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Search results

1000 results found for “glyoxalase”

Name

Description

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  • View Data Sheet

    Name :

    CA14 Human

    Description:

    Carbonic Anhydrase XIV Human Recombinant

    Carbonic anhydrase 14, Carbonate dehydratase XIV, Carbonic anhydrase XIV, CA-XIV, CA14, CAXiV.

    Product # :

    ENZ-761

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    Description

    CA14 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (16-290 a.a.) and having a molecular mass of 33.2kDa. CA14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA14 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CA14 is a part of the Carbonic anhydrases family. Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They present wide variety in tissue distribution and in their subcellular localization. CA14 is a type I membrane protein which shares highest sequence similarity with the other transmembrane CA isoform, CA XII. Nevertheless, they have different patterns of tissue-specific expression and therefore take different physiologic parts.

    • Synonyms

      Carbonic anhydrase 14, Carbonate dehydratase XIV, Carbonic anhydrase XIV, CA-XIV, CA14, CAXiV.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      NPL Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSADGGQHW TYEGPHGQDH WPASYPECGN NAQSPIDIQT DSVTFDPDLP ALQPHGYDQP GTEPLDLHNN GHTVQLSLPS TLYLGGLPRK YVAAQLHLHW GQKGSPGGSE HQINSEATFA ELHIVHYDSD SYDSLSEAAE RPQGLAVLGI LIEVGETKNI AYEHILSHLH EVRHKDQKTS VPPFNLRELL PKQLGQYFRY NGSLTTPPCY QSVLWTVFYR RSQISMEQLE KLQGTLFSTE EEPSKLLVQN YRALQPLNQR MVFASFIQAG SSYTTGEM.

    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.

    Ca14 Human
  • View Data Sheet

    Name :

    OLA1 Human

    Description:

    Obg-Like ATPase 1 Human Recombinant

    Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.

    Product # :

    ENZ-637

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    Description

    OLA1 Human Recombinant produced in E. coli is a single polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 47.3kDa.OLA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The OLA1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Obg-like ATPase 1 (OLA1) acts as a negative regulator of the cellular antioxidant response independent of transcriptional processes. OLA1 curbs the antioxidant response via nontranscriptional mechanisms. OLA1 hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. OLA1 is clearly down-regulated by DNA damage-inducing agents. OLA1 is expressed in all tissues; however it is more abundant in the testis, liver, lung, and brain. OLA1 is overexpressed in a number of malignancies, including cancers of the colon, rectum, ovary, lung, stomach, and uterus.

    • Synonyms

      Obg-like ATPase 1, DNA damage-regulated overexpressed in cancer 45, DOC45, GTP-binding protein 9, OLA1, GTPBP9, PRO2455, PTD004, GBP45, GTBP9.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMPPKKG GDGIKPPPII GRFGTSLKIG IVGLPNVGKS TFFNVLTNSQ ASAENFPFCT IDPNESRVPV PDERFDFLCQ YHKPASKIPA FLNVVDIAGL VKGAHNGQGL GNAFLSHISA CDGIFHLTRA FEDDDITHVE GSVDPIRDIE IIHEELQLKD EEMIGPIIDK LEKVAVRGGD KKLKPEYDIM CKVKSWVIDQ KKPVRFYHDW NDKEIEVLNK HLFLTSKPMV YLVNLSEKDY IRKKNKWLIK IKEWVDKYDP GALVIPFSGA LELKLQELSA EERQKYLEAN MTQSALPKII KAGFAALQLE YFFTAGPDEV RAWTIRKGTK APQAAGKIHT DFEKGFIMAE VMKYEDFKEE GSENAVKAAG KYRQQGRNYI VEDGDIIFFK FNTPQQPKKK.

    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.

