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Search results

1000 results found for “activating transcription factor”

Name

Description

Product #

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  • View Data Sheet

    Name :

    KLK10 Human, Sf9

    Description:

    Kallikrein-10 Human Recombinant, Sf9

    Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    Product # :

    ENZ-1090

    Price :

    Quantity :

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    • source
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    • Citations

    Description

    KLK10 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 252 amino acids (34-276 a.a) and having a molecular mass of 27.8kDa. KLK10 protein is fused to a 6 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK10 protein solution (0.5mg/ml) contains 30% glycerol, 20mM Tris-HCl (pH 8.0), 0.15M NaCl & 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kallikrein-10 (KLK10) is one of the 15 kallikrein subfamily members located in a cluster on chromosome 19. Kallikreins are a subgroup of serine proteases having various physiological functions. KLK10 is secreted and has a role in suppression of tumorigenesis in breast and prostate cancers.

    • Synonyms

      Kallikrein-Related Peptidase 10, KLK10, PRSSL1, NES1, Normal Epithelial Cell-Specific 1, Protease Serine-Like 1, Kallikrein 10, Breast Normal Epithelial Cell Associated Serine Protease, kallikrein-10, Protease, Serine-Like 1, EC 3.4.21.- , EC 3.4.21, EC 3.4.21.74.

    • 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

      ADPALLPQND TRLDPEAYGS PCARGSQPWQ VSLFNGLSFH CAGVLVDQSW VLTAAHCGNK PLWARVGDDH LLLLQGEQLR RTTRSVVHPK YHQGSGPILP RRTDEHDLML LKLARPVVLG PRVRALQLPY RCAQPGDQCQ VAGWGTTAAR RVKYNKGLTC SSITILSPKE CEVFYPGVVT NNMICAGLDR GQDPCQSDSG GPLVCDETLQ GILSWGVYPC GSAQHPAVYT QICKYMSWIN KVIRSNHHHH HH.

    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.

    Kallikrein 10
  • View Data Sheet

    Name :

    tPA Human

    Description:

    Tissue Plasminogen Activator Human Recombinant

    Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    Product # :

    ENZ-263

    Price :

    Quantity :

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    Description

    Tissue Plasminogen Activator Human Recombinant produced in CHO cells is a single, glycosylated polypeptide chain containing 527 amino acids and having a molecular mass of 59008.71 Dalton. tPA is a serine protease enzyme that converts plasminogen to plasmin. The tPA is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells (CHO)

    Formulation

    Each mg of t-PA contains 1.7 gr L-arginine, 0.5 gr phosphoric acid and 4 mg tween 80.

    Purity

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

    Citations

    More Info

    • Introduction

      Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
      This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.

    • Synonyms

      Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Enzymatic Activity

      580,000 IU/mg.

    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.

    T Pa Human
  • View Data Sheet

    Name :

    THG1L Human

    Description:

    tRNA-Histidine Guanylyltransferase 1-Like Human Recombinant

    tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.

    Product # :

    ENZ-639

    Price :

    Quantity :

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    • Citations

    Description

    THG1L Human Recombinant produced in E. coli is a single polypeptide chain containing 292 amino acids (30-298) and having a molecular mass of 34.0 kDa.THG1L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The THG1L solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Probable tRNA (His) guanylyltransferase (THG1L) is a member of the tRNA (His) gyanylytransferase family. THG1L which is localized to the cytoplasm also found adjacent to the nuclear membrane and expressed in various tissues, including liver and lung. THG1L is expressed in a cell cycle-dependent manner and may be involved in cell cycle progression and cell proliferation. THG1L adds a GMP to the 5'-end of tRNA(His) after transcription and RNase P cleavage. This step is vital for accurate recognition of the tRNA and for the fidelity of protein synthesis. Upon DNA damage, THG1L is phosphorylated, presumably by ATM or ATR.

    • Synonyms

      tRNA-histidine guanylyltransferase 1-like (S. cerevisiae), Interphase cytoplasmic foci protein 45, probable tRNA(His) guanylyltransferase, induced by high glucose-1, FLJ11601, FLJ20546, ICF45, IHG-1, EC 2.7.7.79, EC 2.7.7.6.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAKSKFE YVRDFEADDT CLAHCWVVVR LDGRNFHRFA EKHNFAKPND SRALQLMTKC AQTVMEELED IVIAYGQSDE YSFVFKRKTN WFKRRASKFM THVASQFASS YVFYWRDYFE DQPLLYPPGF DGRVVVYPSN QTLKDYLSWR QADCHINNLY NTVFWALIQQ SGLTPVQAQG RLQGTLAADK NEILFSEFNI NYNNELPMYR KGTVLIWQKV DEVMTKEIKL PTEMEGKKMA VTRTRTKPVP LHCDIIGDAF WKEHPEILDE DS.

