More Info

    • Introduction

      PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGF is stored in platelet alpha-granules and released upon platelet activation. The PDGF is involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGF
      have been identified and named PDGFR-alpha and PDGFR-beta. PDGFR-alpha is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-beta interacts with only PDGF-BB and PDGF-AB.

    • Synonyms

      Platelet-derived growth factor subunit A, PDGF subunit A, PDGF-1, Platelet-derived growth factor A chain, Platelet-derived growth factor alpha polypeptide, Pdgfa, Rpa1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Platelet-derived Growth Factor AA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PDGF-AA 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 Platelet-derived Growth Factor-AA in Sterile 4mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MSIEEAIPAV CKTRTVIYEI PRSQVDPTSA NFLIWPPCVE VKRCTGCCNT SSVKCQPSRV HHRSVKVAKV EYVRKKPKLK EVQVRLEEHL ECACATSNLN PDHREEETDV R.

    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.

    Pdgf Aa Rat
  • View Data Sheet

    Name :

    FGF 9 Mouse

    Description:

    Fibroblast Growth Factor-9 Mouse Recombinant

    GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    Product # :

    CYT-349

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    Description

    Fibroblast Growth Factor-9 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids and having a molecular mass of 23308 Dalton.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from 10mM Tris, pH 8.0, 0.15M Amonium Sulfate.

    Purity

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

    Biological Activity

    The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

    Citations

    More Info

    • Introduction

      Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.

    • Synonyms

      GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Mouse Recombinant 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 Fibroblast Growth Factor 9 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 Pro-Leu-Gly-Glu-Val.

    • Background

      What is the molecular weight/Mw of FGF9 Protein?
      FGF9 Protein has a total Mw of 23.3kDa.

      What is the source or expression system of FGF9 Protein?
      Escherichia Coli.

      What is the Purity of FGF9 Protein?
      FGF9 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF9 Protein?
      The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.

      What is the amino acid sequence of FGF9 Protein?
      FGF9 Protein is composed from 205 amino acids.

      What applications can FGF9 Protein be used in?
      FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF9 Protein?
      The endotoxin level is minimal, FGF9 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.

    Fgf9 Mouse
  • View Data Sheet

    Name :

    FGF17 Mouse

    Description:

    Fibroblast Growth Factor 17 Mouse Recombinant

    Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    Product # :

    CYT-1123

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    Description

    Fibroblast Growth Factor 17 Mouse Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 194 amino acid and having a molecular mass of approximately 22.5kDa.FGF17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20 mM Tris-HCl, pH 8.0, 0.02 % Tween-20 and 700 mM NaCl.

    Purity

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

    Biological Activity

    The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10 μg/ml of heparin.

    Citations

    More Info

    • Introduction

      Fibroblast Growth Factor 17 (FGF17) is a part of the fibroblast growth factor family. FGF family members have broad mitogenic and cell survival activities, and are involved in various biological processes includingmorphogenesis, embryonic development cell growth, , tissue repair, tumor growth and invasion. The FGF17 gene is highly expressed in the cerebellum and cortex. The mouse homolog of the FGF17 gene is localized to specific sites in the midline structures of the forebrain, the midbrain-hindbrain junction, developing skeleton and developing arteries, suggesting a part in central nervous system, bone and vascular development.

    • Synonyms

      Fibroblast growth factor 17, FGF-17, FGF17, FGF-13, HH20.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FGF17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fibroblast Growth Factor 17 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 Fibroblast Growth Factor 17 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT.

    • Background

      What is the molecular weight/Mw of FGF17 MOUSE Protein?
      FGF17 MOUSE Protein has a total Mw of 22.5kDa.

      What is the source or expression system of FGF17 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of FGF17 MOUSE Protein?
      FGF17 MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF17 MOUSE Protein?
      The ED50 as determined by a cell proliferation assay using murine balb/c 3T3 cells is < 10 ng/ml, corresponding to a specific activity of > 1.0 × 105 IU/mg in the presence of 10 μg/ml of heparin.

      What is the amino acid sequence of FGF17 MOUSE Protein?
      TQGENHPSPN FNQYVRDQGA MTDQLSRRQI REYQLYSRTS GKHVQVTGRR ISATAEDGNK FAKLIVETDT FGSRVRIKGA ESEKYICMNK RGKLIGKPSG KSKDCVFTEI VLENNYTAFQ NARHEGWFMA FTRQGRPRQA SRSRQNQREA HFIKRLYQGQ LPFPNHAERQ KQFEFVGSAP TRRTKRTRRP QSQT.