    Ola1 Human
  • View Data Sheet

    Name :

    GSK3B Human, sf9

    Description:

    Glycogen synthase kinase-3 beta, sf9 Human Recombinant

    Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    Product # :

    PKA-084

    Price :

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    Description

    GSK3B produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (1-420a.a.) and having a molecular mass of 47.5kDa. GSK3B is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GSK3B protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4), 0.5mM PMSF and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSK3B is a serine-threonine kinase that belongs to the glycogen synthase kinase subfamily. GSK3B is involved in energy metabolism, neuronal cell development, and body pattern formation. Polymorphisms in the GSK3B gene have been implicated in modifying risk of Parkinson disease, and studies in mice show that overexpression of the GSK3B gene may be significant to the pathogenesis of Alzheimer disease.

    • Synonyms

      Glycogen synthase kinase-3 beta, GSK-3 beta, Serine/threonine-protein kinase GSK3B.

    • 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

      MSGRPRTTSF AESCKPVQQP SAFGSMKVSR DKDGSKVTTV VATPGQGPDR PQEVSYTDTK VIGNGSFGVV YQAKLCDSGE LVAIKKVLQD KRFKNRELQI MRKLDHCNIV RLRYFFYSSG EKKDEVYLNL VLDYVPETVY RVARHYSRAK QTLPVIYVKL YMYQLFRSLA YIHSFGICHR DIKPQNLLLD PDTAVLKLCD FGSAKQLVRG EPNVSYICSR YYRAPELIFG ATDYTSSIDV WSAGCVLAEL LLGQPIFPGD SGVDQLVEII KVLGTPTREQ IREMNPNYTE FKFPQIKAHP WTKVFRPRTP PEAIALCSRL LEYTPTARLT PLEACAHSFF DELRDPNVKL PNGRDTPALF NFTTQELSSN PPLATILIPP HARIQAAAST PTNATAASDA NTGDRGQTNN AASASASNST HHHHHH.

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

    Gsk3B Human Sf9
  • View Data Sheet

    Name :

    ASPH Human

    Description:

    Aspartate Beta-Hydroxylase Human Recombinant

    AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    Product # :

    ENZ-488

    Price :

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    Description

    ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The ASPH protein solution contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.

    • Synonyms

      AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.

    • 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 MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.

    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.

    Asph Human
  • View Data Sheet

    Name :

    QPRT Human

    Description:

    Quinolinate Phosphoribosyltransferase Human Recombinant

    Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.

    Product # :

    ENZ-559

    Price :

    Quantity :

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    Description

    QPRT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 317 amino acids (1-297 a.a.) and having a molecular mass of 32.9 kDa. The QPRT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      QPRT is a key enzyme in the catabolism of quinolinate. QPRT is in between the tryptophannicotinamide adenine dinucleotide (NAD) pathway, resulting in the production of nicotinic acid, carbon dioxide and pyrophosphate. Rise of QPRT levels in the brain is related to the pathogenesis of neurodegenerative disorders such as epilepsy, Alzheimer's disease, and Huntington's disease.

    • Synonyms

      Quinolinate phosphoribosyltransferase , QPRTase, QAPRTase.

    • 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 MDAEGLALLL PPVTLAALVD SWLREDCPGL NYAALVSGAG PSQAALWAKS PGVLAGQPFF DAIFTQLNCQ VSWFLPEGSK LVPVARVAEV RGPAHCLLLG ERVALNTLAR CSGIASAAAA AVEAARGAGW TGHVAGTRKT TPGFRLVEKY GLLVGGAASH RYDLGGLVMV KDNHVVAAGG VEKAVRAARQ AADFALKVEV ECSSLQEAVQ AAEAGADLVL LDNFKPEELH PTATVLKAQF PSVAVEASGG ITLDNLPQFC GPHIDVISMG MLTQAAPALD FSLKLFAKEV APVPKIH.

    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.

