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Search results

1000 results found for “Peptide Hormones”

Name

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  • View Data Sheet

    Name :

    Activin B Human

    Description:

    Activin-B Human Recombinant

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    Product # :

    CYT-058

    Price :

    Quantity :

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    Shipped at Room temp

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    • source
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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

    • Background

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

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

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

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

      What applications can ACTIVIN B Protein be used in?

      ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

    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.

    Activin B Human Plant
  • View Data Sheet

    Name :

    PCSK1N Human

    Description:

    Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor Human Recombinant

    ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    Product # :

    PRO-1819

    Price :

    Quantity :

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    • source
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    Description

    PCSK1N Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 251 amino acids (34-260) and having a molecular mass of 26.6 kDa.PCSK1N is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCSK1N solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Proprotein Convertase Subtilisin/Kexin Type 1 Inhibitor (PCSK1N) takes part in the control of the neuroendocrine secretory pathway. PCSK1N inhibits prohormone convertase 1, which regulates the proteolytic cleavage of neuroendocrine peptide precursors. PCSK1Nslows down convertase-mediated processing of proopiomelanocortin and proenkephalin and also monitors the intracellular timing of PCSK1.

    • Synonyms

      ProSAAS precursor, Proprotein convertase subtilisin/kexin type 1 inhibitor, PROSAAS; SAAS, PCSK1N.

    • 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 MGSMARPVKE PRGLSAASPP LAETGAPRRF RRSVPRGEAA GAVQELARAL AHLLEAERQE RARAEAQEAE DQQARVLAQL LRVWGAPRNS DPALGLDDDP DAPAAQLARA LLRARLDPAA LAAQLVPAPV PAAALRPRPP VYDDGPAGPD AEEAGDETPD VDPELLRYLL GRILAGSADS EGVAAPRRLR RAADHDVGSE LPPEGVLGAL LRVKRLETPA PQVPARRLLP P.

    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.

    Pcsk1N Human
  • View Data Sheet

    Name :

    Aminopeptidase

    Description:

    Aminopeptidase Aeromonas Recombinant

    Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    Product # :

    ENZ-275

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • source
    • formulation
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    • Citations

    Description

    The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.

    Source

    Aeromonas Proteolytica.

    Formulation

    Buffered solution containing 10mM Tris-HCl, 100mM NaCl and 5µM ZnSO4, pH 8.0.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    Recombinant Aeromonas Aminopeptidase was found to have an activity of 108 Units/mg protein.

    Citations

    More Info

    • Synonyms

      Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    • Physical Appearance

      Sterile filtered liquid formulation.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C.

    • Unit Definition

      One unit of aminopeptidase activity is defined as the amount of enzyme that releases 1 μmole p-nitroaniline at 25°C in 1 minute.

    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.

    Aminopeptidase
  • View Data Sheet

    Name :

    EDN2 Human

    Description:

    Endothelin-2 Human Recombinant

    ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    Product # :

    HOR-006

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
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    Description

    EDN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (25-178 a.a.) and having a molecular mass of 19.9kDa. EDN2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    EDN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Endothelin-2 is a Hypoxia-induced Autocrine Survival Factor for Breast Tumor Cells. The synthesis of EDN2 by human kidney carcinoma cells is decreased by EGF. EDN2 is a chemoattractant for macrophages and THP-1 monocytic cells. Chemotaxis towards EDN2 is via the MAPK pathway: p44 and p42 are phosphorylated when THP-1 cells are stimulated with EDN2. Migration to EDN2 is inhibited by hypoxia and by pertussis toxin. EDN2 leads to activation of macrophages. EDN2 shares a similar peptide sequence with chemokines and may signal via a similar receptor and MAPK-mediated pathway. Furthermore, EDN2 expression by tumors may modulate the behavior of macrophages such that activated cells accumulate in areas of hypoxia.

    • Synonyms

      ET2, PPET2, Endothelin-2, ET-2, Preproendothelin-2, EDN2.

    • 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 MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR.

