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Search results

1000 results found for “phosphatase and tensin”

Name

Description

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  • View Data Sheet

    Name :

    UBLCP1 Human

    Description:

    Ubiquitin-Like Domain Containing CTD Phosphatase 1 Human Recombinant

    CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

    Product # :

    PRO-151

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    • source
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    • More Info

    Description

    UBLCP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (1-318 a.a) and having a molecular mass of 39.2kDa.UBLCP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBLCP1 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin-like domain-containing CTD phosphatase 1 (UBLCP1) dephosphorylates 26S nuclear proteasomes, thereby decreasing their proteolytic activity. The dephosphorylation averts assembly of the core and regulatory particles (CP and RP) into mature 26S proteasome.

    • Synonyms

      CPUB1, Ubiquitin-like domain-containing CTD phosphatase 1, Nuclear proteasome inhibitor UBLCP1.

    • 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 MGSMALPIIV KWGGQEYSVT TLSEDDTVLD LKQFLKTLTG VLPERQKLLG LKVKGKPAEN DVKLGALKLK PNTKIMMMGT REESLEDVLG PPPDNDDVVN DFDIEDEVVE VENREENLLK ISRRVKEYKV EILNPPREGK KLLVLDVDYT LFDHRSCAET GVELMRPYLH EFLTSAYEDY DIVIWSATNM KWIEAKMKEL GVSTNANYKI TFMLDSAAMI TVHTPRRGLI DVKPLGVIWG KFSEFYSKKN TIMFDDIGRN FLMNPQNGLK IRPFMKAHLN RDKDKELLKL TQYLKEIAKL DDFLDLNHKY WERYLSKKQG Q.

    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.

    Ublcp1 Human
  • View Data Sheet

    Name :

    Darbepoetin

    Description:

    Darbepoetin-Alpha Human Recombinant

    Erythropoietin-Mutant, EPO-mutant, NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    Product # :

    CYT-1263

    Price :

    Quantity :

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    Description

    Darbepoetin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a glycosylated polypeptide chain containing 165 amino acids and having a predicted molecular mass of 18,200 Dalton and apparent glycosylated molecular mass of 37-40kDa. Darbepoetin is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells(CHO).

    Formulation

    Each mg of lyophilized Darbepoetin powder contains 20mM Phosphate Buffer, 0.15M NaCl pH-6.2 & 0.005% Tween-80.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

    More Info

    • Introduction

      Darbepoetin is a mutant recombinant human EPO-Alpha protein re-engineered, containing 5 amino acid changes at N30, T32, V87, N88, T90. Darbepoetin exhibits longer half-life stimulating red blood cell production than Erythropoietin. Darbepoetin maintains hemoglobin more effectively compared to EPO-Alpha.

    • Synonyms

      NESP, Novel Erythropoiesis Stimulating Protein, EPO Mutant.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD.

    • Background

      What is the molecular weight/Mw of DARBEPOETIN Protein?
      DARBEPOETIN Protein has a total Mw of 38.5kDa.

      What is the source or expression system of DARBEPOETIN Protein?
      Chinese Hamster Ovary Cells(CHO).

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

      What is the Biological Activity of DARBEPOETIN Protein?
      The Specific Activity was measured by Normocyth -aemic mice and was found to be 1,000,000 IU/mg.

      What is the amino acid sequence of DARBEPOETIN Protein?
      APPRLICDSR VLERYLLEAK EAENITTGCN ETCSLNENIT VPDTKVNFYA WKRMEVGQQA VEVWQGLALL SEAVLRGQAL LVNSSQVNET LQLHVDKAVS GLRSLTTLLR ALGAQKEAIS PPDAASAAPL RTITADTFRK LFRVYSNFLR GKLKLYTGEA CRTGD

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

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

    Darbepoetin
  • View Data Sheet

    Name :

    PPM1F Antibody

    Description:

    Protein Phosphatase 1F, Mouse Anti Human

    Protein phosphatase 1F, Ca(2+)/calmodulin-dependent protein kinase phosphatase, CaM-kinase phosphatase, CaMKPase, Partner of PIX 2, Protein fem-2 homolog, hFem-2, KIAA0015, POPX2, PPM1F, CAMKP, FEM-2.

    Product # :

    ANT-502

    Price :

    Quantity :

    Shipping Method :

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    • formulation
    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      Protein Phosphatase 1F (PPM1F) is a part of the PP2C family of Ser/Thr protein phosphatases whose members are known to be negative regulators of cell stress response pathways. PPM1F interacts with Rho guanine nucleotide exchange factors (PIX), and as a result blocks the effects of p21-activated kinase 1 (PAK), a protein kinase mediating biological effects downstream of Rho GTPases. Calcium/calmodulin-dependent protein kinase II gamma (CAMK2G/CAMK-II) is one of the substrates of PPM1F. PPM1F is found to be an apoptosis Promoter.

    • Synonyms

      Protein phosphatase 1F, Ca(2+)/calmodulin-dependent protein kinase phosphatase, CaM-kinase phosphatase, CaMKPase, Partner of PIX 2, Protein fem-2 homolog, hFem-2, KIAA0015, POPX2, PPM1F, CAMKP, FEM-2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PPM1F mAb, clone PAT6D11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PPM1F protein 1-454 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and k light chain.