    Qprt Human
  • View Data Sheet

    Name :

    CNDP1 Human

    Description:

    CNDP Dipeptidase 1 Human Recombinant

    Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    Product # :

    ENZ-927

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    Description

    CNDP1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 489 amino acids (27-507a.a.) and having a molecular mass of 54.9kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CNDP1 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    CNDP1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CNDP Dipeptidase 1, also known as CNDP1 is a member of the peptidase M20A family. CNDP1 Mannheim which is the shortest allelic form has been more common in the absence of nephropathy in addition to being associated with lower serum carnosinase levels. Furthermore, Carnosine inhibited the increased production of fibronectin as well as collagen type VI in podocytes and the increased production of TGF-beta in mesangial cells. Diabetic patients with the CNDP1 Mannheim variant are less at risk for nephropathy. In addition, on renal cells carnosine protects against the adverse effects of high glucose levels.

    • Synonyms

      Carnosine Dipeptidase 1 (Metallopeptidase M20 Family), Glutamate Carboxypeptidase-Like Protein 2, CNDP Dipeptidase 1, Serum Carnosinase, Carnosinase 1, CPGL2, CN1, Carnosine Dipeptidase 1, EC 3.4.13.20, HsT2308.

    • 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

      SPSPPPALLE KVFQYIDLHQ DEFVQTLKEW VAIESDSVQP VPRFRQELFR MMAVAADTLQ RLGARVASVD MGPQQLPDGQ SLPIPPVILA ELGSDPTKGT VCFYGHLDVQ PADRGDGWLT DPYVLTEVDG KLYGRGATDN KGPVLAWINA VSAFRALEQD LPVNIKFIIE GMEEAGSVAL EELVEKEKDR FFSGVDYIVI SDNLWISQRK PAITYGTRGN SYFMVEVKCR DQDFHSGTFG GILHEPMADL VALLGSLVDS SGHILVPGIY DEVVPLTEEE INTYKAIHLD LEEYRNSSRV
      EKFLFDTKEE ILMHLWRYPS LSIHGIEGAF DEPGTKTVIP GRVIGKFSIR LVPHMNVSAV EKQVTRHLED VFSKRNSSNK MVVSMTLGLH PWIANIDDTQ YLAAKRAIRT VFGTEPDMIR DGSTIPIAKM FQEIVHKSVV LIPLGAVDDG EHSQNEKINR WNYIEGTKLF AAFFLEMAQL HLEHHHHHH.

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    Cndp1 Human
  • View Data Sheet

    Name :

    ADK Human

    Description:

    Adenosine Kinase Human Recombinant

    Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK.

    Product # :

    PKA-367

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    Description

    Adenosine Kinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 362 amino acids (22-362a.a.) and having a molecular mass of 40.5 kDa. Adenosine Kinase protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    ADK protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA, 50mM NaCl & 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

    • Synonyms

      Adenosine 5'-phosphotransferase, EC 2.7.1.20, AK, ADK.

    • 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 MRENILFGMG NPLLDISAVV DKDFLDKYSL KPNDQILAED KHKELFDELV KKFKVEYHAG GSTQNSIKVA QWMIQQPHKA ATFFGCIGID KFGEILKRKA AEAHVDAHYY EQNEQPTGTC AACITGDNRS LIANLAAANC YKKEKHLDLE KNWMLVEKAR VCYIAGFFLT VSPESVLKVA HHASENNRIF TLNLSAPFIS QFYKESLMKV MPYVDILFGN ETEAATFARE QGFETKDIKE IAKKTQALPK MNSKRQRIVI FTQGRDDTIM ATESEVTAFA VLDQDQKEII DTNGAGDAFV GGFLSQLVSD KPLTECIRAG HYAASIIIRR TGCTFPEKPD FH.

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    Adk Human
  • View Data Sheet

    Name :

    Pfu DNA Polymerase

    Description:

    Pfu-DNA Polymerase Recombinant

    DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    Product # :

    ENZ-265

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    Description

    Pfu DNA Polymerase is a thermo-stable enzyme having a Mw of about 90kDa. Pfu DNA Polymerase is derived from E. coli that and cloned from Pyrococcus furiosus strain Vc1 DSM3638. Pfu DNA Polymerase replicates DNA at 75°C, catalyzing the polymerization of nucleotides into duplex DNA in the 5´ to 3´ direction in the existence of magnesium. Pfu DNA Polymerase possesses 3´ to 5´ exonuclease (proofreading) activity. Base misinsertions that take place during polymerization are swiftly removed by the proofreading activity of the polymerase. Therefore, Pfu DNA Polymerase is suggested for use in PCR and primer extension reactions that require high-fidelity synthesis. Pfu DNA Polymerase-generated PCR fragments are blunt-ended.