      What applications can FGF17 MOUSE Protein be used in?
      FGF17 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF17 MOUSE Protein?
      The endotoxin level is minimal, FGF17 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.

    Fgf17 Mouse
  • View Data Sheet

    Name :

    CFL2 Human

    Description:

    Cofilin-2 Human Recombinant

    Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    Product # :

    PRO-912

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    Description

    CFL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-166 a.a.) and having a molecular mass of 20.9kDa.CFL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CFL2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CFL2 protein is a member of the actin-binding proteins ADF family which contains 1 ADF-H domain. Cofilin is a broadly distributed intracellular actin-modulating protein which binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Defects in the CFL2 gene are the cause of nemaline myopathy type 7 (NEM7).

    • Synonyms

      Cofilin-2, Cofilin- muscle isoform, CFL2, NEM7.

    • 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 MASGVTVNDE VIKVFNDMKV RKSSTQEEIK KRKKAVLFCL SDDKRQIIVE EAKQILVGDI GDTVEDPYTS FVKLLPLNDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKFTG IKHEWQVNGL DDIKDRSTLG EKLGGNVVVS LEGKPL.

    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.

    Cfl2 Human
  • View Data Sheet

    Name :

    GOT1 Human

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Human Recombinant

    EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    Product # :

    ENZ-528

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    Description

    GOT1 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GOT1 Human solution containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

    • Synonyms

      EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    • 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 MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.

    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.

    Got1 Human
  • View Data Sheet

    Name :

    RNF7 Human

    Description:

    Ring Finger Protein 7 Human Recombinant

    RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.

    Product # :

    PRO-1671

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    Description

    RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).

    • Synonyms

      RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.

    • 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 MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.

    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.

    Rnf7 Human
  • View Data Sheet

    Name :

    HCV NS3 47.8kDa

    Description:

    Hepatitis C Virus NS3 47.8kDa Recombinant

    Product # :

    HCV-010

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    Description

    Recombinant HCV NS3 Genotype 1a produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 47.8kDa and fused to a His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 1mg/ml in 20mM sodium carbonate pH-9.6.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HCV is a small 50nm, enveloped, single-stranded, positive sense RNAvirus in the family Flaviviridae.
      HCV has a high rate of replication with approximately one trillion particles produced each day in an infected individual. Due to lack of proofreading by the HCV RNA polymerase, the HCV has an exceptionally high mutation rate, a factor that may help it elude the host's immune response. Hepatitis C virus is classified into six genotypes(1-6) with several subtypes within each genotype. The preponderance and distribution of HCV genotypes varies globally. Genotype is clinically important in determining potential response to interferon-based therapy and the required duration of such therapy. Genotypes 1 and 4 are less responsive to interferon-based treatment than are the other genotypes (2, 3, 5 and 6).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      HCV NS3 although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized HCV NS3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Hcv Ns3 478Kda
  • View Data Sheet

    Name :

    GM- CSF Human, Sf9

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Human Recombinant, Sf9

    CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    Product # :

    CYT-416

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    Description

    GM-CSF Human Recombinant produced in insect cells is a single, glycosylated, polypeptide chain containing 127 amino acids (18-144) and having a molecular mass of 14.6kDa. GM-CSF is fused to a C-terminal His -tag (6x His) and purified by proprietary chromatographic techniques.

    Source

    Insect Cells.

    Formulation

    The protein was lyophilized with PBS.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    Citations

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GMCSF, Pluripoietin-alpha, Molgramostin, Sargramostim.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GMCSF 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 Granulocyte Macrophage Colony Stimulating Factor 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-Ala-Arg-Ser.

    • Background

      Recombinant Granulocyte-Macrophage Colony-Stimulating Factor (GMCSF) is a protein that plays a crucial role in the production and differentiation of white blood cells, including granulocytes and macrophages. It is a potent stimulator of hematopoietic stem cells, which are responsible for the production of all blood cells in the body. Recombinant GMCSF is a synthetic version of the protein that is produced using recombinant DNA technology.