    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.

    Thg1L Human
  • View Data Sheet

    Name :

    CD80 Human

    Description:

    CD80 Human Recombinant

    CD80 Molecule, CD80 Antigen (CD28 Antigen Ligand 1, B7-1 Antigen), B-Lymphocyte Activation Antigen B7, CTLA-4 Counter-Receptor B7.1, Activation B7-1 Antigen, CD28LG1, CD28LG, LAB7, BB1, B7, Costimulatory Molecule Variant IgV-CD80, T-Lymphocyte Activation Antigen CD80, Costimulatory Factor CD80, CD80 Antigen, B7-1, B7.1.

    Product # :

    PRO-2473

    Price :

    Quantity :

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    • description
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    • Citations

    Description

    CD80 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 216 amino acids (35-242a.a.) and having a molecular mass of 24.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD80 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CD80 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

      CD80 which is a member of cell surface immunoglobulin superfamily takes part in the costimulatory signal essential for T-lymphocyte activation. CD80 binds to either human or mouse CD28 and CTLA-4 – binding to CD28 induces T-cell proliferation and cytokine production while binding to CTLA-4 inhibits T-cell activation. CD80 is expressed on activated B cells, activated T cells, and macrophages.

    • Synonyms

      CD80 Molecule, CD80 Antigen (CD28 Antigen Ligand 1, B7-1 Antigen), B-Lymphocyte Activation Antigen B7, CTLA-4 Counter-Receptor B7.1, Activation B7-1 Antigen, CD28LG1, CD28LG, LAB7, BB1, B7, Costimulatory Molecule Variant IgV-CD80, T-Lymphocyte Activation Antigen CD80, Costimulatory Factor CD80, CD80 Antigen, B7-1, B7.1.

    • 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

      VIHVTKEVKE VATLSCGHNV SVEELAQTRI YWQKEKKMVL TMMSGDMNIW PEYKNRTIFD ITNNLSIVIL ALRPSDEGTY ECVVLKYEKD AFKREHLAEV TLSVKADFPT PSISDFEIPT SNIRRIICST SGGFPEPHLS WLENGEELNA INTTVSQDPE TELYAVSSKL DFNMTTNHSF MCLIKYGHLR VNQTFNWNTT KQEHFPDNLE HHHHHH.

    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.

    Cd80 Human
  • View Data Sheet

    Name :

    CXCL8 Macaque

    Description:

    Interleukin-8 Rhesus Macaque Recombinant

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

    Product # :

    CHM-004

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    Description

    IL 8 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa.The IL 8 Rhesus Macaque is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-8 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 IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

    • Background

      What is the molecular weight/Mw of CXCL8 MACAQUE Protein?
      CXCL8 MACAQUE Protein has a total Mw of 9.1kDa.

      What is the source or expression system of CXCL8 MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CXCL8 MACAQUE Protein?
      CXCL8 MACAQUE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 MACAQUE Protein?
      Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

      What is the amino acid sequence of CXCL8 MACAQUE Protein?
      AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

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

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

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

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

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

    Il 8 Rhesus Macaque
  • View Data Sheet

    Name :

    PON1 Human (170-232)

    Description:

    Paraoxonase-1 (170-232) Human Recombinant

    Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    Product # :

    ENZ-1198

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    Description

    The PON1 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The PON1 His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 63 amino acid residues of the PON1 Human, 170-232 amino acids.

    Source

    Escherichia Coli.

    Formulation

    Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      Serum paraoxonase, arylesterase 1, EC 3.1.1.2, EC 3.1.8.1, PON 1.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized PON1 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 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile!

      Please filter the product by an appropriate sterile filter before using it on cell culture.

    • Background

      PON1takes part in the detoxification of organophosphate insecticides such as parathion.

      PON1 is related to high-density lipoprotein (HDL) in the plasma and takes an important part in lipid metabolism and antioxidant defense.

      PON1 was first known for its ability to protect against oxidative stress and hydrolyze organophosphates.

      PON1 reduces oxidative stress by preventing the oxidation of lipids in LDL particles, which is extremely important in mitigating atherosclerosis and other cardiovascular diseases.

      PON1 has anti-inflammatory effects which help reduce inflammatory markers in different disease states.