    Source

    Escherichia Coli.

    Formulation

    50mM Tris-HCl, pH 8.2, 1mM DTT, 0.1mM EDTA, 0.05% CHAPS and 50% glycerol.

    More Info

    • Introduction

      Pfu DNA polymeraseenzyme is found in the hyperthermophilic archaeonPyrococcus furiosus, where it functions in vivoto replicate the organism's DNA. In vitro, Pfu is used to swiftly amplify DNAin the Polymerase Chain Reaction, where the enzyme serves the central function of copying a new strand of DNA during each extension step. Pfu DNA polymerase has superior thermostability and 'proofreading' properties compared to other thermostable polymerases. Unlike Taq DNA polymerase, Pfu DNA polymerase possesses 3' to 5' exonuclease proof reading activity, meaning that it works its way along the DNA from the 5' endto the 3' endand corrects nucleotidemisin corporation errors. Pfu DNA polymerase-generated PCRfragments will have fewer errors than Taq-generated PCR inserts. As a result, Pfu is more commonly used for molecular cloning of PCR fragments than the historically popular Taq. Pfu DNA polymerase is superior for techniques that require high-fidelity DNA synthesis, but can also be used in conjunction with Taq polymerase to obtain the fidelity of Pfu with the speed of Taq polymerase activity.

    • Synonyms

      DNA polymerase, EC 2.7.7.7, Pfu polymerase, Pfu-DNA Polymerase.

    • Physical Appearance

      Sterile liquid formulation.

    • Stability

      Pfu DNA Polymerase although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Applications

      1. Ideal for high-fidelity amplification.
      2. 3'-5' exonuclease activity provides a low error rate.
      3. One of the most thermostable DNA polymerases known.
      4. Lack of extendase activity means no unwanted 3’ overhangs.
      5. Optimal for blunt-end PCR cloning.
      6. Optimum temperature near 75°C.
      7. 95% active after 1-hour incubation at 98°C.

    • PCR Protocol

      Add the following components to amplify 1kb DNA template: 0.2µl Pfu-DNA Polymerase.4µl 2.5mM dNTPs.5µl 10x buffer with MgSO4. 1µl Primers mix (10µM each).1µl Template.38µl ddH2O. Amplify using the following cycling parameters: Heat Soak: 1 cycle at 94°C/4 min.Denaturation: 30 cycles at 94°C/30 sec.Annealing: 30 cycles at 55°C /30 sec.Extension: 30 cycles at 72°C /90 sec. Final: 1 cycle at 72°C /5 min.

    • Unit Definition

      1U of enzyme catalyzes the incorporation of 10nmol of dNTP into acid-insoluble product in 30 minutes at 75°C.

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    Pfu Dna Polymerase
  • View Data Sheet

    Name :

    GZMB Human

    Description:

    Granzyme-B Human Recombinant

    Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.

    Product # :

    ENZ-855

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    Description

    GZMB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (21-247 a.a.) and having a molecular mass of 27.8kDa.GZMB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GZMB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Granzyme-B (GZMB) is essential for target cell lysis in cell-mediated immune responses. GZMB is related to an activation cascade of caspases responsible for apoptosis execution. GZMB cuts caspase-3, -7, -9 and 10 to activate enzymes mediating apoptosis.