    • Clone

      PAT6D11AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PPM1F antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Ppm1F Antibody
  • View Data Sheet

    Name :

    MBP E.Coli, His

    Description:

    Maltose Binding Protein E.coli Recombinant, His Tag

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2322

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • 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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

    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.

    Mbp Ecoli His
  • View Data Sheet

    Name :

    MME Human

    Description:

    Membrane Metalloendopeptidase Human Recombinant

    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-1053

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    Description

    MME Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 a.a.) and having a molecular mass of 80.9kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).MME is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Membrane Metalloendopeptidase, also known as MME is a zinc metallopeptidase which is expressed at the cell surface of various cells. MME degrades the amyloid beta peptide whose abnormal misfolding as well as aggregation in neural tissue has been implicated as the cause for Alzheimer's disease. MME is expressed in an extended range of tissues and is especially plentiful in the kidney. MME is also a common acute lymphocytic leukemia antigen which is a significant cell surface marker in the diagnosis of human acute lymphocytic leukemia (ALL). MME is used in hematological diagnosis because it is expressed by early B, pro-B and pre-B lymphocytes, and also by lymph node germinal centers.

    • 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 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

      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 EIMSTVNISI TNEEDVVVYA PEYLTKLKPI 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

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    MME Human
  • View Data Sheet

    Name :

    ACE Human

    Description:

    Angiotensin Converting Enzyme Human Recombinant

    Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    Product # :

    ENZ-1156

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    Description

    ACE Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 1235 amino acids (30-1256 a.a.) and having a molecular mass of 142kDa. ACE is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/mg. Defined by the amount of enzyme that cleaves 1pmol of McaRPPGFSAFK(Dnp)-OH per minute at 25C˚.

    More Info

    • Introduction

      Angiotensin Converting Enzyme (ACE) is a zinc metallopeptidase vital for blood pressure control and salt and water metabolism.ACE converts angiotensin I to angiotensin II by release of the terminal His-Leu which causes the vasoconstrictor activity of angiotensin to increase.ACE inactivates bradykinin, a potent vasodilator and has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety.

    • Synonyms

      Angiotensin-converting enzyme, ACE, Dipeptidyl carboxypeptidase I, Kininase II, CD_antigen: CD143, DCP, DCP1, ACE1, CD143

    • 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

      LDPGLQPGNF SADEAGAQLF AQSYNSSAEQ VLFQSVAASW AHDTNITAEN ARRQEEAALL SQEFAEAWGQ KAKELYEPIW QNFTDPQLRR IIGAVRTLGS ANLPLAKRQQ YNALLSNMSR IYSTAKVCLP NKTATCWSLD PDLTNILASS RSYAMLLFAW EGWHNAAGIP LKPLYEDFTA LSNEAYKQDG FTDTGAYWRS WYNSPTFEDD LEHLYQQLEP LYLNLHAFVR RALHRRYGDR YINLRGPIPA HLLGDMWAQS WENIYDMVVP FPDKPNLDVT STMLQQGWNA THMFRVAEEF FTSLELSPMP PEFWEGSMLE KPADGREVVC HASAWDFYNR KDFRIKQCTR VTMDQLSTVH HEMGHIQYYL QYKDLPVSLR RGANPGFHEA IGDVLALSVS TPEHLHKIGL LDRVTNDTES DINYLLKMAL EKIAFLPFGY LVDQWRWGVF SGRTPPSRYN FDWWYLRTKY QGICPPVTRN ETHFDAGAKF HVPNVTPYIR YFVSFVLQFQ FHEALCKEAG YEGPLHQCDI YRSTKAGAKL RKVLQAGSSR PWQEVLKDMV GLDALDAQPL LKYFQPVTQW LQEQNQQNGE VLGWPEYQWH PPLPDNYPEG IDLVTDEAEA SKFVEEYDRT SQVVWNEYAE ANWNYNTNIT TETSKILLQK NMQIANHTLK YGTQARKFDV NQLQNTTIKR IIKKVQDLER AALPAQELEE YNKILLDMET TYSVATVCHP NGSCLQLEPD LTNVMATSRK YEDLLWAWEG WRDKAGRAIL QFYPKYVELI NQAARLNGYV DAGDSWRSMY ETPSLEQDLE RLFQELQPLY LNLHAYVRRA LHRHYGAQHI NLEGPIPAHL LGNMWAQTWS NIYDLVVPFP SAPSMDTTEA MLKQGWTPRR MFKEADDFFT SLGLLPVPPE FWNKSMLEKP TDGREVVCHA SAWDFYNGKD FRIKQCTTVN LEDLVVAHHE MGHIQYFMQY KDLPVALREG ANPGFHEAIG DVLALSVSTP KHLHSLNLLS SEGGSDEHDI NFLMKMALDK IAFIPFSYLV DQWRWRVFDG SITKENYNQE WWSLRLKYQG LCPPVPRTQG DFDPGAKFHI PSSVPYIRYF VSFIIQFQFH EALCQAAGHT GPLHKCDIYQ SKEAGQRLAT AMKLGFSRPW PEAMQLITGQ PNMSASAMLS YFKPLLDWLR TENELHGEKL GWPQYNWTPN SARSEGPLPD SGRVSFLGLD LDAQQARVEH HHHHH

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    Ace Human
  • View Data Sheet

    Name :

    SPP1 Human

    Description:

    Osteopontin Human Recombinant

    Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    Product # :

    CYT-635

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    Description

    Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
      Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.

