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Search results

1000 results found for “stem cell”

Name

Description

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  • View Data Sheet

    Name :

    MZB1 Human

    Description:

    Marginal Zone B And B1 Cell-Specific Protein Human Recombinant

    Marginal Zone B and B1 Cell-Specific Protein, MZB1, PACAP, Mesenteric Oestrogen-Dependent Adipose Gene- 7, Plasma Cell-Induced ER Protein 1, Proapoptotic Caspase Adaptor Protein, Mesenteric Estrogen-Dependent Adipose 7, Plasma Cell-Induced Resident Endoplasmic Reticulum Protein, Plasma Cell-Induced Resident ER Protein, Proapoptotic Caspase Adapter Protein, MEDA-7, pERp1, HSPC190, Caspase-2 Binding Protein, Marginal Zone B- And B1-Cell-Specific Protein, MEDA7, MGC29506.

    Product # :

    PRO-608

    Price :

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    Description

    MZB1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 120 amino acids (1-97) and having a molecular mass of 12.9 kDa.MZB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MZB1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Marginal zone B- and B1-cell-specific protein (MZB1) functions as a hormone-regulated adipokine/proinflammatory cytokine which is implicated in causing chronic inflammation and affecting cellular expansion. MZB1 links with immunoglobulin M (IgM) heavy and light chains and stimulate s IgM assembly and secretion. MZB1 exerts its effect by acting as a molecular chaperone or as an oxidoreductase as it exhibits a low level of oxidoreductase activity. MZB1 helps to diversify peripheral B-cell functions by regulating Ca(2+) stores, antibody secretion and integrin activation.

    • Synonyms

      Marginal Zone B and B1 Cell-Specific Protein, MZB1, PACAP, Mesenteric Oestrogen-Dependent Adipose Gene- 7, Plasma Cell-Induced ER Protein 1, Proapoptotic Caspase Adaptor Protein, Mesenteric Estrogen-Dependent Adipose 7, Plasma Cell-Induced Resident Endoplasmic Reticulum Protein, Plasma Cell-Induced Resident ER Protein, Proapoptotic Caspase Adapter Protein, MEDA-7, pERp1, HSPC190, Caspase-2 Binding Protein, Marginal Zone B- And B1-Cell-Specific Protein, MEDA7, MGC29506.

    • 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 MGSMPAELWL TSYGVREVDQ VKRLTGPGLS EGPEPSISVM VTGGPWPTRL SRTCLHYLGE FGEDQIYEAH QQGRGALEAL LCGGPQGACS EKVSATREEL.

    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.

    Mzb1 Human
  • View Data Sheet

    Name :

    TTC33 Human

    Description:

    Tetratricopeptide Repeat Domain 33 Human Recombinant

    Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.

    Product # :

    PRO-1217

    Price :

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    Description

    TTC33 Human Recombinant produced in E. coli is a single polypeptide chain containing 285 amino acids (1-262) and having a molecular mass of 31.8 kDa.TTC33 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TTC33 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Tetratricopeptide repeat protein 33 (TTC33) is comprised of 3 TPR repeats.

    • Synonyms

      Tetratricopeptide Repeat Domain 33, Osmosis-Responsive Factor, Tetratricopeptide Repeat Protein 33, TPR Repeat Protein 33, OSRF.

    • 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 MGS MASFGWK RKIGEKVSKV TSQQFEAEAA DEKDVVDNDE GNWLHAIKRR KEILLEGCAE KSKQLKDEGA SLAENKRYRE AIQKWDEALQ LTPNDATLYE MKSQVLMSLH EMFPAVHAAE MAVQQNPHSW ESWQTLGRAQ LGLGEIILAI RSFQVALHIY
      PMNPEIWKED LSWARTLQEQ QKVAQRIKKS EAPAEVTHFS PKSIPDYDFE SDEIVAVCAA IAEKEKTVSA NKTMVIVSAS GAIETVTEKE DGATPPDGSV FIKAR

    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.

    Ttc33 Human
  • View Data Sheet

    Name :

    VASP Human

    Description:

    Vasodilator-Stimulated Phosphoprotein Human Recombinant

    Vasodilator-stimulated phosphoprotein, VASP.