      PON1 takes part in cholesterol metabolism, influencing the stability and formation of HDL particles, which are vital for lipid transport and reverse cholesterol efflux.

    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.

    Paraoxonase 1 Human
  • View Data Sheet

    Name :

    GUK1 Human, Active

    Description:

    Guanylate Kinase 1 Human Recombinant, Active

    GMK, GMP kinase.

    Product # :

    PKA-309

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    Description

    GUK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (1-197 a.a.)and having a total molecular mass of 23.9 kDa. GUK1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GUK1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 units/mg and is defined as the amount of enzyme that convert 1.0 umole of GMP and ATP to GDP and ADP per minute at pH 7.5 at 37C in coupled system with PK/LDH.

    Citations

    More Info

    • Introduction

      GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.

    • Synonyms

      GMK, GMP kinase.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA.

    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.

    Guk1 Human Active
  • View Data Sheet

    Name :

    CD247 Human, Sf9

    Description:

    CD247 Human Recombinant, Sf9

    CD247 Molecule, T-Cell Surface Glycoprotein CD3 Zeta Chain, T-Cell Receptor T3 Zeta Chain, CD247 Antigen, CD3Z, TCRZ, T3Z, T-Cell Antigen Receptor Complex, Zeta Subunit Of CD3, CD3Z Antigen, Zeta Polypeptide (TiT3 Complex), CD3z Antigen, Zeta Polypeptide (TiT3 Complex) , CD247 Antigen, Zeta Subunit , TCR Zeta Chain, CD3zeta Chain, CD3-ZETA, IMD25, CD3H, CD3Q.    

    Product # :

    PRO-2529

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    Description

    CD247 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 122 amino acids (52-164a.a.) and having a molecular mass of 14.1kDa. (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). CD247 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD247 protein solution (0.2mg/ml) contains 20mM Tris-HCl buffer (pH 6.8), 50% glycerol, 1mM DTT, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      T-cell surface glycoprotein CD3 zeta chain (CD247) is a member of the CD3Z/FCER1G family. CD247 is T-cell receptor zeta, which along with T-cell receptor alpha/beta and gamma/delta heterodimers, and also with CD3-gamma, -delta and -epsilon, creates the T-cell receptor-CD3 complex. The zeta chain has a central role in coupling antigen recognition to several intracellular signal-transduction pathways. Low expression of the CD247 antigen causes impaired immune response.

    • Synonyms

      CD247 Molecule, T-Cell Surface Glycoprotein CD3 Zeta Chain, T-Cell Receptor T3 Zeta Chain, CD247 Antigen, CD3Z, TCRZ, T3Z, T-Cell Antigen Receptor Complex, Zeta Subunit Of CD3, CD3Z Antigen, Zeta Polypeptide (TiT3 Complex), CD3z Antigen, Zeta Polypeptide (TiT3 Complex) , CD247 Antigen, Zeta Subunit , TCR Zeta Chain, CD3zeta Chain, CD3-ZETA, IMD25, CD3H, CD3Q.

    • 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

      ADPRVKFSRS ADAPAYQQGQ NQLYNELNLG RREEYDVLDK RRGRDPEMGG KPQRRKNPQE GLYNELQKDK MAEAYSEIGM KGERRRGKGH DGLYQGLSTA TKDTYDALHM QALPPRHHHH HH

    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.

    Cd247 Protein
  • View Data Sheet

    Name :

    UBE2E1 Human

    Description:

    Ubiquitin Conjugating Enzyme E2E1 Human Recombinant

    Ubiquitin carrier protein E1, Ubiquitin-conjugating enzyme E2E 1 (homologous to yeast UBC4/5), Ubiquitin-protein ligase E1, UBCH6, EC 6.3.2.19.

    Product # :

    ENZ-647

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    Description

    UBE2E1 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (1-193) and having a molecular mass of 23.8 kDa.UBE2E1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The UBE2E1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UBE2E1 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2E1 accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. UBE2E1 catalyzes the covalent attachment of ISG15 to other proteins. UBE2E1 mediates the selective degradation of short-lived and abnormal proteins. In vitro, UBE2E1 also catalyzes 'Lys-48'-linked polyubiquitination.

    • Synonyms

      Ubiquitin carrier protein E1, Ubiquitin-conjugating enzyme E2E 1 (homologous to yeast UBC4/5), Ubiquitin-protein ligase E1, UBCH6, EC 6.3.2.19.