    • Synonyms

      Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.

    • 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 RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.

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    Spp1 Human
  • View Data Sheet

    Name :

    CTSS Antibody

    Description:

    Cathepsin-S, Mouse Anti Human

    Cathepsin S, MGC3886, CTSS, Cathepsin-S.

    Product # :

    ANT-485

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.

    • Synonyms

      Cathepsin S, MGC3886, CTSS, Cathepsin-S.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human CTSS mAb, clone PAT1F9A, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CTSS protein 17-331 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2b heavy chain and Kappa light chain.

    • Clone

      PAT1F9AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:500.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      CTSS antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Ctss Antibody
  • View Data Sheet

    Name :

    MMP 8 Human, His

    Description:

    Matrix Metalloproteinase-8 Human Recombinant, His Tag

    CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.

    Product # :

    ENZ-766

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    Description

    MMP 8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (101-467a.a) and having a molecular mass of 44.3kDa. MMP 8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MMP 8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Full-length recombinant human neutrophil pro-collagenase (MMP-8), latent form.
      Matrix metalloproteinase 8 (MMP-8), or neutrophil collagenase, degrades interstitial collagens, acting preferentially on collagen type I.
      Increased full-length MMP-8 protein was associated with infiltration into the skin of neutrophils, which are the major cell type that expresses MMP-8.
      MMP-8 is synthesized and stored in specific granules in neutrophil leukocytes. MMP-8 activity is therefore regulated by factors such as surface-bound ligands (IgG or complement components) that release it through degranulation.Once released and activated through proteolytic or oxidative mechanisms, MMP-8 plays a major role in the connective tissue turnover that accompanies inflammatory processes.

    • Synonyms

      CLG1, HNC, MMP-8, PMNL-CL, Neutrophil collagenase, Matrix metalloproteinase-8, MMP-8, PMNL collagenase.

    • 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 MGSLTPGNPK WERTNLTYRI RNYTPQLSEA EVERAIKDAF ELWSVASPLI FTRISQGEAD INIAFYQRDH GDNSPFDGPN GILAHAFQPG QGIGGDAHFD AEETWTNTSA NYNLFLVAAH EFGHSLGLAH SSDPGALMYP NYAFRETSNY SLPQDDIDGI QAIYGLSSNP IQPTGPSTPK PCDPSLTFDA ITTLRGEILF FKDRYFWRRH PQLQRVEMNF ISLFWPSLPT GIQAAYEDFD RDLIFLFKGN QYWALSGYDI LQGYPKDISN YGFPSSVQAI DAAVFYRSKT YFFVNDQFWR YDNQRQFMEP GYPKSISGAF PGIESKVDAV FQQEHFFHVF SGPRYYAFDL IAQRVTRVAR GNKWLNCRYG.

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    Mmp 8 Human His
  • View Data Sheet

    Name :

    HSD17B14 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 14 Human Recombinant

    17-beta-hydroxysteroid dehydrogenase 14, 17-beta-HSD 14, 17-beta-hydroxysteroid dehydrogenase DHRS10, Dehydrogenase/reductase SDR family member 10, Retinal short-chain dehydrogenase/reductase retSDR3, HSD17B14, DHRS10, SDR3, SDR47C1, retSDR3.

    Product # :

    ENZ-029

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    Description

    HSD17B14 Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 306 amino acids (1-270 a.a.) and having a molecular mass of 32.4kDa. The HSD17B14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSD17B14 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      17-beta-hydroxysteroid dehydrogenase 14 (HSD17B14) is a member of the 17-beta-HSD family of proteins, which regulate the availability of steroids within various tissues throughout the body. 17-beta-hydroxysteroid dehydrogenases (HSD17B14) are mainly involved in metabolism of steroids at the C17 position and also of other substrates, such as fatty acids, prostaglandins, and xenobiotics. HSD17B14 exists as a homotetramer that localizes to the cytoplasm and is highly expressed in the brain, placenta, liver and kidney.

    • Synonyms

      17-beta-hydroxysteroid dehydrogenase 14, 17-beta-HSD 14, 17-beta-hydroxysteroid dehydrogenase DHRS10, Dehydrogenase/reductase SDR family member 10, Retinal short-chain dehydrogenase/reductase retSDR3, HSD17B14, DHRS10, SDR3, SDR47C1, retSDR3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMATG TRYAGKVVVV TGGGRGIGAG IVRAFVNSGA RVVICDKDES GGRALEQELP GAVFILCDVT QEDDVKTLVS ETIRRFGRLD CVVNNAGHHP PPQRPEETSA QGFRQLLELN LLGTYTLTKL ALPYLRKSQG NVINISSLVG AIGQAQAVPY VATKGAVTAM TKALALDESP YGVRVNCISP GNIWTPLWEE LAALMPDPRA TIREGMLAQP LGRMGQPAEV GAAAVFLASE ANFCTGIELL VTGGAELGYG CKASRSTPVD APDIPS.