    Product # :

    PRO-191

    Price :

    Quantity :

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    • description
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    • Citations

    Description

    VASP 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 363 amino acids (1-343 a.a.) and having a molecular mass of 37.5kDa (Molecular weight on SDS-PAGE will appear higher). The VASP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The VASP solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol, 200mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Vasodilator-stimulated phosphoprotein (VASP) belongs to the Ena-VASP protein family. VASP is linked with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. In addition, VASP may be involved in the intracellular signaling pathways which regulate integrin-extracellular matrix interactions.

    • Synonyms

      Vasodilator-stimulated phosphoprotein, VASP.

    • 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 MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSD.

    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.

    Vasp Human
  • View Data Sheet

    Name :

    CYGB Human

    Description:

    Cytoglobin Human Recombinant

    HGB, STAP, Cytoglobin, CYGB.

    Product # :

    PRO-842

    Price :

    Quantity :

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    • description
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    Description

    CYGB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-190 a.a.) and having a molecular mass of 23.5kDa. The CYGB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cytoglobin is a globin protein found in the brain and is mainly utilized in marine mammals. CYGB acts a a protector under conditions of hypoxia. The suggested function of CYGB is the modulation of oxygen and nitric oxide metabolism or scavenging free radicals within a cell.

    • Synonyms

      HGB, STAP, Cytoglobin, CYGB.

    • 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 MEKVPGEMEI ERRERSEELS EAERKAVQAM WARLYASCED VGVAILVRFF VNFPSAKQYF SQFKHMEDPL EMERSPQLRK HACRVMGALN TVVENLHDPD KVSSVLALVG KAHALKHKVE PVYFKILSGV ILEVVAEEFA SDFPPETQRA WAKLRGLIYS HVTAAYKEVG WVQQVPNATT PPATLPSSGP.

    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.

    Cygb Human
  • 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

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    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 :

    IL12p40 Human Baculovirus

    Description:

    Interleukin-12 p40 Human Recombinant, Baculovirus

    NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 2.

    Product # :

    CYT-134

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    Description

    IL 12 p40 Human Recombinant produced in Hi-5 cell using Baculovirus is a single polypeptide chain containing 315 amino acids (23-328) and having a molecular mass of 35.8kDa.IL 12 p40 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Baculovirus

    Formulation

    The IL 12 p40 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT, 100mM PMSF and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    IL12p40 Human Baculovirus - Product image 1

    Citations

    More Info

    • Introduction

      Active IL-12 is a p70 disulphide-linked dimer composed of p35 and p40 subunits. The protein is a pleiotropic cytokine produced primarily by antigen presenting cells and has multiple effects on T lymphocytes and natural killer cells in terms of stimulating cytotoxicity, proliferation, production of other cytokines and Th1 subset differentiation.

    • Synonyms

      NKSF2, CTL maturation factor (TCMF), Cytotoxic lymphocyte maturation factor 40 kDa subunit (CLMF p40), TSF, Edodekin-alpha, IL-12 p40, IL-12B, IL-12 subunit p40, NK cell stimulatory factor chain 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

      ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH

    • Background

      What is the molecular weight/Mw of IL12P40 HUMAN BACULOVIRUS Protein?
      IL12P40 HUMAN BACULOVIRUS Protein has a total Mw of 35.8kDa.

      What is the source or expression system of IL12P40 HUMAN BACULOVIRUS Protein?
      Baculovirus.
      What is the Purity of IL12P40 HUMAN BACULOVIRUS Protein?
      IL12P40 HUMAN BACULOVIRUS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12P40 HUMAN BACULOVIRUS Protein?
      The biological functionality of IL12P40 HUMAN BACULOVIRUS Protein will be determined in the future.

      What is the amino acid sequence of IL12P40 HUMAN BACULOVIRUS Protein?
      ADPIWELKKD VYVVELDWYP DAPGEMVVLT CDTPEEDGIT WTLDQSSEVL GSGKTLTIQV KEFGDAGQYT CHKGGEVLSH SLLLLHKKED GIWSTDILKD QKEPKNKTFL RCEAKNYSGR FTCWWLTTIS TDLTFSVKSS RGSSDPQGVT CGAATLSAER VRGDNKEYEY SVECQEDSAC PAAEESLPIE VMVDAVHKLK YENYTSSFFI RDIIKPDPPK NLQLKPLKNS RQVEVSWEYP DTWSTPHSYF SLTFCVQVQG KSKREKKDRV FTDKTSATVI CRKNASISVR AQDRYYSSSW SEWASVPCSH HHHHH.
      What applications can IL12P40 HUMAN BACULOVIRUS Protein be used in?
      IL12P40 HUMAN BACULOVIRUS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12P40 HUMAN BACULOVIRUS Protein?
      The endotoxin level is minimal, IL12P40 HUMAN BACULOVIRUS Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12P40 HUMAN BACULOVIRUS 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 IL12P40 HUMAN BACULOVIRUS?
      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 12 P40 Human Baculovirus
  • View Data Sheet

    Name :

    BACE1 Human

    Description:

    Beta-Secretase 1 Human Recombinant

    Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE,  ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.