    • Background

      What is the molecular weight/Mw of EDN2 HUMAN Protein?
      EDN2 HUMAN Protein has a total Mw of 19.9kDa.

      What is the source or expression system of EDN2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EDN2 HUMAN Protein?
      EDN2 HUMAN Protein is > 85% pure as determined by SDS-PAGE.

      What is the Biological Activity of EDN2 HUMAN Protein?
      The biological functionality of EDN2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of EDN2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSQAAATLE QPASSSHAQG THLRLRRCSC SSWLDKECVY FCHLDIIWVN TPEQTAPYGL GNPPRRRRRS LPRRCQCSSA RDPACATFCL RRPWTEAGAV PSRKSPADVF QTGKTGATTG ELLQRLRDIS TVKSLFAKRQ QEAMREPRST HSRWRKR.

      What applications can EDN2 HUMAN Protein be used in?
      EDN2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for EDN2 HUMAN Protein?
      The endotoxin level is minimal, EDN2 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant EDN2 HUMAN 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 EDN2 HUMAN?
      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.

    Edn2 Human His
  • View Data Sheet

    Name :

    SULT2A1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    Product # :

    ENZ-141

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    Description

    SULT2A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-285a.a) and having a molecular mass of 35.9kDa.SULT2A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SULT2A1 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.

    • Synonyms

      Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.

    • 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 MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE

    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.

    Sult2A1 Human
  • View Data Sheet

    Name :

    GHBP Rat

    Description:

    GH Binding Protein Rat Recombinant

    GHBP, GH receptor.

    Product # :

    CYT-933

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    Description

    GHBP produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 255 amino acids (19-265.a.) and having a molecular mass of 29.4kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GHBP protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GH receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, GH performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.

    • Synonyms

      GHBP, GH receptor.

    • 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

      FPGSGATPAT LGKASPVLQR INPSLRESSS GKPRFTKCRS PELETFSCYW TEGDDHNLKV PGSIQLYYAR RIAHEWTPEW KECPDYVSAG ANSCYFNSSY TSIWIPYCIK LTTNGDLLKE KCFTVDEIVQ PDPPIGLNWT LLNISLPGIR GDIQVSWQPP PSADVLKGWI ILEYEIQYKE VNETKWKTMS PIWSTSVPLY SLRLDKEHEV RVRSRQRSFE KYSEFSEVLR VTFPQMDTLA ACEEDFRLEH 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.

    Ghr Rat
  • View Data Sheet

    Name :

    SERPING1 Human

    Description:

    Serpin Peptidase Inhibitor, Clade G Member 1 Human Recombinant

    C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    Product # :

    PRO-1401

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    Description

    SERPING1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 499 amino acids (23-500a.a) and having a molecular mass of 55.1kDa. SERPING1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    SERPING1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Plasma protease C1 inhibitor (SERPING1) is a part of the serpin superfamily of serine protease inhibitors. SERPING1 plays an important role in regulating activation of both the complement and contact systems. That isdue to the fact that SERPING1 regulates the activation of complement factor C1 in addition to the activity of activated C1 by coupling with the active catalytic site at the light chains of C1r and C1s. SERPING1 insufficiency results in hereditary angioedema, which is characterized by recurrent episodes of localized angioedema of the skin, gastrointestinal mucosa or upper respiratory mucosa.

    • Synonyms

      C1IN, C1INH, C1NH, HAE1, HAE2 , Plasma protease C1 inhibitor, C1 esterase inhibitor, C1-inhibiting factor, Serpin G1, Name, SERPING1.