    • Synonyms

      Granzyme B, C11, CTLA-1, Cathepsin G-like 1, CTSGL1, Cytotoxic T-lymphocyte proteinase 2, Lymphocyte protease, Fragmentin-2, Granzyme-2, Human lymphocyte protein, HLP, SECT, T-cell serine protease 1-3E, CGL1, CSPB, CTLA1, GRB, GZMB, CCPI, CGL-1, CSP-B.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIIGGHEAKP HSRPYMAYLM IWDQKSLKRC GGFLIQDDFV LTAAHCWGSS INVTLGAHNI KEQEPTQQFI PVKRPIPHPA YNPKNFSNDI MLLQLERKAK RTRAVQPLRL PSNKAQVKPG QTCSVAGWGQ TAPLGKHSHT LQEVKMTVQE DRKCESDLRH YYDSTIELCV GDPEIKKTSF KGDSGGPLVC NKVAQGIVSY GRNNGMPPRA CTKVSSFVHW IKKTMKRY.

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    Gzmb Human
  • View Data Sheet

    Name :

    NPEPPS Human

    Description:

    Aminopeptidase Puromycin Sensitive Human Recombinant

    PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.

    Product # :

    ENZ-1196

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    Description

    NPEPPS Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 925 amino acids (1-919 a.a.) and having a molecular mass of 104kDa. NPEPPS is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    NPEPPS protein solution (0.25mg/ml) containing 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 800 pmol/min/ug and is defined as the amount of enzyme that cleaves 1 pmole of H-Leu[1]AMC per minute at pH7.0 at 37°C.

    More Info

    • Synonyms

      PSA, MP100, AAP-S, Puromycin-sensitive aminopeptidase, Cytosol alanyl aminopeptidase, aminopeptidase puromycin sensitive.

    • 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

      MWLAAAAPSL ARRLLFLGPP PPPLLLLVFS RSSRRRLHSL GLAAMPEKRP FERLPADVSP INYSLCLKPD LLDFTFEGKL EAAAQVRQAT NQIVMNCADI DIITASYAPE GDEEIHATGF NYQNEDEKVT LSFPSTLQTG TGTLKIDFVG ELNDKMKGFY RSKYTTPSGE VRYAAVTQFE ATDARRAFPC WDEPAIKATF DISLVVPKDR VALSNMNVID RKPYPDDENL VEVKFARTPV MSTYLVAFVV GEYDFVETRS KDGVCVRVYT PVGKAEQGKF ALEVAAKTLP FYKDYFNVPY PLPKIDLIAI ADFAAGAMEN GLVTYRETA LLIDPKNSCS SSRQWVALVV GHELAHQWFG NLVTMEWWTH LWLNEGFASW IEYLCVDHCF PEYDIWTQFV SADYTRAQEL DALDNSHPIE VSVGHPSEVD EIFDAISYSK GASVIRMLHD YIGDKDFKKG MNMYLTKFQQ KNAATEDLWE SLENASGKPI AAVMNTWTKQ MGFPLIYVEA EQVEDDRLLR LSQKKFCAGG SYVGEDCPQW MVPITISTSE DPNQAKLKIL MDKPEMNVVL KNVKPDQWVK LNLGTVGFYR TQYSSAMLES LLPGIRDLSL PPVDRLGLQN DLFSLARAGI ISTVEVLKVM EAFVNEPNYT VWSDLSCNLG ILSTLLSHTD FYEEIQEFVK DVFSPIGERL GWDPKPGEGH LDALLRGLVL GKLGKAGHKA TLEEARRRFK DHVEGKQILS ADLRSPVYLT VLKHGDGTTL DIMLKLHKQA DMQEEKNRIE RVLGATLLPD LIQKVLTFAL SEEVRPQDTV SVIGGVAGGS KHGRKAAWKF IKDNWEELYN RYQGGFLISR LIKLSVEGFA VDKMAGEVKA FFESHPAPSA ERTIQQCCEN ILLNAAWLKR DAESIHQYLL QRKASPPTVH HHHHH.

    • Background

      NPEPPS is involved in the proteolytic degradation of misfolded or damaged proteins, contributing to the maintenance of protein homeostasis within the cell. It specifically removes N-terminal amino acids from peptides, thereby regulating their activity and facilitating their further degradation by other proteases.