    Product # :

    ENZ-1119

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    Description

    BACE1 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 442 amino acids (22-457 a.a.) and having a molecular mass of 49.2kDa. BACE1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BACE1 protein solution containing Phosphate-Buffered Saline (pH 7.4) containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 5 pmol/min/ug in which one unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C.

    Citations

    More Info

    • Introduction

      Beta-secretase 1 or BACE1 or beta-site amyloid precursor protein cleaving enzyme 1, is a protein that is encoded by the BACE1 gene in humans. Expression of BACE1 is seen primarily in neurons as it is crucial for the creation of myelin sheats in the peripheric nervous system. Beta-secretase 1 is a proteas that is located in the cell membrane (transmembrane). The enzyme consists of 2 active sites (aspartate residues) in the extracellular domain that can act as a dimer.

    • Synonyms

      Beta-Secretase, Membrane-Associated Aspartic Protease, Beta-Site APP Cleaving Enzyme, Beta-Site APP-Cleaving Enzyme, Aspartyl Protease, EC 3.4.23.46, Memapsin-2, Asp, BACE, ASP2, Beta-Site Amyloid Beta A4 Precursor Protein-Cleaving Enzyme, Beta-Site Amyloid Precursor Protein Cleaving Enzyme, Transmembrane Aspartic Proteinase Asp2, Beta-Secretase 1 Precursor Variant, Beta-Site APP-Cleaving Enzyme, APP Beta-Secretase, EC 3.4.23, KIAA1149, HSPC104.

    • 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

      TQHGIRLPLR SGLGGAPLGL RLPRETDEEP EEPGRRGSFV EMVDNLRGKS GQGYYVEMTV GSPPQTLNIL VDTGSSNFAV GAAPHPFLHR YYQRQLSSTY RDLRKGVYVP YTQGKWEGEL GTDLVSIPHG PNVTVRANIA AITESDKFFI NGSNWEGILG LAYAEIARPD DSLEPFFDSL VKQTHVPNLF SLQLCGAGFP LNQSEVLASV GGSMIIGGID HSLYTGSLWY TPIRREWYYE VIIVRVEING QDLKMDCKEY NYDKSIVDSG TTNLRLPKKV FEAAVKSIKA ASSTEKFPDG FWLGEQLVCW QAGTTPWNIF PVISLYLMGE VTNQSFRITI LPQQYLRPVE DVATSQDDCY KFAISQSSTG TVMGAVIMEG FYVVFDRARK RIGFAVSACH VHDEFRTAAV EGPFVTLDME DCGYNIPQTD ESTLMTHHHH 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.

    Bace1 Human
  • View Data Sheet

    Name :

    PSME2 Human

    Description:

    Proteasome Activator Subunit 2 Human Recombinant

    Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.

    Product # :

    PRO-975

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    Description

    PSME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 259 amino acids (1-239) and having a molecular mass of 29.5 kDa.PSME2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PSME2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PSME2 is an IFN-gamma inducible proteasome activator essential for production of several key histocompatibility (MHC) class I antigens. Downregulation of PSME2 causes unusual proteasome activation and is connected to the development of intimal hyperplasia (IH) in animal models.

    • Synonyms

      Proteasome (prosome, macropain) activator subunit 2 (PA28 beta), PA28beta, Activator of multicatalytic protease subunit 2, Proteasome activator 28 subunit beta, 11S regulator complex subunit beta, PA28B, REG-beta, cell migration-inducing protein 22, MCP activator 31-kD subunit, proteasome activator complex subunit 2, Proteasome activator hPA28 subunit beta.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAKPCGVRLS GEARKQVEVF RQNLFQEAEE FLYRFLPQKI IYLNQLLQED SLNVADLTSL RAPLDIPIPD PPPKDDEMET DKQEKKEVPK CGFLPGNEKV LSLLALVKPE VWTLKEKCIL VITWIQHLIP KIEDGNDFGV AIQEKVLERV NAVKTKVEAF QTTISKYFSE RGDAVAKASK ETHVMDYRAL VHERDEAAYG ELRAMVLDLR AFYAELYHII SSNLEKIVNP KGEEKPSMY

    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.