    • 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 MNPNATSSSS QDPESLQDRG EGKVATTVIS KMLFVEPILE VSSLPTTNST TNSATKITAN TTDEPTTQPT TEPTTQPTIQ PTQPTTQLPT DSPTQPTTGS FCPGPVTLCS DLESHSTEAV LGDALVDFSL KLYHAFSAMK KVETNMAFSP FSIASLLTQV LLGAGENTKT NLESILSYPK DFTCVHQALK GFTTKGVTSV SQIFHSPDLA IRDTFVNASR TLYSSSPRVL SNNSDANLEL INTWVAKNTN NKISRLLDSL PSDTRLVLLN AIYLSAKWKT TFDPKKTRME PFHFKNSVIK VPMMNSKKYP VAHFIDQTLK AKVGQLQLSH NLSLVILVPQ NLKHRLEDME QALSPSVFKA IMEKLEMSKF QPTLLTLPRI KVTTSQDMLS IMEKLEFFDF SYDLNLCGLT EDPDLQVSAM QHQTVLELTE TGVEAAAASA ISVARTLLVF EVQQPFLFVL WDQQHKFPVF MGRVYDPRA.

    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.

    Serping1 Human
  • View Data Sheet

    Name :

    BMP 2 Human, Monomer

    Description:

    Bone Morphogenetic Protein-2 Human Recombinant, Monomer

    BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    Product # :

    CYT-627

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    Description

    Bone Morphogenetic Protein-2 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 115 amino acids (283-396) and having a molecular mass of 13009 Dalton. The BMP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-2 solution contains 10mM NaAc pH=3.5 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BMP2 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein induces bone formation. BMP2 is a candidate gene for the autosomal dominant disease of fibrodysplasia (myositis) ossificans progressiva.

    • Synonyms

      BMP-2, BMP2A, Bone morphogenetic protein 2, BMP-2A, BMP2.

    • 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. Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

    • Background

      What is the molecular weight/Mw of BMP2 Protein?
      BMP2 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP2 Protein?
      Escherichia Coli.

      What is the Purity of BMP2 Protein?
      BMP2 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP2 Protein?
      The biological functionality of BMP2 Protein will be determined in the future.

      What is the amino acid sequence of BMP2 Protein?
      MQAKHKQRKR LKSSCKRHPL YVDFSDVGWN DWIVAPPGYH AFYCHGECPF PLADHLNSTN HAIVQTLVNS VNSKIPKACC VPTELSAISMLYLDENEKVV LKNYQDMVVE GCGCR.

      What applications can BMP2 Protein be used in?
      BMP2 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP2 Protein?
      The endotoxin level is minimal, BMP2 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.

    Bmp 2 Human Monomer
  • View Data Sheet

    Name :

    Epigen Human

    Description:

    Epigen Human Recombinant

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

    Product # :

    CYT-601

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    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
  • View Data Sheet

    Name :

    CCNH Human

    Description:

    Cyclin-H Human Recombinant

    CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    Product # :

    PKA-364

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    Description

    CCNH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 39.8 kDa. The CCNH is fused to a 20 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCNH solution contains 20mM Tris-HCl pH-8, 2mM DTT, 2mM EDTA, 0.1M NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CCNH is part of the cyclin family that is known for its protein abundance through the cell cycle. Cyclins act as regulators of CDK kinases. CCNH forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, therefore it functions as a CDK-activating kinase (CAK). CCNH and its kinase collaborator are components of TFIIH, as well as RNA polymerase II protein complexes.

    • Synonyms

      CCNH, CAK, p34, p37, Cyclin-H, MO15-associated protein.

    • Physical Appearance

      Sterile Filtered clear 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 MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP HEEMTLCKYY EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH PRIIMLTCAF LACKVDEFNV SSPQFVGNLR ESPLGQEKAL EQILEYELLL IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI LENPEILRKT ADDFLNRIAL TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE NRTCLSQLLD IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD DYVSKKSKHE EEEWTDDDLV ESL.

    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.

    Ccnh Human
  • View Data Sheet

    Name :

    PSMD11 Human

    Description:

    Proteasome 26S Subunit, Non-ATPase 11 Human Recombinant

    S9, Rpn6, p44.5, MGC26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit p44.5, PSMD11.3844, 26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit RPN6.