      Recombinant GMCSF has been extensively studied for its potential therapeutic applications in a variety of medical conditions, including cancer, autoimmune diseases, and infectious diseases. In cancer, GMCSF is used as an immunostimulatory agent to enhance the immune response against cancer cells. By stimulating the production and differentiation of white blood cells, GM-CSF can increase the number of immune cells that can recognize and attack cancer cells. This approach has been successfully used in the treatment of several types of cancer, including melanoma and leukemia.

      In autoimmune diseases, recombinant GMCSF has been investigated as a potential treatment for conditions such as rheumatoid arthritis and multiple sclerosis. These diseases are characterized by an overactive immune response that attacks healthy tissues in the body. By modulating the immune response, GMCSF may be able to reduce inflammation and prevent further damage to affected tissues.

      In infectious diseases, recombinant GMCSF has been studied as a potential treatment for conditions such as sepsis and HIV/AIDS. In sepsis, a severe bacterial infection, GMCSF may be able to stimulate the production of white blood cells and improve the immune response against the infection. In HIV/AIDS, GMCSF may be able to enhance the immune response against the virus and reduce the risk of opportunistic infections.

      Recombinant GMCSF is typically administered by injection, either directly into the affected tissue or into the bloodstream. It is generally well-tolerated, although some patients may experience side effects such as fever, fatigue, and muscle pain.

      In conclusion, recombinant GMCSF is a promising therapeutic agent with potential applications in a variety of medical conditions. Its ability to stimulate the production and differentiation of white blood cells makes it a valuable tool in the treatment of cancer, autoimmune diseases, and infectious diseases. Ongoing research is likely to uncover new uses for this protein and further refine its therapeutic potential.

      What is the molecular weight/Mw of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of GM- CSF HUMAN, SF9 Protein?
      Insect Cells.
      What is the Purity of GM- CSF HUMAN, SF9 Protein?
      GM- CSF HUMAN, SF9 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM- CSF HUMAN, SF9 Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line) is < 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of GM- CSF HUMAN, SF9 Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Pro-Ala-Arg-Ser.

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

      What is the endotoxin level for GM- CSF HUMAN, SF9 Protein?
      The endotoxin level is minimal, GM- CSF HUMAN, SF9 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.

    Gm Csf Human Sf9
  • View Data Sheet

    Name :

    SSX1 Human

    Description:

    Synovial Sarcoma, X Breakpoint 1 Human Recombinant

    Synovial Sarcoma X Breakpoint 1, Cancer/Testis Antigen 5.1, CT5.1, SSRC Sarcoma Synovial X-Chromosome-Related 1, Cancer/Testis Antigen Family 5 Member 1, Cancer/Testis Antigen Family 5, Protein SSX1, Member 1, SSX1.

    Product # :

    PRO-1379

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    Description

    SSX1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (1-188 a.a) and having a molecular mass of 24.3kDa.SSX1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SSX1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synovial Sarcoma, X Breakpoint 1 (SSX1) is a member of a family of highly homologous synovial sarcoma X (SSX) breakpoint proteins. SSX proteins are localized to the nucleus and expressed in testis and some types of cancers and, hence, they are classified as C/T (cancer/testis) antigens. These proteins may serve as transcriptional repressors. SSX1 genes are involved in the t (X;18) translocation typically found in all synovial sarcomas. This translocation leads to the fusion of the synovial sarcoma translocation gene on chromosome 18 to one of the SSX genes on chromosome X. These hybrid proteins are most likely responsible for transforming activity.

    • Synonyms

      Synovial Sarcoma X Breakpoint 1, Cancer/Testis Antigen 5.1, CT5.1, SSRC Sarcoma Synovial X-Chromosome-Related 1, Cancer/Testis Antigen Family 5 Member 1, Cancer/Testis Antigen Family 5, Protein SSX1, Member 1, SSX1.

    • 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 MGSMNGDDTF AKRPRDDAKA SEKRSKAFDD IATYFSKKEW KKMKYSEKIS YVYMKRNYKA MTKLGFKVTL PPFMCNKQAT DFQGNDFDND HNRRIQVEHP QMTFGRLHRI IPKIMPKKPA EDENDSKGVS EASGPQNDGK QLHPPGKANI SEKINKRSGP KRGKHAWTHR LRERKQLVIY EEISDPEEDD E.

    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.

    Ssx1 Human
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