    Psme2 Human
  • View Data Sheet

    Name :

    SYT11 Human

    Description:

    Synaptotagmin XI Human Recombinant

    Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    Product # :

    PRO-2301

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    Description

    SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.

    • Synonyms

      Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.

    • 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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.

    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.

    Syt11 Human
  • View Data Sheet

    Name :

    Osteocrin Human

    Description:

    Osteocrin Human Recombinant

    Osteocrin, Musclin, OSTN.

    Product # :

    PRO-420

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    Description

    The recombinant Human Osteocrin is produced with N-terminal fusion of His Tag. The Human Osteocrin His-Tagged Fusion Protein is 13.6 kDa containing 106 amino acid residues of the human Osteocrin and 16 additional amino acid residues – His Tag (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer, pH 4.0.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Osteocrin is a recently identified secreted protein expression of which was only detected in bone, peaking just after birth and decreasing markedly with age. A 1280-bp mRNA encodes osteocrin producing a mature protein of 103 amino acids with a molecular mass of 11.4 kDa. In primary osteoblastic cell cultures osteocrin expression coincided with matrix formation then decreased in very mature cultures. Treatment of cultures with 1,25-dihydroxyvitamin D3 resulted in a rapid dose- dependent down-regulation of osteocrin expression, suggesting direct regulation. Chronic treatment of primary cultures with osteocrin-conditioned media inhibited mineralization and reduced osteocalcin and alkaline phosphatase expression. These results suggest that osteocrin represents a novel, unique vitamin D-regulated bone-specific protein that appears to act as a soluble osteoblast regulator.

    • Synonyms

      Osteocrin, Musclin, OSTN.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10μg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASHMVDVT TTEAFDSGVI DVQSTPTVRE EKSATDLTAK LLLLDELVSL ENDVIETKKK RSFSGFGSPL DRLSAGSVDH KGKQRKVVDH PKRRFGIPMD RIGRNRLSNS RG.

    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.

    Musclin Human
  • View Data Sheet

    Name :

    IL6 Mouse

    Description:

    Interleukin-6 Mouse Recombinant

    IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

    Product # :

    CYT-350

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    Description

    Interleukin-6 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids and having a molecular mass of 21709 Dalton. The IL-6 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 96.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

    Citations

    More Info

    • Introduction

      Interleukin-6 is a potent pro-inflammatory cytokine primarily produced by activated T cells and an assortment of other cells including endothelial cells and macrophages. IL-6 affects B and T lymphocytes and has been shown to have a role in host defense, acute phase reactions, immune responses and hematopoiesis.

    • Synonyms

      IFN-b2, B cell differentiation factor (BCDF), BSF-2, HPGF, HSF, MGI-2, IL-6, Interleukin HP-1, B-cell hybridoma growth factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin-6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL6 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 Mouse Il-6 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

    • Background

      Research Paper on Interleukin-6 Mouse Recombinant

      Abstract:

      Interleukin-6 (IL-6) Mouse Recombinant stands at the forefront of immunological exploration, unraveling the intricacies of immune modulation. This research paper delves into its molecular attributes and implications within the realm of immunological studies. By examining its functions, synonyms like DIF, TNFA, and TNFSF2, and potential applications, we gain insights into its pivotal role in shaping immune responses.

      Introduction:

      IL-6 Mouse Recombinant has emerged as a linchpin in immunological research. This paper seeks to comprehensively elucidate its molecular characteristics and the impact it bears on immune mechanisms.

      Molecular Architecture and Insights:

      Delving into the molecular makeup of IL-6 Mouse Recombinant, we unveil its crucial role in immune signaling. Its interactions and functions contribute significantly to orchestrating immune responses.

      Navigating Immune Dynamics:

      The well-established influence of IL-6 on immune cell activation and inflammation is a cornerstone. IL-6 Mouse Recombinant allows for a more intricate exploration of these immune processes, augmenting our understanding of cytokine-mediated functions.