    • 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 MGSMSDDDSR ASTSSSSSSS SNQQTEKETN TPKKKESKVS MSKNSKLLST SAKRIQKELA DITLDPPPNC SAGPKGDNIY EWRSTILGPP GSVYEGGVFF LDITFTPEYP FKPPKVTFRT RIYHCNINSQ GVICLDILKD NWSPALTISK VLLSICSLLT DCNPADPLVG SIATQYMTNR AEHDRMARQW TKRYAT

    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.

    Ube2E1 Human
  • View Data Sheet

    Name :

    IL5 Mouse, Sf9

    Description:

    Interleukin-5 Mouse Recombinant, Sf9

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

    Product # :

    CYT-1195

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

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    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    • Background

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

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

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

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

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

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

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

      Who supplies recombinant IL 5 MOUSE, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL 5 MOUSE, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 5 Mouse
  • View Data Sheet

    Name :

    CD247 Human

    Description:

    CD247 Human Recombinant

    T-cell surface glycoprotein CD3 zeta chain, T-cell receptor T3 zeta chain, CD247, CD3Z, T3Z, TCRZ, CD3H, CD3Q, CD3-ZETA.

    Product # :

    PRO-1335

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    Description

    CD247 Human Recombinant produced in E. coli is a single polypeptide chain containing 136 amino acids (52-164) and having a molecular mass of 15.4kDa.CD247 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CD247 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      T-cell surface glycoprotein CD3 zeta chain (CD247) is a member of the CD3Z/FCER1G family. CD247 is T-cell receptor zeta, which along with T-cell receptor alpha/beta and gamma/delta heterodimers, and also with CD3-gamma, -delta and -epsilon, creates the T-cell receptor-CD3 complex. The zeta chain has a central role in coupling antigen recognition to several intracellular signal-transduction pathways. Low expression of the CD247 antigen causes impaired immune response.

    • Synonyms

      T-cell surface glycoprotein CD3 zeta chain, T-cell receptor T3 zeta chain, CD247, CD3Z, T3Z, TCRZ, CD3H, CD3Q, CD3-ZETA.

    • 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 MGSRVKFSRS ADAPAYQQGQ NQLYNELNLG RREEYDVLDK RRGRDPEMGG KPQRRKNPQE GLYNELQKDK MAEAYSEIGM KGERRRGKGH DGLYQGLSTA TKDTYDALHM QALPPR.

    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.

    Cd247 Human
  • View Data Sheet

    Name :

    TARS Human

    Description:

    Threonyl-tRNA Synthetase Human Recombinant

    Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    Product # :

    ENZ-571

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    Description

    TARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 743 amino acids (1-723) and having a molecular mass of 85.6kDa.TARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 150mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Threonyl-tRNA synthetase, cytoplasmic (TARS) is a member of the class-II aminoacyl-tRNA synthetase family. The main role of TARS is in tRNA aminoacylation. The N-terminal domain of the TARS enzyme is responsible for the competition with the ribosome whereas the catalytic and the C-terminal domain are involved in binding the 2 anticodon arm-like structures in the operator.

    • Synonyms

      Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.

    • 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 MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP
      GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF.

    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.

    Tars Human
  • View Data Sheet

    Name :

    GARS Human

    Description:

    Glycyl-TRNA Synthetase Human Recombinant

    Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

    Product # :

    ENZ-805

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    Description

    GARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 270 amino acids (43-289 a.a) and having a molecular mass of 30kDa.GARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GARS protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GARS is an (alpha)2 dimer which is a member of the class II family of tRNA synthetases. GARS is a glycyl-tRNA synthetase, one of the aminoacyl-tRNA synthetases which charge tRNAs with their cognate amino acids. GARS catalyzes the attachment of glycine to tRNA(Gly). In addition, GARS is able to produce diadenosine tetraphosphate (Ap4A), which is a universal pleiotropic signaling molecule required for cell regulation pathways, by direct condensation of two ATPs. GARS has been demonstrated to be a target of autoantibodies in the human autoimmune diseases, polymyositis or dermatomyositis.

    • Synonyms

      Glycine--tRNA ligase, Diadenosine tetraphosphate synthetase, AP-4-A synthetase, Glycyl-tRNA synthetase, GlyRS, GARS, CMT2D, DSMAV, HMN5, SMAD1.