    Product # :

    ENZ-760

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    Description

    PSMD11 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 442 amino acids (1-422a.a) and having a molecular mass of 49.6kDa. PSMD11 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PSMD11 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      The 26S proteasome is a multicatalytic proteinase complex with a well ordered structure composed of two complexes- a 20S core and a 19S regulator. PSMD11 is a non-ATPase subunit of the 19S regulator. The 20S core is composed of four rings of 28 non-identical subunits; two rings are composed of 7 alpha subunits and two rings are composed of 7 beta subunits. The 19S regulator is composed of a base that contains six ATPase subunits and two non-ATPase subunits, and a lid that contains up to ten non-ATPase subunits. Proteasomes are spread throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An indispensable function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides.

    • Synonyms

      S9, Rpn6, p44.5, MGC26S proteasome regulatory subunit S9, 26S proteasome regulatory subunit p44.5, PSMD11.3844, 26S proteasome non-ATPase regulatory subunit 11, 26S proteasome regulatory subunit RPN6.

    • 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 MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK LT.

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    Psmd11 Human
  • View Data Sheet

    Name :

    CNDP2 Human

    Description:

    CNDP Dipeptidase 2 Human Recombinant

    Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    Product # :

    ENZ-681

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    Description

    CNDP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 498 amino acids (1-475) and having a molecular mass of 55.3 kDa. CNDP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CNDP2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      CNDP Dipeptidase 2 (CNDP2), is a cytosolic, non-specific dipeptidase which is a part of the peptidase M20A protein family. CNDP2 is a secreted peptidase homologous to M20 peptidases. CNDP2 expresses through all adult and fetal tissue, though, an isoform missing exons 3 and 4 expresses in all fetal tissue in adult liver. Over expression of CPGL-B in hepatocellular carcinoma cells results in significant inhibition of HC cell viability, colony formation, cell invasiveness and tumor configuration.

    • Synonyms

      Cytosolic non-specific dipeptidase, CNDP dipeptidase 2, CN2, CPGL, HsT2298, PEPA, Glutamate carboxypeptidase-like protein 1, Peptidase A.

    • 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 MGSMAALTTL FKYIDENQDR YIKKLAKWVA IQSVSAWPEK RGEIRRMMEV AAADVKQLGG SVELVDIGKQ KLPDGSEIPL PPILLGRLGS DPQKKTVCIY GHLDVQPAAL EDGWDSEPFT LVERDGKLYG RGSTDDKGPV AGWINALEAY QKTGQEIPVN VRFCLEGMEE SGSEGLDELI FARKDTFFKD VDYVCISDNY WLGKKKPCIT YGLRGICYFF IEVECSNKDL HSGVYGGSVH EAMTDLILLM GSLVDKRGNI LIPGINEAVA AVTEEEHKLY DDIDFDIEEF AKDVGAQILL HSHKKDILMH RWRYPSLSLH GIEGAFSGSG AKTVIPRKVV GKFSIRLVPN MTPEVVGEQV TSYLTKKFAE LRSPNEFKVY MGHGGKPWVS DFSHPHYLAG RRAMKTVFGV EPDLTREGGS IPVTLTFQEA TGKNVMLLPV GSADDGAHSQ NEKLNRYNYI EGTKMLAAYL YEVSQLKD.

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    Cndp2 Human
  • View Data Sheet

    Name :

    GH Zebrafish Mutant

    Description:

    Growth Hormone Mutant Zebrafish Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    Product # :

    CYT-709

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    Description

    Somatotropin Zebrafish Mutant G113R Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 185 amino acids with an additional Ala at the N-terminus and having a molecular mass of 21.18 kDa. The Zebrafish Mutant G113R Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.5% NaHCO3 pH-8.

    Purity

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

    Citations

    More Info

    • Introduction

      GH is a member of the somatotropin/prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the growth hormone locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five growth hormones, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the growth hormone locus. Mutations in or deletions of the gene lead to growth hormone deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary growth hormone, Growth hormone 1, Somatotropin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Growth-Hormone although stable at room temperature for at least two weeks, should be stored desiccated below -18°C. Upon reconstitution and filter sterilization GH can be stored at 4°C, pH 9 for up to 4 weeks. For long term storage and more diluted solutions 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 Zebrafish Mutant G113R in 0.4% NaHCO3 or water adjusted to pH-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions, preferably in a presence of a carrier protein such as BSA or similar.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Gln-Arg-Leu-Phe-Asn.