      Synonyms and Network Connections:

      Understanding the synonyms associated with IL-6, such as DIF, TNFA, and TNFSF2, amplifies our grasp of immune signaling networks. IL-6 Mouse Recombinant aids in unraveling the complexity of these interconnected pathways.

      Potential Applications in Research and Beyond:

      Beyond the confines of research, IL-6 Mouse Recombinant holds promise in deciphering immune-related diseases. Its significance extends to potential therapeutic interventions and diagnostic applications.

      Clinical Implications and Future Prospects:

      The clinical relevance of IL-6 Mouse Recombinant is underscored by its role in diseases characterized by altered IL-6 signaling. Unearthing its therapeutic potential paves the way for innovative strategies in disease management.

      Conclusion:

      Within the realm of immunology, IL-6 Mouse Recombinant assumes a pivotal role. Its molecular insights, fundamental functions, and potential applications position it as a cornerstone in advancing our comprehension of immune regulation.

      What is the molecular weight/Mw of IL6 MOUSE Protein?
      IL6 MOUSE Protein has a total Mw of 21.7kDa.

      What is the source or expression system of IL6 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IL6 MOUSE Protein?
      IL6 MOUSE Protein is >96% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL6 MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of IL-6-dependent murine 7TD1 cells is < 0.02 ng/ml, corresponding to a specific activity of > 50,000,000 units/mg.

      What is the amino acid sequence of IL6 MOUSE Protein?
      FPTSQVRRGD FTEDTTPNRP VYTTSQVGGL ITHVLWEIVE MRKELCNGNS DCMNNDDALA ENNLKLPEIQ RNDGCYQTGY NQEICLLKIS SGLLEYHSYL EYMKNNLKDN KKDKARVLQR DTETLIHIFN QEVKDLHKIV LPTPISNALL TDKLESQKEW LRTKTIQFIL KSLEEFLKVT LRSTRQT.

      What applications can IL6 MOUSE Protein be used in?
      IL6 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL6 MOUSE Protein?
      The endotoxin level is minimal, IL6 MOUSE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL6 MOUSE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL6 MOUSE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

    Il 6 Mouse
  • View Data Sheet

    Name :

    Prolactin Mouse, His

    Description:

    Prolactin Mouse Recombinant, His Tag

    AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    Product # :

    CYT-1060

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    Description

    Prolactin Mouse produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 222 amino acids (30-228a.a.) and having a molecular mass of 25 kDa. Prolactin Mouse protein is fused to a 23 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    The Prolactin Mouse solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      AV290867, Gha1, Prl1a1, Growth hormone a1, Mammotropin, Luterotropic hormone, Lutetropin, PRL.

    • 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 MGSQPLPICS AGDCQTSLRE LFDRVVILSH YIHTLYTDMF IEFDKQYVQD REFMVKVIND CPTSSLATPE DKEQALKVPP EVLLNLILSL VQSSSDPLFQ LITGVGGIQE APEYILSRAK EIEEQNKQLL EGVEKIISQA YPEAKGNGIY VWSQLPSLQ GVDEESKILS LRNTIRCLRR DSHKVDNFLK VLRCQIAHQN NC.

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

    Mouse Prolactin
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    HPSE Human

    Description:

    Heparanase-1 Human Recombinant

    Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    Product # :

    ENZ-778

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    Description

    HPSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (36-543 a.a) and having a molecular mass of 60kDa.HPSE is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.

    • Synonyms

      Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSQDVVDLD FFTQEPLHLV SPSFLSVTID ANLATDPRFL ILLGSPKLRT LARGLSPAYL RFGGTKTDFL IFDPKKESTF EERSYWQSQV NQDICKYGSI PPDVEEKLRL EWPYQEQLLL REHYQKKFKN STYSRSSVDV LYTFANCSGL DLIFGLNALL RTADLQWNSS NAQLLLDYCS SKGYNISWEL GNEPNSFLKK ADIFINGSQL GEDFIQLHKL LRKSTFKNAK LYGPDVGQPR RKTAKMLKSF LKAGGEVIDS VTWHHYYLNG RTATKEDFLN PDVLDIFISS VQKVFQVVES TRPGKKVWLG ETSSAYGGGA PLLSDTFAAG FMWLDKLGLS ARMGIEVVMR QVFFGAGNYH LVDENFDPLP DYWLSLLFKK LVGTKVLMAS VQGSKRRKLR VYLHCTNTDN PRYKEGDLTL YAINLHNVTK YLRLPYPFSN KQVDKYLLRP LGPHGLLSKS VQLNGLTLKM VDDQTLPPLM EKPLRPGSSL GLPAFSYSFF VIRNAKVAAC I.