    • 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 MGSPISLPAA ASRSSMDGAG AEEVLAPLRL AVRQQGDLVR KLKEDKAPQV DVDKAVAELK ARKRVLEAKE LALQPKDDIV DRAKMEDTLK RRFFYDQAFA IYGGVSGLYD FGPVGCALKN NIIQTWRQHF IQEEQILEID CTMLTPEPVL KTSGHVDKFA DFMVKDVKNG ECFRADHLLK AHLQKLMSDK KCSVEKKSEM ESVLAQLDNY GQQELADLFV NYNVKSPITG NDLSPPVSFN LMFKTFIGPG.

    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.

    Glycyl Trna Synthetase Human
  • View Data Sheet

    Name :

    OPG Mouse

    Description:

    Osteoprotegerin Mouse Recombinant

    Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.

    Product # :

    CYT-956

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    Description

    OPG Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 388 amino acids (22-401a.a.) and having a molecular mass of 44.4kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).OPG is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 11B, Ocif, Opg, Tnfrsf11b, Osteoclastogenesis inhibitory factor, TR1.

    • 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

      ETLPPKYLHY DPETGHQLLC DKCAPGTYLK QHCTVRRKTL CVPCPDHSYT DSWHTSDECV YCSPVCKELQ SVKQECNRTH NRVCECEEGR YLEIEFCLKH RSCPPGSGVV QAGTPERNTV CKKCPDGFFS GETSSKAPCI KHTNCSTFGL LLIQKGNATH DNVCSGNREA TQKCGIDVTL CEEAFFRFAV PTKIIPNWLS VLVDSLPGTK VNAESVERIK RRHSSQEQTF QLLKLWKHQN RDQEMVKKII QDIDLCESSV QRHLGHSNLT TEQLLALMES LPGKKISPEE IERTRKTCKS SEQLLKLLSL WRIKNGDQDT LKGLMYALKH LKTSHFPKTV THSLRKTMRF LHSFTMYRLY QKLFLEMIGN QVQSVKISCL LEHHHHHH.

    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.

    Opg Mouse
  • View Data Sheet

    Name :

    ARSG Human

    Description:

    Arylsulfatase G Human Recombinant

    Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    Product # :

    ENZ-677

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    Description

    ARSG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 532 amino acids (17-525) and having a molecular mass of 57kDa.ARSG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Arylsulfatase G (ARSG) is a member of the sulfatase enzyme family. Sulfatases are enzymes which hydrolyze sulfate esters from sulfated steroids, carbohydrates, proteoglycans, and glycolipids. Sulfatases are involved in hormone biosynthesis, modulation of cell signaling, and degradation of macromolecules. The ARSG protein exhibits arylsulfatase activity at acidic pH, as is characteristic of lysosomal sulfatases. The Arylsulfatase G enzyme localizes in the lysosomes. ARSG is inhibited by phosphate, which forms a covalent bond with the active site 3-oxoalanine. Arylsulfatase G is widely expressed, having very low expression in the brain, lung, heart and skeletal muscle.

    • Synonyms

      Arylsulfatase G, ASG, ARSG, KIAA1001, UNQ839/PRO1777.

    • 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 MGSGFLYPLV DFCISGKTRG QKPNFVIILA DDMGWGDLGA NWAETKDTAN LDKMASEGMR FVDFHAAAST CSPSRASLLT GRLGLRNGVT RNFAVTSVGG LPLNETTLAE VLQQAGYVTG IIGKWHLGHH GSYHPNFRGF DYYFGIPYSH DMGCTDTPGY NHPPCPACPQ GDGPSRNLQR DCYTDVALPL YENLNIVEQP VNLSSLAQKY AEKATQFIQR ASTSGRPFLL YVALAHMHVP LPVTQLPAAP RGRSLYGAGL WEMDSLVGQI KDKVDHTVKE NTFLWFTGDN GPWAQKCELA GSVGPFTGFW QTRQGGSPAK QTTWEGGHRV PALAYWPGRV PVNVTSTALL SVLDIFPTVV ALAQASLPQG RRFDGVDVSE VLFGRSQPGH RVLFHPNSGA AGEFGALQTV RLERYKAFYI TGGARACDGS TGPELQHKFP LIFNLEDDTA EAVPLERGGA EYQAVLPEVR KVLADVLQDI ANDNISSADY TQDPSVTPCC NPYQIACRCQ AA.

    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.

    Arsg Human
  • View Data Sheet

    Name :

    NAT1 Human

    Description:

    N-Acetyltransferase 1 Human Recombinant

    N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.