    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.

    Growth Hormone Zebrafish Mutant
  • View Data Sheet

    Name :

    MME Human, Active

    Description:

    Membrane Metalloendopeptidase Human Recombinant, Active

    Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.

    Product # :

    ENZ-1116

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    Description

    MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.

    Citations

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    • Introduction

      Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.

    • Synonyms

      Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.

    • 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

      ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH

    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.

    Mme Protein
  • View Data Sheet

    Name :

    PTMS Human

    Description:

    Prothymosin Human Recombinant

    ParaT, parathymosin.

    Product # :

    PRO-1735

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    Description

    PTMS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 125 amino acids (1-102aa) and having a molecular mass of 13.9kDa.PTMS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PTMS protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Parathymosin, also known as PTMS is a member of the pro/parathymosin family. PTMS may mediate immune function by blocking the effect of prothymosin alpha which confers resistance to particular opportunistic infections. Among the diseases associated with PTMS are hepatitis b, and alzheimer's disease.

    • Synonyms

      ParaT, parathymosin.

    • 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 MGSMSEKSVE AAAELSAKDL KEKKEKVEEK ASRKERKKEV VEEEENGAEE EEEETAEDGE EEDEGEEEDE EEEEEDDEGP ALKRAAEEED EADPKRQKTE NGASA

    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.

    Ptms Human
  • View Data Sheet

    Name :

    Leptin Chicken

    Description:

    Leptin Chicken Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-505

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    Description

    Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

    Citations

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    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

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

      Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.

    • Protein content

      Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

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

    Leptin Chicken
  • View Data Sheet

    Name :

    Leptin Pufferfish

    Description:

    Leptin Pufferfish Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-530

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    Description

    Leptin Pufferfish (Takifugu rubripes) Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 16 kDa. Bioactive Leptin Pufferfish (Takifugu rubripes) Recombinant was prepared according to the sequence published by Kurokawa et al. (2005)Peptides 26, 745-750 in two forms: monomer and covalent dimer. MS analysis revealed molecular masses of 15,291 and 30,585 Da, close to the theoretical values of 15,270 and 30,540 Da. CD spectra revealed high similarity to mammalian leptins. Other details of its preparation will be soon published by Yacobovitz et al (in press), General and Comparative Endocrinology.The Pufferfish Leptin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pufferfish Leptin was lyophilized from a concentrated (0.85mg/ml) solution with 0.003mM NaHCO3.

    Purity

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

    Biological Activity

    Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. The affinity of human leptin receptors is considerably lower campared to mammalian leptins.

    Citations

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    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Pufferfish Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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 Pufferfish Leptin in sterile 0.4% NaHCO3 pH-9 not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      ALPGALDAMDVEKMKSKVTWKAQGLVARIDKHFPDRGLRFDTDKVE

      GSTSVVASLESYNNLISDRFGGVSQIKTEISSLAGYLNHWREGNCQE

      QQPKVWPRRNIFNHTVSLEALMRVREFLKLLQKNVDLLERC

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 1.28 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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 Pufferfish
  • View Data Sheet

    Name :

    SULT1B1 Human

    Description:

    Sulfotransferase Family, Cytosolic, 1B, Member 1 Human Recombinant

    Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.

    Product # :

    ENZ-610

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    Description

    SULT1B1 Human Recombinant produced in E. coli is a single polypeptide chain containing 320 amino acids (1-296) and having a molecular mass of 37.4kDa.SULT1B1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SULT1B1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

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    • Introduction

      SULT1B1 enzyme in humans is encoded by the SULT1B1 gene. SULT1B1 holds a binding site for 3-prime-phosphoadenosine 5-prime-phosphosulfate, a sulfate donor, in addition to a cysteine residue conserved in the ST1 gene family of sulfotransferases. Sulfotransferases like SULT1B1 catalyze the biotransformation of a great amount of endogenous amalgams such as bile acids, neurotransmitters, steroids, and thyroid hormones, in addition to drugs and xenobiotics.