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    Hsd17B14 Human
  • View Data Sheet

    Name :

    CSK Human

    Description:

    C-Src Tyrosine Kinase Human Recombinant

    Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.

    Product # :

    PKA-062

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    Description

    CSK Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 473 amino acids (1-450) and having a molecular mass of 53.1 kDa.The CSK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSK protein (0.5mg/ml) is containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      C-Src Tyrosine Kinase, also known as CSK, regulates cell growth, migration, differentiation, and immune response. CSK Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases. CSK is a protein coding gene which suppresses signaling by several surface receptors. Among CSK's related pathways are PI-3K cascade and Signaling by FGFR.

    • Synonyms

      Tyrosine-protein kinase CSK, C-Src kinase, Protein-tyrosine kinase CYL, CSK, C-Src Tyrosine Kinase.

    • 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 MGSMSAIQAA WPSGTECIAK YNFHGTAEQD LPFCKGDVLT IVAVTKDPNW YKAKNKVGRE GIIPANYVQK REGVKAGTKL SLMPWFHGKI TREQAERLLY PPETGLFLVR ESTNYPGDYT LCVSCDGKVE HYRIMYHASK LSIDEEVYFE NLMQLVEHYT SDADGLCTRL IKPKVMEGTV AAQDEFYRSG WALNMKELKL LQTIGKGEFG DVMLGDYRGN KVAVKCIKND ATAQAFLAEA SVMTQLRHSN LVQLLGVIVE EKGGLYIVTE YMAKGSLVDY LRSRGRSVLG GDCLLKFSLD VCEAMEYLEG NNFVHRDLAA RNVLVSEDNV AKVSDFGLTK EASSTQDTGK LPVKWTAPEA LREKKFSTKS DVWSFGILLW EIYSFGRVPY PRIPLKDVVP RVEKGYKMDA PDGCPPAVYE VMKNCWHLDA AMRPSFLQLR EQLEHIKTHE LHL.

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    Csk Human
  • View Data Sheet

    Name :

    CTGF Human (183-255)

    Description:

    Connective Tissue Growth Factor (183-255 a.a.) Human Recombinant

    CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    Product # :

    CYT-1174

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    Description

    CTGF Human Recombinant is a single, glycosylated polypeptide chain containing 80 amino acids (183-255a.a) and having a molecular mass of 9.1kDa (calculated). CTGF is fused to a 7 a.a His tag at N-terminal.

    Source

    HEK293 cells.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Connective Tissue Growth Factor is a part of the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF, Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: tumorigenesis,fibrosis and vascular ailments. Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes.
      The full length protein consists of 4 modules: Module I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
      Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
      Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion.
      Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins.
      Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy.
      In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells.
      CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.

    • Synonyms

      CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

    • 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 deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.

    • Background

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

      What is the source or expression system of CTGF Protein?
      HEK293 cells.

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

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

      What is the amino acid sequence of CTGF Protein?
      MHHHHHHRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK.

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

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

    Ctgf Protein
  • View Data Sheet

    Name :

    SARS Human

    Description:

    Seryl-tRNA Synthetase Human Recombinant

    Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    Product # :

    ENZ-229

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    Description

    SARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 537 amino acids (1-514) and having a molecular mass of 61.2kDa.SARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Seryl-tRNA synthetase, cytoplasmic (SARS) is a member of the class-II aminoacyl-tRNA synthetase family. Aminoacyl-tRNA synthetases’ role is to catalyze the aminoacylation of tRNAs by their corresponding amino acids, as a result linking amino acids with tRNA-contained nucleotide triplets. The SARS enzyme catalyzes the attachment of serine to tRNA (Ser). SARS enzyme is probably able to aminoacylate tRNA (Sec) with serine, to form the misacylated tRNA L-seryl-tRNA (Sec), which will be then converted into selenocysteinyl-tRNA (Sec).

    • Synonyms

      Serine--tRNA ligase cytoplasmic, Seryl-tRNA synthetase, SerRS, Seryl-tRNA(Ser/Sec) synthetase, SARS, SERS.

    • 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 MGSMVLDLDL FRVDKGGDPA LIRETQEKRF KDPGLVDQLV KADSEWRRCR FRADNLNKLK NLCSKTIGEK MKKKEPVGDD ESVPENVLSF DDLTADALAN LKVSQIKKVR LLIDEAILKC DAERIKLEAE RFENLREIGN LLHPSVPISN DEDVDNKVER IWGDCTVRKK YSHVDLVVMV DGFEGEKGAV VAGSRGYFLK GVLVFLEQAL IQYALRTLGS RGYIPIYTPF FMRKEVMQEV AQLSQFDEEL YKVIGKGSEK SDDNSYDEKY LIATSEQPIA ALHRDEWLRP EDLPIKYAGL STCFRQEVGS HGRDTRGIFR VHQFEKIEQF VYSSPHDNKS WEMFEEMITT AEEFYQSLGI PYHIVNIVSG SLNHAASKKL DLEAWFPGSG AFRELVSCSN CTDYQARRLR IRYGQTKKMM DKVEFVHMLN ATMCATTRTI CAILENYQTE KGITVPEKLK EFMPPGLQEL IPFVKPAPIE QEPSKKQKKQ HEGSKKKAAA RDVTLENRLQ NMEVTDA.