    Product # :

    ENZ-144

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    Description

    NAT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 310 amino acids (1-290) and having a molecular mass of 36.1 kDa.The NAT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAT1 protein 0.5mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 2mM DTT and 10% Glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NAT1 is a member of the arylamine N-acetyltransferase family. NAT1 catalyzes N- or O-acetylation of heterocyclic and arylamine substrates in the detoxification of a large number of drugs. Several alleles triggering high levels of N-acetyltransferase activity were linked to colon and urinary bladder cancers, since NAT1 also bioactivate numerous known carcinogens. NAT1 aids metabolize drugs and other xenobiotics, and takes part in the detoxification of a plethora of hydrazine and arylamine drugs.

    • Synonyms

      N-acetyltransferase 1 (arylamine N-acetyltransferase), AAC1, Arylamide acetylase 1, Monomorphic arylamine N-acetyltransferase, MNAT, NAT-1.

    • Physical Appearance

      NAT1 is supplied as a 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 MDIEAYLERI GYKKSRNKLD LETLTDILQH QIRAVPFENL NIHCGDAMDL GLEAIFDQVV RRNRGGWCLQ VNHLLYWALT TIGFETTMLG GYVYSTPAKK YSTGMIHLLL QVTIDGRNYI VDAGFGRSYQ MWQPLELISG KDQPQVPCIF RLTEENGFWY LDQIRREQYI PNEEFLHSDL LEDSKYRKIY SFTLKPRTIE DFESMNTYLQ TSPASVFTSK SFCSLQTPDG VHCLVGFTLT HRRFNYKDNT DLIEFKTLSE EEIEKVLKNI FNISLQRKLV PKHGDRFFTI

    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.

    Nat1 Human
  • View Data Sheet

    Name :

    IL7 Human, His

    Description:

    Interleukin-7 Human Recombinant, His Tag

    Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    Product # :

    CYT-485

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    Description

    IL-7 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 152 amino acids fragment (26-177) and having a total molecular mass of 21.97 kDa with an amino-terminal hexahistidine tag. The IL-7 His-Tag protein is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Interleukin -7 His is supplied in 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Interleukin-7 is a potent lymphoid cell growth factor produced primarily by stromal cells.
      IL-7 has been shown to support the proliferation and differentiation of pre B- and early T cells as well as displaying a biological effect on cells of NK and myeloid lineages.

    • Synonyms

      Lymphopoietin 1 (LP-1), pre-B cell factor, IL-7.

    • 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. Please avoid freeze thaw cycles.

    • Background

      What is the molecular weight/Mw of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein has a total Mw of 21.97kDa.

      What is the source or expression system of IL7 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of IL7 HUMAN, HIS Protein?
      IL7 HUMAN, HIS Protein is composed from 152 amino acids.

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

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

      Who supplies recombinant IL7 HUMAN, HIS that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL7 HUMAN, HIS?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 7 Human His
  • View Data Sheet

    Name :

    CXCL8 Human, Pichia

    Description:

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

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

    Product # :

    CHM-349

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    Description

    Interleukin-8 Human Recombinant produced in Yeast is a single, glycosylated polypeptide chain containing 79 amino acids and having a molecular mass of 9 kDa. The IL-8 is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium phosphate buffer pH-8.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Chemotactic activity was reached at 25ng/ml on human neutrophils.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Background

      What is the molecular weight/Mw of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein has a total Mw of 9kDa.

      What is the source or expression system of CXCL8 HUMAN, PICHIA Protein?
      Pichia Pastoris.

      What is the Purity of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL8 HUMAN, PICHIA Protein?
      Chemotactic activity was reached at 25ng/ml on human neutrophils.

      What is the amino acid sequence of CXCL8 HUMAN, PICHIA Protein?
      CXCL8 HUMAN, PICHIA Protein is composed from 79 amino acids.

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

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

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

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

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

    Il 8 77 Human Pichia
  • View Data Sheet

    Name :

    p38a/SAPK2 Human

    Description:

    p38a/SAPK2 Human Recombinant

    Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    Product # :

    PKA-217

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    Description

    p38/SAPK2 is a non-glycosilated polypeptide produced by phosphorylation of the purified p38 alpha with MKK6 having a molecular mass of 42.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    p38/SAPK2 is supplied in 25mM Tris-HCl, 150mM NaCl, 1mM DTT, 50% glycerol, pH 8.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      p38a/SAPK2 is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various environmental stresses and proinflammatory cytokines. The activation requires its phosphorylation by MAP kinase kinases (MKKs), or its autophosphorylation triggered by the interaction of MAP3K7IP1/TAB1 protein with this kinase. The substrates of this kinase include transcription regulator ATF2, MEF2C, and MAX, cell cycle regulator CDC25B, and tumor suppressor p53, which suggest the roles of this kinase in stress related transcription and cell cycle regulation, as well as in genotoxic stress response. Four alternatively spliced transcript variants of this gene encoding distinct isoforms have been reported.