    • Synonyms

      Sulfotransferase family cytosolic 1B member 1, Thyroid hormone sulfotransferase, Sulfotransferase 1B1, Sulfotransferase 1B2, ST1B1, EC 2.8.2.-, SULT1B2.

    • 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 MGSHMLSPKD ILRKDLKLVH GYPMTCAFAS NWEKIEQFHS RPDDIVIATY PKSGTTWVSE IIDMILNDGD IEKCKRGFIT EKVPMLEMTL PGLRTSGIEQ LEKNPSPRIV KTHLPTDLLP KSFWENNCKM IYLARNAKDV SVSYYHFDLM NNLQPFPGTW EEYLEKFLTG KVAYGSWFTH VKNWWKKKEE HPILFLYYED MKENPKEEIK KIIRFLEKNL NDEILDRIIH HTSFEVMKDN PLVNYTHLPT TVMDHSKSPF MRKGTAGDWK NYFTVAQNEK FDAIYETEMS KTALQFRTEI

    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.

    Sult1B1 Human
  • View Data Sheet

    Name :

    GH Mouse

    Description:

    GH Mouse Recombinant

    GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.

    Product # :

    CYT-540

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    Description

    Growth Hormone Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids and having a molecular mass of 22 kDa. Mouse GH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Mouse Growth Hormone Recombinant Lyophilized from a 0.2 μm filtered solution of 20mM HEPES, 4% Sucrose, 4% Mannitol, 0.02% Tween 80, pH 8.0.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.

    • Synonyms

      GH1, GH, GHN, GH-N, hGH-N, Pituitary GH, GH-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Growth Hormone Mouse
  • View Data Sheet

    Name :

    BDNF Human

    Description:

    Brain-Derived Neurotrophic Factor Human Recombinant

    Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    Product # :

    CYT-207

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    Description

    BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

    Purity

    BDNF is greater than 950% as determined SDS-PAGE.

    Biological Activity

    The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

    Activity

    bdnf activity - Product image 1

    Citations

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    • Introduction

      BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.

    • Synonyms

      Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

    • Background

      Final Thoughts

      Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.

      What is the molecular weight/Mw of BDNF Protein?
      BDNF Protein has a total Mw of 27kDa.

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

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

      What is the Biological Activity of BDNF Protein?
      The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

      What is the amino acid sequence of BDNF Protein?
      MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

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

    • Protein content

      BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor as a Reference Standard.

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

    Bdnf Human
  • View Data Sheet

    Name :

    PEPD Human

    Description:

    Peptidase D Human Recombinant

    Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.

    Product # :

    ENZ-856

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    Description

    PEPD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-493a.a.) and having a molecular mass of 56.9kDa.PEPD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    PEPD protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

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    • Introduction

      Peptidase D, also known as PEPD, Is a part of the peptidase family. PEPD is involved in collagen metabolism due to the high level of iminoacids in collagen. PEPD recycles proline, and sets the pace for the production of collagen. PEPD is also parts dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position.

    • Synonyms

      Xaa-Pro dipeptidase, X-Pro dipeptidase, Imidodipeptidase, Peptidase D, Proline dipeptidase, Prolidase, PRD, PEPD, Xaa-Pro dipeptidase isoform 1, PROLIDASE.