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    Sars Human
  • View Data Sheet

    Name :

    Desmin Human

    Description:

    Desmin Human Recombinant

    Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    Product # :

    PRO-520

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    Description

    Desmin Human Recombinant having a calculated molecular mass of 53,539 Dalton, showing a 55kDa band on SDS-page, pI-5.16.

    Source

    Escherichia Coli.

    Formulation

    Desmin was lyophilized from a 1mg/ml solution containing 30mM Tris-HCl pH 8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Desmin is a muscle-specific class III intermediate filament. Homopolymers of this protein form a stable intracytoplasmic filamentous network connecting myofibrils to each other and to the plasma membrane. Mutations in this gene are associated with desmin-related myopathy, a familial cardiac and skeletal myopathy (CSM), and with distal myopathies.

    • Synonyms

      Desmin, DES, CSM1, CSM2, CMD1I, FLJ12025, FLJ39719, FLJ41013, FLJ41793.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Desmin between 2-8°C, do not freeze. Upon reconstitution Desmin should be stored at -20°C. Please prevent freeze-thaw cycles.

    • Solubility

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

    • Reconstitution to filaments

      After Desmin is dissolved in 9.5M urea buffer (see formulation), protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4M urea and then to low salt condition (50mM NaCl, 2mM dithiothreitol, 10mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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    Desmin Human
  • View Data Sheet

    Name :

    DHRS9 Human

    Description:

    Dehydrogenase/Reductase Member 9 Human Recombinant

    Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.

    Product # :

    ENZ-216

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    Description

    DHRS9 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 327 amino acids (18-319) and having a molecular mass of 35.9kDa.DHRS9 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHRS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 9 (DHRS9) functions as a homotetramer, which converts both 3-alpha-tetrahydroprogesterone (allopregnanolone) and 3-alpha-androstanediol to dihydroxyprogesterone and is believed to have a part in retinoic acid biosynthesis.

    • Synonyms

      Dehydrogenase/reductase SDR family member 9, 3-alpha hydroxysteroid dehydrogenase, 3-alpha-HSD, NADP-dependent retinol dehydrogenase/reductase, RDH-E2, RDHL, Short-chain dehydrogenase/reductase retSDR8, DHRS9, RDH15, RDHTBE, SDR9C4, RETSDR8, 3ALPHA-HSD.

    • 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 MGSHMRKGKL KIEDITDKYI FITGCDSGFG NLAARTFDKK GFHVIAACLT ESGSTALKAE TSERLRTVLL DVTDPENVKR TAQWVKNQVG EKGLWGLINN AGVPGVLAPT DWLTLEDYRE PIEVNLFGLI SVTLNMLPLV KKAQGRVINV SSVGGRLAIV GGGYTPSKYA VEGFNDSLRR DMKAFGVHVS CIEPGLFKTN LADPVKVIEK KLAIWEQLSP DIKQQYGEGY IEKSLDKLKG NKSYVNMDLS PVVECMDHAL TSLFPKTHYA AGKDAKIFWI PLSHMPAALQ DFLLLKQKAE LANPKAV.

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    Dhrs9 Human
  • View Data Sheet

    Name :

    HYAL1 Human

    Description:

    Hyaluronidase Human Recombinant

    Hyaluronidase-1, Hyal-1,Hyaluronoglucosaminidase-1, Lung carcinoma protein 1, LuCa-1, HYAL1, Hyaluronidase 1, Hyaluronoglucosaminidase 1, Hyaluronoglucosaminidase1, LUCA 1,MPS9, NAT6, Plasma hyaluronidase, Tumor suppressor LUCA 1.

    Product # :

    ENZ-1155

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    Description

    HYAL1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-435 a.a) containing a total of 420 amino acids, having a molecular mass of 46.9 kDa. HYAL1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The HYAL1 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hyaluronidase-1 or HYAL1 is a protein, part of the endolytic glycoside hydrolase proteins group. Human hyaluronidases proteins, are 5 endo­β­N­acetyl­hexosaminidases (including HYAL1, HYAL2, HYAL3). Hyaluronidase-1 causes degradation to hyaluronic acid in the extracellular matrix of somatic tissues. HYAL1 needs an acidic environment and is the most common hyaluronidase in the plasma. Mutations in this protein can lead to mucopolysaccharidosis type IX and hyaluronidase deficiency.