    • Synonyms

      Mitogen-activated protein kinase 14, EC 2.7.11.24, Mitogen-activated protein kinase p38 alpha, MAP kinase p38 alpha, Cytokine suppressive anti-inflammatory drug-binding protein, CSAID-binding protein, CSBP, MAX-interacting protein 2, MAP kinase MXI2, SAPK2A, RK, p38, EXIP, Mxi2, CSBP1, CSBP2, CSPB1, PRKM14, PRKM15, p38ALPHA.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Unit Definition

      No protease activity detectable, specific activity is 2.357.900 U*/mg (*1 U = 1 pmol/min transferred to myelin basic protein at 30°C).

    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.

    P38Alpha Human
  • View Data Sheet

    Name :

    KLRC3 Human

    Description:

    Killer Cell Lectin-Like Receptor Subfamily C, Member 3 Human Recombinant

    Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.

    Product # :

    PRO-1230

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    Description

    KLRC3 Human Recombinant produced in E. coli is a single polypeptide chain containing 171 amino acids (94-240) and having a molecular mass of 19.0 kDa.KLRC3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The KLRC3 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      KLRC3 belongs to the NKG2 group that can be found mostly in natural killer (NK) cells and encodes a family of transmembrane proteins known for their C-type lectin domain and their type II membrane orientation (extracellular C terminus). The NKG2 gene family is situated inside the NK complex, a region which has quite a few C-type lectin genes mostly expressed on NK cells.

    • Synonyms

      Killer Cell Lectin-Like Receptor Subfamily C Member 3, NK Cell Receptor E, NKG2-E Type II Integral Membrane Protein, NKG2-E-Activating NK Receptor, NKG2E.

    • 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 MGSMIPFLEQ NNSSPNTRTQ KARPCGHCPE EWITYSNSCY YIGKERRTWE ESLQACASKN SSSLLSIDNE EEMKFLASIL PSSWIGVFRN SSHHPWVTIN GLAFKHEIKD SDHAERNCAM LHVRGLISDQ CGSSRIIRRG FIMLTRLVLN S

    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.

    Klrc3 Human
  • View Data Sheet

    Name :

    CD96 Human

    Description:

    CD96 Human Recombinant

    CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.

    Product # :

    PRO-2445

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    Description

    CD96 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 490 amino acids (22-503a.a.) and having a molecular mass of 54.6kDa.CD96 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CD96 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CD96 is a type I membrane protein which is a part of the immunoglobulin superfamily. CD96 functions as cell markers in immune-phynotyping and participates in antigen presentation. CD96 plays a role in the adhesive interactions of activated T and NK cells through the late phase of the immune response.

    • Synonyms

      CD96 Molecule, T Cell-Activated Increased Late Expression Protein, Cell Surface Antigen CD96, CD96 Antigen, T Cell Activation, Increased Late Expression, T-Cell Surface Protein Tactile, TACTILE.

    • 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

      VWEKTVNTEE NVYATLGSDV NLTCQTQTVG FFVQMQWSKV TNKIDLIAVY HPQYGFYCAY GRPCESLVTF TETPENGSKW TLHLRNMSCS VSGRYECMLV LYPEGIQTKI YNLLIQTHVT ADEWNSNHTI EIEINQTLEI PCFQNSSSKI SSEFTYAWSV EDNGTQETLI SQNHLISNST LLKDRVKLGT DYRLHLSPVQ IFDDGRKFSC HIRVGPNKIL RSSTTVKVFA KPEIPVIVEN NSTDVLVERR FTCLLKNVFP KANITWFIDG SFLHDEKEGI YITNEERKGK DGFLELKSVL TRVHSNKPAQ SDNLTIWCMA LSPVPGNKVW NISSEKITFL LGSEISSTDP PLSVTESTLD TQPSPASSVS PARYPATSSV TLVDVSALRP NTTPQPSNSS MTTRGFNYPW TSSGTDTKKS VSRIPSETYS SSPSGAGSTL HDNVFTSTAR AFSEVPTTAN GSTKTNHVHI TGIVVNKPKD GMLEHHHHHH.

    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.