    • 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 MGSMAAATGP SFWLGNETLK VPLALFALNR QRLCERLRKN PAVQAGSIVV LQGGEETQRY CTDTGVLFRQ ESFFHWAFGV TEPGCYGVID VDTGKSTLFV PRLPASHATW MGKIHSKEHF KEKYAVDDVQ YVDEIASVLT SQKPSVLLTL RGVNTDSGSVCREASFDGIS KFEVNNTILH PEIVECRVFK TDMELEVLRY TNKISSEAHR EVMKAVKVGM KEYELESLFE HYCYSRGGMR HSSYTCICGS GENSAVLHYG HAGAPNDRTI QNGDMCLFDM GGEYYCFASD ITCSFPANGK FTADQKAVYE AVLRSSRAVM GAMKPGVWWP DMHRLADRIH LEELAHMGIL SGSVDAMVQA HLGAVFMPHG LGHFLGIDVH DVGGYPEGVE RIDEPGLRSL RTARHLQPGM VLTVEPGIYF IDHLLDEALA DPARASFLNR EVLQRFRGFG GVRIEEDVVV TDSGIELLTC VPRTVEEIEA CMAGCDKAFT PFSGPK.

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    Pepd Human
  • View Data Sheet

    Name :

    MMP 9 Rabbit

    Description:

    Matrix Metalloproteinase-9 Rabbit Recombinant

    Matrix metalloproteinase-9, MMP-9, 92 kDa type IV collagenase, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    Product # :

    ENZ-121

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    Description

    MMP-9 Rabbit Recombinant is a full length secreted protein (688 amino acids - a.a. 20-707). The MMP-9 is expressed in insect cells and fused to a 30 aa C-terminal Myc-His tag, having a total MW of 79.94kDa. Purified MMP9 protein appears at 95kDa on SDS-PAGE gel due to protein modification.

    Source

    Baculovirus system, insect cells.

    Formulation

    The MMP-9 solution (0.3mg/ml) contains 50mM Tris, 150mM NaCl, 10% Glycerol, pH 7.5.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases that break down extracellular matrix proteins. The MMP9 is secreted as a 92kDa zymogen. Cleavage of ProMMP-9 results in the active enzyme, having a molecular weight of approximately 82kDa. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by the several cell types: monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells. MMP9 is involved in inflammatory responses, tissue remodeling, wound healing, tumor growth and metastasis. MMP9 may also play an important part in local proteolysis of the extracellular matrix and in leukocyte migration, as well as in bone osteoclastic resorption. MMP9 cleaves type IV and type V collagens into large C-terminal three qu

    • Synonyms

      Matrix metalloproteinase-9, MMP-9, 92 kDa type IV collagenase, 92 kDa gelatinase, Gelatinase B, GELB, MMP9, CLG4B.

    • 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

      APRRRQPTLVVFPGELRTRLTDRQLAEEYLFRYGYTRVASMHGDSQSLRLPLLLLQK
      HLSLPETGELDNATLEAMRAPRCGVPDVGKFQTFEGDLKWHHHNITYWIQNYSEDLP
      RDVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHA
      FPPGPGIQGDAHFDDEELWSLGKGVVVPTYFGNADGAPCHFPFTFEGRSYTACTTD
      GRSDGMAWCSTTADYDTDRRFGFCPSERLYTQDGNADGKPCEFPFIFQGRTYSACT
      TDGRSDGHRWCATTASYDKDKLYGFCPTRADSTVVGGNSAGELCVFPFVFLGKEYS
      SCTSEGRRDGRLWCATTSNFDSDKKWGFCPDKGYSLFLVAAHEFGHALGLDHSSVP
      ERLMYPMYRYLEGSPLHEDDVRGIQHLYGPNPNPQPPATTTPEPQPTAPPTACPTWP
      ATVRPSEHPTTSPTGAPSAGPTGPPTASPSAAPTASLDPAEDVCNVNVFDAIAEIGNK
      LHVFKDGRYWRFSEGSGRRPQGPFLIADTWPALPAKLDSAFEEPLTKKLFFFSGRQV
      WVYTGASVLGPRRLDKLGLGPEVPHVTGALPRAGGKVLLFGAQRFWRFDVKTQTVD
      SRSGAPVDQMFPGVPLNTHDVFQYREKAYFCQDRFFWRVSTRNEVNLVDQVGYVS
      FDILHCPEDENLYFQGLEEQKLISEEDLNSAVDHHHHHH.