    • Synonyms

      Hyaluronidase-1, Hyal-1,Hyaluronoglucosaminidase-1, Lung carcinoma protein 1, LuCa-1, HYAL1, Hyaluronidase 1, Hyaluronoglucosaminidase 1, Hyaluronoglucosaminidase1, LUCA 1,MPS9, NAT6, Plasma hyaluronidase, Tumor suppressor LUCA 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

      FRGPLLPNRP FTTVWNANTQ WCLERHGVDV DVSVFDVVAN PGQTFRGPDM TIFYSSQLGT YPYYTPTGEP VFGGLPQNAS LIAHLARTFQ DILAAIPAPD FSGLAVIDWE AWRPRWAFNW DTKDIYRQRS RALVQAQHPD WPAPQVEAVA QDQFQGAARA WMAGTLQLGR ALRPRGLWGF YGFPDCYNYD FLSPNYTGQC PSGIRAQNDQ LGWLWGQSRA LYPSIYMPAV LEGTGKSQMY VQHRVAEAFR VAVAAGDPNL PVLPYVQIFY DTTNHFLPLD ELEHSLGESA AQGAAGVVLW VSWENTRTKE SCQAIKEYMD TTLGPFILNV TSGALLCSQA LCSGHGRCVR RTSHPKALLL LNPASFSIQL TPGGGPLSLR GALSLEDQAQ MAVEFKCRCY PGWQAPWCER KSMWHHHHHH

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    Hyaluronidase Enzyme
  • View Data Sheet

    Name :

    IDE Human

    Description:

    Insulin-Degrading Enzyme Human Recombinant

    Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.

    Product # :

    ENZ-813

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    Description

    IDE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Leu1019) containing 1026 amino acids including a 7 aa His tag at C-terminus. The total calculated molecular mass is 119kDa.

    Source

    Escherichia Coli.

    Formulation

    IDE filtered (0.4µm) in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 10% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase which degrades intracellular insulin, and thus terminates insulins activity, as well as playing a part in intercellular peptide signaling by degrading various peptides such as amylin, bradykinin, and kallidin. The preferential affinity of the IDE enzyme for insulin results in insulin-mediated inhibition of the degradation of additional peptides such as beta-amyloid. Deficiencies in IDE protein's function are linked with Alzheimer's disease and type 2 diabetes mellitus nevertheless mutations in the IDE gene have not been demonstrated to be causative for these diseases. Insulin-Degrading Enzyme localizes mainly to the cytoplasm however in some cell types it localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. In addition, IDE degrades amyloid formed by APP and IAPP. Furthermore, IDE plays a part in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

    • Synonyms

      Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.

    • Physical Appearance

      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

      MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE LLKFHSAYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR GLPLFPLVKP HINFMAAKL E HHHHHH.

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    Ide Human
  • View Data Sheet

    Name :

    SMS Human

    Description:

    Spermine Synthase Human Recombinant

    Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    Product # :

    ENZ-230

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    Description

    SMS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-366) and having a molecular mass of 43.8kDa.SMS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Spermine synthase (SMS) is amember of the spermidine/spermine synthase family. SMS is an enzyme which converts spermidine into spermine. The SMS enzyme is essential for normal viability, growth and fertility involved in polyamine metabolism. Defects in the SMS gene are the cause of Snyder-Robinson syndrome (SRS), also known as X-linked mental retardation Snyder-Robinson type. SRS is categorized by moderate intellectual deficit, hypotonia, an unsteady gait, osteoporosis, kyphoscoliosis and facial asymmetry, its transmission is X-linked recessive.

    • Synonyms

      Spermine synthase, SPMSY, Spermidine aminopropyltransferase, SMS, SRS, SpS, MRSR.

    • 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 MGSHMAAARH STLDFMLGAK ADGETILKGL QSIFQEQGMA ESVHTWQDHG YLATYTNKNG SFANLRIYPH GLVLLDLQSY DGDAQGKEEI DSILNKVEER MKELSQDSTG RVKRLPPIVR GGAIDRYWPT ADGRLVEYDI DEVVYDEDSP YQNIKILHSK QFGNILILSG DVNLAESDLA YTRAIMGSGK EDYTGKDVLI LGGGDGGILC EIVKLKPKMV TMVEIDQMVI DGCKKYMRKT CGDVLDNLKG DCYQVLIEDC IPVLKRYAKE GREFDYVIND LTAVPISTSP EEDSTWEFLR LILDLSMKVL KQDGKYFTQG NCVNLTEALS LYEEQLGRLY CPVEFSKEIV CVPSYLELWV FYTVWKKAKP.

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    Sms Human
  • View Data Sheet

    Name :

    Omentin Human, His

    Description:

    Omentin Human Recombinant, His Tag

    Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    Product # :

    CYT-551

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    Description

    Omentin Human Recombinant is produced in E.Coli by recombinant DNA technology is a single, polypeptide chain containing 294 amino acids and having a molecular mass of 32.7 kDa. Recombinant Human Omentin contains His tag fused at N-Terminus.Intelectin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of lyophilized powder contains 20mM Tris & 50mM NaCl pH-8.0.

    Purity

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

    More Info

    • Introduction

      Omentin is a recently recognized gene highly localized to the mental tissue (visceral adipose tissue). Omentin is present in the stromal vascular cells in the adipose tissue rather than in the adipocytes. Omentin is predominantly expressed in the visceral adipose tissue than the subcutaneous tissue, with the omentin mRNA being 150 times higher in the visceral adipose tissue. Omentin has also been detected in human blood using western blot analysis, and seems to increase insulin-stimulated glucose uptake in 3T3-L1 adipocytes in mice. Omentin seems to increase Akt phosphorylation irrespective of insulin presence. Its role in glucose metabolism and obesity remains to be described; an insulin-sensitizing action is possible.Differences in Omentin expression has been noted in adipose tissue from normals and patients with inflammatory bowel disease although its significance is unknown.