    Cd96 Human
  • View Data Sheet

    Name :

    GLO1 Human, Active

    Description:

    Glyoxalase-I Human Recombinant, Active

    GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    Product # :

    ENZ-999

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    Description

    Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 400 units/mg. One unit will form 1.0umol of S-lactoylgutathione from methylglyoxal and reduced glutathione per minute at pH6.5 at 25C

    Citations

    More Info

    • Introduction

      GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

    • Synonyms

      GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

    • 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

      MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.

    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.

    Glo1 Human Active
  • View Data Sheet

    Name :

    IRF5 Human

    Description:

    IFN Regulatory Factor-5 Human Recombinant

    IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    Product # :

    CYT-816

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • More Info
    • SDS-PAGE
    • Citations

    Description

    IRF5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (176-240a.a) and having a molecular mass of 10.7kDa.IRF5 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IRF5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    SDS-PAGE

    IRF5 Human - Product image 1

    Citations

    More Info

    • Introduction

      IFN Regulatory Factor-5, also known as IRF5 belongs to the IFN regulatory factor (IRF) family, a group of transcription factors with various functions, including virus-mediated activation of IFN, and modulation of cell growth, differentiation, apoptosis, and immune system activity. Members of the IRF family are characterized by a conserved N-terminal DNA-binding domain containing tryptophan (W) repeats. Multiple transcript variants encoding different isoforms have been found for this gene. In addition, IRF5 is implicated in the induction of IFNs IFNA and INFB and inflammatory cytokines upon virus infection. IRF5 is activated by TLR7 or TLR8 signaling.

    • Synonyms

      IFN Regulatory Factor 5, IRF-5, SLEB10, IBD14.

    • 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

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

    • Background

      What is the molecular weight/Mw of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein has a total Mw of 10.7kDa.

      What is the source or expression system of IRF5 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IRF5 HUMAN Protein?
      IRF5 HUMAN Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of IRF5 HUMAN Protein?
      The biological functionality of IRF5 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IRF5 HUMAN Protein?
      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSPPTL QPPTLQPPVV LGPPAPDPSP LAPPPGNPAG FRELLSEVLE PGPLPASLPP AGEQLLPDLL I

      What applications can IRF5 HUMAN Protein be used in?
      IRF5 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IRF5 HUMAN Protein?
      The endotoxin level is minimal, IRF5 HUMAN Protein was purified using conventional chromatography techniques.



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

    Irf 5 Human
  • View Data Sheet

    Name :

    OPG Human, Hi-5

    Description:

    Osteoprotegerin Human Recombinant, Hi-5

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    Product # :

    CYT-633

    Price :

    Quantity :

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    More Info

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

    Description

    Recombinant Osteoprotegerin produced in baculovirus is a signle, glycosylated polypeptide chain containing 389 amino acid residues (22-401 a.a.), having a calculated molecular mass of 44.7 kDa. The Osteoprotegerin is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Hi-5.

    Formulation

    Osteoprotegerin protein contains PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 range ≤ 8 ng/ml and is measured by its ability to inhibit cytotoxicity using Jurkat human acute T cell leukemia cells in the presence of 2ng/ml of human TRAIL (CAT# cyt-1014).

    Citations

    More Info

    • Introduction

      Osteoprotegerin acts as decoy receptor for rankl and thereby neutralizes its function in osteoclastogenesis. OPG inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local rankl/opg ratio. Osteoprotegerin may also play a role in preventing arterial calcification. May act as decoy receptor for trail and protect against apoptosis. Trail binding blocks the inhibition of osteoclastogenesis.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, Osteoprotegerin, TR1, MGC29565.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      ADPETFPPKY LHYDEETSHQ LLCDKCPPGT YLKQHCTAKW KTVCAPCPDH YYTDSWHTSD ECLYCSPVCK ELQYVKQECN RTHNRVCECK EGRYLEIEFC LKHRSCPPGF GVVQAGTPER NTVCKRCPDG FFSNETSSKA PCRKHTNCSV FGLLLTQKGN ATHDNICSGN SESTQKCGID VTLCEEAFFR FAVPTKFTPN WLSVLVDNLP GTKVNAESVE RIKRQHSSQE QTFQLLKLWK HQNKDQDIVK KIIQDIDLCE NSVQRHIGHA NLTFEQLRSL MESLPGKKVG AEDIEKTIKA CKPSDQILKL LSLWRIKNGD QDTLKGLMHA LKHSKTYHFP KTVTQSLKKT IRFLHSFTMY KLYQKLFLEM IGNQVQSVKI SCLSHHHHHH.

    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.

    Osteoprotegerin Human Hi 5
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