    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.

    Hpse Human
  • View Data Sheet

    Name :

    Leptin tA Mouse

    Description:

    Leptin Antagonist Triple Mutant Mouse Recombinant

    Product # :

    CYT-354

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    Description

    Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 99.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant is capable of inhibiting Leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human Leptin receptor. It also inhibits various Leptin effects in several in vitro bioassays.

    Citations

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    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Amino Acid Sequence

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

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Mouse
  • View Data Sheet

    Name :

    NOV Human, HEK

    Description:

    Nephroblastoma Overexpressed Human Recombinant, HEK

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-1032

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    Description

    NOV Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 33-357) containing 331 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 36.5kDa (calculated).

    Source

    HEK293 cells.

    Formulation

    NOV filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week 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. NOV is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      QRCPPQCPGR CPATPPTCAP GVRAVLDGCS CCLVCARQRG ESCSDLEPCD ESSGLYCDRS ADPSNQTGIC TAVEGDNCVF DGVIYRSGEK FQPSCKFQCT CRDGQIGCVP RCQLDVLLPE PNCPAPRKVE VPGECCEKWI CGPDEEDSLG GLTLAAYRPE ATLGVEVSDS SVNCIEQTTE WTACSKSCGM GFSTRVTNRN RQCEMLKQTR LCMVRPCEQE PEQPTDKKGK KCLRTKKSLK AIHLQFKNCT SLHTYKPRFC GVCSDGRCCT PHNTKTIQAE FQCSPGQIVK KPVMVIGTCT CHTNCPKNNE AFLQELELKT TRGKMHHHHH H.

    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.

    Nov Protein
  • View Data Sheet

    Name :

    CST3 Human, His Active

    Description:

    Cystatin C, His BioActive Human Recombinant

    Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    Product # :

    PRO-2632

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    Description

    CST3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (27-146 a.a.) and having a molecular mass of 15.6kDa.CST3 is fused to a 21 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CST3 solution (0.25mg/1ml) contains 0.1M NaCl, 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The IC50 value is < 2.0nM. The inhibitory function of Cystatin 3 on protease activity of papain was measured by a fluorometric assay using Z-FR-AMC at pH 7.5 at 25˚C.

    Citations

    More Info

    • Introduction

      Cystatin C is part to the cystatin protein family, which has members with various cystatin-like sequences. Part of the proteins has the ability to act as active cysteine protease inhibitors, other members has lost or never had the ability. Three sub members of the cystatin protein family are the type 1 cystatins, type 2 cystatins & kininogens. The locus in chromosome twenty holds the most type 2 cystatin genes. Cystatin C can be found in the cystatin locus, it is the most common extracellular inhibitor of cysteine proteases, that is available in big volumes in biological fluids and exist in every tissue in the body.

    • Synonyms

      Cystatin-C, Cystatin-3, Neuroendocrine basic polypeptide, Gamma-trace, Post-gamma-globulin, CST3, MGC117328.

    • 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 MSSPGKPPRL VGGPMDASVE EEGVRRALDF AVGEYNKASN DMYHSRALQV VRARKQIVAG VNYFLDVELG RTTCTKTQPN LDNCPFHDQP HLKRKAFCSF QIYAVPWQGT MTLSKSTCQD A

    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.

    Cystatin C Human
  • View Data Sheet

    Name :

    SNRPC Human, Sf9

    Description:

    Small Nuclear Ribonucleoprotein Polypeptide C Human Recombinant, Sf9

    U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    Product # :

    PRO-1510

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    Description

    SNRPC Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 25,000 Dalton. SNRPC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    SNRPC is supplied in 20mM HEPES buffer pH-7.5, 0.01mM EDTA and 0.02% SDS.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNRPC is a member of the U1 small nuclear ribonucleoprotein C family. The SNRPC protein component of the U1 small nuclear ribonucleoprotein (snRNP) particle required for the formation of the spliceosome. SNRPC participates in the processing of nuclear precursor messenger RNA splicing. snRNP particles are tackled by autoantibodies frequently produced by patients with connective tissue diseases.