    • Synonyms

      Intelectin-1, HL1, LFR, HL-1, INTL, ITLN, hIntL.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASTDEANT YFKEWTCSSS PSLPRSCKEI KDECPSAFDG LYFLRTENGV IYQTFCDMTS GGGGWTLVAS VHENDMRGKC TVGDRWSSQQ GSKAVYPEGD GNWANYNTFG SAEAATSDDY KNPGYYDIQA KDLGIWHVPN KSPMQHWRNS SLLRYRTDTG FLQTLGHNLF GIYQKYPVKY GEGKCWTDNG PVIPVVYDFG DAQKTASYYS PYGQREFTAG FVQFRVFNNE RAANALCAGM RVTGCNTEHH CIGGGGYFPE ASPQQCGDFS GFDWSGYGTH VGYS.

    • Applications

      Elisa
      Western blot.

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    Omentin Human His
  • View Data Sheet

    Name :

    ErbB3 Mouse

    Description:

    Tyrosine Kinase ErbB-3 Mouse Recombinant

    Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.

    Product # :

    PKA-085

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    Description

    ErbB3 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 630 amino acids (20-641.a.) and having a molecular mass of 69.5kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ErbB3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ErbB3 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ErbB3, also called Her3 (human epidermal growth factor receptor 3), is a type I membrane glycoprotein that is a member of the ErbB family of tyrosine kinase receptors. ErbB family members serve as receptors for the epidermal growth factor (EGF) family of growth factors. Among ErbB family members, ErbB3 is unique in that it contains a defective kinase domain. ErbB3 is expressed in keratinocytes, melanocytes, skeletal muscle cells, embryonic myoblasts and Schwann cells. Monomeric ErbB3 serves as a low affinity receptor for the heregulins (HRG). ErbB3 can induce specific antibody production in vivo, hence to inhibit tumor cell growth. ErbB-3 can be used to treat early, medium and advanced or post-operative breast cancer with over-expression of ErbB2. According to its mechanism of action, ErbB3 is classified as a therapeutic for cancer.

    • Synonyms

      Receptor tyrosine-protein kinase erbB-3, Glial growth factor receptor, Proto-oncogene-like protein c-ErbB-3.

    • 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

      SEMGNSQAVC PGTLNGLSVT GDADNQYQTL YKLYEKCEVV MGNLEIVLTG HNADLSFLQW IREVTGYVLV AMNEFSVLPL PNLRVVRGTQ VYDGKFAIFV MLNYNTNSSH ALRQLRFTQL TEILLGGVYI EKNDKLCHMD TIDWRDIVRV PDAEIVVKNN GGNCPPCHEV CKGRCWGPGP EDCQILTKTI CAPQCNGRCF GPNPNQCCHD ECAGGCSGPQ DTDCFACRHF NDSGACVPRC PAPLVYNKLT FQLEPNPHIK YQYGGVCVAS CPHNFVVDQT FCVRACPADK MEVDKNGLKM CEPCRGLCPK ACEGTGSGSR YQTVDSSNID GFVNCTKILG NLDFLITGLN GDPWHKIPAL DPEKLNVFRT VREITGYLNI QSWPPHMHNF SVFSNLTTIG GRSLYNRGFS LLIMKNLNVT SLGFRSLKEI SAGRVYISAN QQLCYHHSLN WTRLLRGPAE ERLDIKYNRP LGECVAEGKV CDPLCSSGGC WGPGPGQCLS CRNYSREGVC VTHCNVLQGE PREFVHEAHC FSCHPECQPM EGTSTCNGSG SDACARCAHF RDGPHCVNSC PHGILGAKGP IYKYPDAQNE CRPCHENCTQ GCKGPELQDC LGQAEVLMSK PHLEHHHHHH.

    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.

    Erbb3 Mouse
  • View Data Sheet

    Name :

    GAPDH Mouse, Active

    Description:

    GAPDH Mouse Recombinant, Active

    Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    Product # :

    ENZ-986

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    Description

    GAPDH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 356 amino acids (1-333a.a.) and having a molecular mass of 38.2kDa.GAPDH is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GAPDH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 40 units/mg, and is defined as the amount of enzyme that convert 1.0 umole of glyceraldehyde-3-phosphate to 1,3-Bisphosphoglycerate per minute at pH 8.5 at 37C.

    More Info

    • Introduction

      GAPDH is a catalytic enzyme normally known to play a role in glycolysis. GAPDH exists as a tetramer composed of 36-kDa subunits and has a range of intracellular functions. GAPDH catalyzes the reversible reduction of 1,3-bisphosphoglycerate to glyceraldehyde 3-phosphophate in the presence of NADPH. Besides functioning as a glycolytic enzyme in cytoplasm, GAPDH has function in intracellular processes such as membrane fusion, microtubule bundling, phosphotransferase activity, nuclear RNA export, DNA replication and DNA repair. GAPDH catalyzes a vital energy-yielding step in carbohydrate metabolism, the reversible oxidative phosphorylation of glyceraldehyde-3-phosphate in the presence of inorganic phosphate and nicotinamide adenine dinucleotide (NAD). The enzyme exists as a tetramer of identical chains.