    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.

    Mmp 9 Rabbit
  • View Data Sheet

    Name :

    XPNPEP1 Human

    Description:

    X-Prolyl Aminopeptidase-1 Human Recombinant

    X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.

    Product # :

    ENZ-880

    Price :

    Quantity :

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    Shipped with Ice Packs

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    More Info

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

    Description

    XPNPEP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 655 amino acids (1-623 a.a) and having a molecular mass of 73.4kDa. XPNPEP1 is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    XPNPEP1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 20% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      X-Prolyl Aminopeptidase-1, also known as XPNPEP1 is a member of the peptidase M24B family. XPNPEP1 encodes the cytosolic form of a metalloaminopeptidase which catalyzes the cleavage of the N-terminal amino acid adjacent to a proline residue. Furthermore, XPNPEP1 plays a role in degradation as well as maturation of tachykinins, neuropeptides and peptide hormones.

    • Synonyms

      X-Prolyl Aminopeptidase (Aminopeptidase P) 1, Soluble, XPNPEPL, SAMP, X-Prolyl Aminopeptidase 1, Soluble, Aminoacylproline Aminopeptidase, Cytosolic Aminopeptidase P, Soluble Aminopeptidase P, X-Pro Aminopeptidase 1, EC 3.4.11.9, XPNPEPL1, X-Prolyl Aminopeptidase (Aminopeptidase P)-Like, Aminopeptidase P, Cytosolic, Xaa-Pro Aminopeptidase 1, XPNPEP, APP1, Xaa-Pro aminopeptidase 1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFELRRQ ASMPPKVTSE LLRQLRQAMR NSEYVTEPIQ AYIIPSGDAH QSEYIAPCDC RRAFVSGFDG SAGTAIITEE HAAMWTDGRY FLQAAKQMDS NWTLMKMGLK DTPTQEDWLV SVLPEGSRVG VDPLIIPTDY WKKMAKVLRS AGHHLIPVKE NLVDKIWTDR PERPCKPLLT LGLDYTGISW KDKVADLRLK MAERNVMWFV VTALDEIAWL FNLRGSDVEH NPVFFSYAII GLETIMLFID GDRIDAPSVK EHLLLDLGLE AEYRIQVHPY KSILSELKAL CADLSPREKV WVSDKASYAV SETIPKDHRC CMPYTPICIA KAVKNSAESE GMRRAHIKDA VALCELFNWL EKEVPKGGVT EISAADKAEE FRRQQADFVD LSFPTISSTG PNGAIIHYAP VPETNRTLSL DEVYLIDSGA QYKDGTTDVT RTMHFGTPTA YEKECFTYVL KGHIAVSAAV FPTGTKGHLL DSFARSALWD SGLDYLHGTG HGVGSFLNVH EGPCGISYKT FSDEPLEAGM IVTDEPGYYE DGAFGIRIEN VVLVVPVKTK YNFNNRGSLT FEPLTLVPIQ TKMIDVDSLT DKECDWLNNY HLTCRDVIGK ELQKQGRQEA LEWLIRETQP ISKQH.

    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.

    Xpnpep1 Human
  • View Data Sheet

    Name :

    PFN2 Human

    Description:

    Profilin-2 Human Recombinant

    Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    Product # :

    PRO-809

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

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

    Description

    PFN2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.2 kDa. PFN2 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN2 protein solution (1mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PFN2 is a ubiquitous actin monomer-binding protein which is part of the profilin family. PFN2 regulates actin polymerization in response to extra cellular signals. PFN2 binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, while it increases it at low concentrations. PFN2 binds to PIP2, it inhibits the formation of IP3 and DG.

    • Synonyms

      Profilin-II, PFN2, Profilin-2, PFL, D3S1319E.

    • 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 MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF TNGLALGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH GGGLNKKAYS MAKYLRDSGF.

    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.

    Pfn2 Human
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