    • Synonyms

      U1 small nuclear ribonucleoprotein C, U1 snRNP C, U1-C, U1C, SNRPC, Yhc1.

    • 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.

    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.

    Snrpc Human Sf9
  • View Data Sheet

    Name :

    VEGFC Human, Sf9

    Description:

    Vascular Endothelial Growth Factor C Human Recombinant, Sf9

    Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

    Product # :

    CYT-948

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    Description

    VEGFC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 125 amino acids (112-227a.a.) and having a molecular mass of 14.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). VEGFC is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    VEGFC protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      VEGF-C, also known as Vascular Endothelial Growth Factor Related Protein (VRP), is a recently discovered VEGF growth factor family member that is most closely related to VEGF-D. Human VEGF-C cDNA encodes a pre-pro-protein of 416 amino acids residues. It is almost identical to the mouse VEGF-C protein. Similar to VEGF-D, VEGF-C has a VEGF homology domain spanning the middle third of the precursor molecule and long N- and C-terminal extensions. In adults, VEGF-C is highly expressed in heart, placenta, ovary and small intestine. Recombinant human VEGF-C, lacking the N- and C-terminal extensions and containing only the middle VEGF homology domain, forms primarily non-covalently linked dimers. This protein is a ligand for both VEGFR-2/KDR and VEGFR-3/FLT-4. Since VEGFR-3 is strongly expressed in lymphatic endothelial cells, it has been postulated that VEGF-C is involved in the regulation of the growth and/or differentiation of lymphatic endothelium. Although recombinant human VEGF-C is also a mitogen for vascular endothelial cells, it is much less potent than VEGF-A.

    • Synonyms

      Vascular Endothelial Growth Factor C, Vascular Endothelial Growth Factor-Related Protein, Flt4-L, VRP, FLT4 Ligand DHM, Flt4 Ligand, LMPH1D, VEGF-C, Vascular endothelial growth factor C, VEGF-C, Flt4 ligand, Flt4-L, Vascular endothelial growth factor-related protein.

    • 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

      ADPAHYNTEI LKSIDNEWRK TQCMPREVCI DVGKEFGVAT NTFFKPPCVS VYRCGGCCNS EGLQCMNTST SYLSKTLFEI TVPLSQGPKP VTISFANHTS CRCMSKLDVY RQVHSIIRRH HHHHH.

    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.

    Vegfc Human Sf9
  • View Data Sheet

    Name :

    HAX1 Human

    Description:

    HCLS1 Associated Protein X-1 Human Recombinant

    HCLS1-associated protein X-1, HS1-associating protein X-1, HS1-binding protein 1, HAX-1, HSP1BP-1, HAX1, HS1BP1.

    Product # :

    PRO-1417

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    Description

    HAX1 Human Recombinant produced in E. coli is a single polypeptide chain containing 299 amino acids (1-279) and having a molecular mass of 33.7kDa. HAX1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The HAX1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HAX1 associates with hematopoietic cell-specific Lyn substrate 1, which is a substrate of Src family tyrosine kinases. HAX1 also interacts with the product of the polycystic kidney disease 2 gene, mutations in which are associated with autosomal-dominant polycystic kidney disease, and with the F-actin-binding protein, cortactin. It was earlier thought HAX1 is mainly localized to the mitochondria, however, recent studies indicate it to be localized in the cell body. Mutations in the HAX1 gene result in autosomal recessive severe congenital neutropenia, aka Kostmann disease.

    • Synonyms

      HCLS1-associated protein X-1, HS1-associating protein X-1, HS1-binding protein 1, HAX-1, HSP1BP-1, HAX1, HS1BP1.

    • 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 MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPELPGP ESETPGERLR EGQTLRDSML KYPDSHQPRI FGGVLESDAR SESPQPAPDW GSQRPFHRFD DVWPMDPHPR TREDNDLDSQ VSQEGLGPVL QPQPKSYFKS ISVTKITKPD GIVEERRTVV DSEGRTETTV TRHEADSSPR GDPESPRPPA LDDAFSILDL FLGRWFRSR.

    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.

    Hax1 Human
  • View Data Sheet

    Name :

    RAN Human

    Description:

    RAN, Member RAS Oncogene Family Human Recombinant

    ARA24, Gsp1, TC4, GTP-binding nuclear protein Ran, GTPase Ran, Ras-related nuclear protein, Ras-like protein TC4, Androgen receptor-associated protein 24, Ras-like, RANP1.