    • Synonyms

      Glyceraldehyde-3-phosphate dehydrogenase, GAPDH, Peptidyl-cysteine S-nitrosylase GAPDH, Gapdh, Gapd, Glyceraldehyde-3-phosphate dehydrogenase isoform 2, G3PD, GAPD, HEL-S-162eP.

    • 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 MGSMVKVGVN GFGRIGRLVT RAAICSGKVE IVAINDPFID LNYMVYMFQY DSTHGKFNGT VKAENGKLVI NGKPITIFQE RDPTNIKWGE AGAEYVVEST GVFTTMEKAG AHLKGGAKRV IISAPSADAP MFVMGVNHEK YDNSLKIVSN ASCTTNCLAP LAKVIHDNFG IVEGLMTTVH AITATQKTVD GPSGKLWRDG RGAAQNIIPA STGAAKAVGK VIPELNGKLT GMAFRVPTPN VSVVDLTCRL EKPAKYDDIK KVVKQASEGP LKGILGYTED QVVSCDFNSN SHSSTFDAGA GIALNDNFVK LISWYDNEYG YSNRVVDLMA YMASKE.

    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.

    Gapdh Mouse Active
  • View Data Sheet

    Name :

    TRPT1 Human

    Description:

    tRNA Phosphotransferase 1 Human Recombinant

    tRNA 2'-phosphotransferase 1, TRPT1.

    Product # :

    ENZ-208

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    Description

    TRPT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-253) and having a molecular mass of 30.3kDa.TRPT1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TRPT1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      tRNA 2'-phosphotransferase 1 (TRPT1) is a member of the KptA/TPT1 family. TRPT1 catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate. TRPT1 is broadly expressed; it is weakly or not expressed in the lung, spleen, small intestine and peripheral blood leukocytes.

    • Synonyms

      tRNA 2'-phosphotransferase 1, TRPT1.

    • 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 MGSHMNFSGG GRQEAAGSRG RRAPRPREQD RDVQLSKALS YALRHGALKL GLPMGADGFV PLGTLLQLPQ FRGFSAEDVQ RVVDTNRKQR FALQLGDPST GLLIRANQGH SLQVPKLELM PLETPQALPP MLVHGTFWKH WPSILLKGLS CQGRTHIHLA PGLPGDPGII SGMRSHCEIA VFIDGPLALA DGIPFFRSAN GVILTPGNTD GFLLPKYFKE ALQLRPTRKP LSLAGDEETE CQSSPKHSSR ERRRIQQ.

    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.

    Trpt1 Human
  • View Data Sheet

    Name :

    GSTM1 Human

    Description:

    Glutathione S-Transferase M1 Human Recombinant

    GST1, GSTM1-1, GSTM1a-1a, GSTM1b-1b, GTH4, GTM1, H-B, MU, MU-1, GST HB subunit 4, GST class-mu 1.

    Product # :

    ENZ-780

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    Description

    GSTM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203 amino acids (1-181 a.a) and having a molecular mass of 23.6kDa.GSTM1 is fused to a 22 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTM1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GSTM1-1, GSTM1a-1a, GSTM1b-1b, GTH4, GTM1, H-B, MU, MU-1, GST HB subunit 4, GST class-mu 1.

    • 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 RSMPMILGYW DIRGLAHAIR LLLEYTDSSY EEKKYTMGDA PDYDRSQWLN EKFKLGLDFP NLPYLIDGAH KITQSNAILC YIARKHNLCG ETEEEKIRVD ILENQTMDNH MQLGMICYNP EFEKLKPKYL EELPEKLKLY SEFLGKRPWF AGNKGLEKIS AYMKSSRFLP RPVFSKMAVW GNK.

    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.

    Gstm1 Human
  • View Data Sheet

    Name :

    PNP Human

    Description:

    Purine Nucleoside Phosphorylase Human Recombinant

    Purine nucleoside phosphorylase, Inosine phosphorylase, NP, PUNP, PRO1837, FLJ94043, FLJ97288, FLJ97312, MGC117396, MGC125915, MGC125916, PNP.

    Product # :

    ENZ-025

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    Description

    PNP 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 309 amino acids (1-289 a.a.) and having a molecular mass of 34.2kDa. The PNP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PNP is a member of the PNP/MTAP phosphorylase family of proteins. PNP catalyzes the reversible phosphorolysis of ribonucleosides and 2’-deoxyribonucleosides with specificity for guanine, hypoxanthine and their analogs. PNP deficiency is a rare autosomal recessive genetic disease linked to a severe defect in T-lymphocyte function and neurologic disorder in children, comprising four percent of combined immunodeficiency cases.

    • Synonyms

      Purine nucleoside phosphorylase, Inosine phosphorylase, NP, PUNP, PRO1837, FLJ94043, FLJ97288, FLJ97312, MGC117396, MGC125915, MGC125916, PNP.

    • 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 MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS.

    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.

    Pnp Human
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