    Product # :

    PRO-841

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    Description

    RAN Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.5 kDa. The RAN is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      RAN is a GTP-binding protein that participates in nucleocytoplasmic transport. RAN is necessary for the import of protein into the nucleus and also for RNA export. RAN takes part in chromatin condensation and control of cell cycle. The RAN complex with BIRC5 participates in mitotic spindle formation by being as a physical scaffold to assist the delivery of the RAN effector molecule TPX2 to microtubules. RUN increases AR-mediated transactivation.

    • Synonyms

      ARA24, Gsp1, TC4, GTP-binding nuclear protein Ran, GTPase Ran, Ras-related nuclear protein, Ras-like protein TC4, Androgen receptor-associated protein 24, Ras-like, RANP1.

    • 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 MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD LEVAQTTALP DEDDDL.

    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.

    Ran Human
  • 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 :

    GDF10 Human

    Description:

    Growth differentiation factor 10 Human Recombinant

    Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.

    Product # :

    CYT-659

    Price :

    Quantity :

    Shipping Method :

    Ice Icon

    Shipped with Ice Packs

    Add To Cart

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    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page
    • Citations

    Description

    GDF10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 111 amino acids (369-478 a.a.) and having a total molecular mass of 12.5 kDa. GDF10 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GDF10 solution (1mg/ml) contains 10mM Sodium citrate (pH 3.5), 1mM DTT, 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    GDF10 Human - Product image 1

    Citations

    More Info

    • Introduction

      GDF10 is a member of the BMP family and the TGF-beta superfamily. GDF10 is expressed in femur, brain, lung, skeletal, muscle, pancreas and testis, and has a role in head formation and possibly multiple roles in skeletal morphogenesis. In humans, GDF10 mRNA is found in the cochlea and lung of fetuses, and in testis, retina, pineal gland, and other neural tissues of adults. The BMP family members are regulators of cell growth and differentiation in both embryonic and adult tissues. These proteins are characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing 7 conserved cysteine residues.

    • Synonyms

      Bone morphogenetic protein 3b, BMP-3b, Growth/differentiation factor 10, GDF-10, Bone-inducing protein, BIP, GDF10, BMP3B.

    • 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

      MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.

    • Background

      What is the molecular weight/Mw of GDF10 HUMAN Protein?
      GDF10 HUMAN Protein has a total Mw of 12.5kDa.

      What is the source or expression system of GDF10 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of GDF10 HUMAN Protein?
      GDF10 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF10 HUMAN Protein?
      The biological functionality of GDF10 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of GDF10 HUMAN Protein?
      MQWDEPRVCS RRYLKVDFAD IGWNEWIISP KSFDAYYCAG ACEFPMPKIV RPSNHATIQS IVRAVGIIPG IPEPCCVPDK MNSLGVLFLD ENRNVVLKVY PNMSVDTCAC R.

      What applications can GDF10 HUMAN Protein be used in?
      GDF10 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF10 HUMAN Protein?
      The endotoxin level is minimal, GDF10 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.

    Gdf10 Human
  • View Data Sheet

    Name :

    Epigen Human

    Description:

    Epigen Human Recombinant

    EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    Product # :

    CYT-601

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

    Add To Cart

    More Info

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

    Description

    Epigen Recombinant Human produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 72 amino acids and having a molecular mass of 7.9 kDa. Epigen is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    EPGN was lyophilized from 20mM PBS buffer pH-7.4 .

    Purity

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

    Biological Activity

    Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.

    Citations

    More Info

    • Introduction

      EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.

    • Synonyms

      EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA

    • Background

      What is the molecular weight/Mw of EPIGEN Protein?
      EPIGEN Protein has a total Mw of 7.9kDa.

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

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

      What is the Biological Activity of EPIGEN Protein?
      Determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells. The expected ED50 for this effect is less than 300 ng/ml, corresponding to a specific activity of > 3.3 ×103 IU/mg.

      What is the amino acid sequence of EPIGEN Protein?
      AVTVTPPITA QQADNIEGPI ALKFSHLCLE DHNSYCINGA CAFHHELEKA ICRCFTGYTG ERCEHLTLTS YA

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

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

    Epgn Human
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