      This enzyme is particularly important in the nervous system, where it degrades neuropeptides and helps regulate synaptic signaling and neuronal communication.

    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.

    Npepps Human
  • View Data Sheet

    Name :

    PNMT Human

    Description:

    Phenylethanolamine-N-Methyltransferase Human Recombinant

    PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    Product # :

    ENZ-457

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    Description

    Recombinant Human PNMT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 282 amino acids (1-282 a.a.) and having a molecular mass of 30.8 kDa.PNMT is purified by conventional chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PNMT protein solution contains 20mM Tris-HCl, pH-8 & 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PNMT is an enzyme located in the adrenal medulla and it catalyzes the final step of the catecholamine biosynthesis pathway. PNMT has beta-carboline 2N-methyltransferase activity. PNMT takes part in regulating epinephrine production. Glucocorticoid receptors form multimers of PNMT independent of the DNA binding domain. PNMT expression is regulated late in mouse gestation by AP2-alpha and glucocorticoids.

    • Synonyms

      PENT, PNMTase, Noradrenaline-N-methyltransferase, Phenylethanolamine N-methyltransferase, PNMT, MGC34570.

    • 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

      MSGADRSPNA GAAPDSAPGQ AAVASAYQRF EPRAYLRNNY APPRGDLCNP NGVGPWKLRC LAQTFATGEV SGRTLIDIGS GPTVYQLLSA CSHFEDITMT DFLEVNRQEL GRWLQEEPGA FNWSMYSQHA CLIEGKGECW QDKERQLRAR VKRVLPIDVH QPQPLGAGSP APLPADALVS AFCLEAVSPD LASFQRALDH ITTLLRPGGH LLLIGALEES WYLAGEARLT VVPVSEEEVR EALVRSGYKV RDLRTYIMPA HLQTGVDDVK GVFFAWAQKV GL.

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    Pnmt Human
  • View Data Sheet

    Name :

    REXO1 Human

    Description:

    RNA Exonuclease 1 Human Recombinant

    RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.

    Product # :

    ENZ-767

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    Description

    REXO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1060-1221a.a) and having a molecular mass of 22.3kDa. REXO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The REXO1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      REXO1 is an exonuclease domain-containing protein which binds to Elongin. The Elongin complex stimulates the rate of transcription elongation by RNA polymerase II by suppressing the transient pausing of the polymerase at many sites along the DNA template. REXO1 is composed of 1221 amino acids and its mRNA is ubiquitously expressed. REXO1 is a putative stem cell marker and is highly expressed in embryonic and adult stem cells.

    • Synonyms

      RNA exonuclease 1 homolog, Elongin-A-binding protein 1, EloA-BP1, Transcription elongation factor B polypeptide 3-binding protein 1, REXO1, ELOABP1, KIAA1138, TCEB3BP1.

    • 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 KDRWGSIYAL DCEMSYTTYG LELTRVTVVD TDVHVVYDTF VKPDNEIVDY NTRFSGVTEA DLADTSVTLR DVQAVLLSMF SADTILIGHS LESDLLALKV IHSTVVDTSV LFPHRLGLPY KRSLRNLMAD YLRQIIQDNV DGHSSSEDAG ACMHLVIWKV REDAKTKR.

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    Rexo1 Human
  • View Data Sheet

    Name :

    N6AMT1 Human

    Description:

    N-6 Adenine-Specific DNA Methyltransferase 1 Human Recombinant

    N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.

    Product # :

    ENZ-834

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    Description

    N6AMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-214 a.a) and having a molecular mass of 25.3kDa. N6AMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    N6AMT1 protein solution (0.25 mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-6 Adenine-Specific DNA Methyltransferase 1, also known as N6AMT1 is part of the methyltransferase family. N6AMT1 is implicated in the methylation of release factor I during translation termination. In addition, N6AMT1 is involved in converting the arsenic metabolite monomethylarsonous acid to the less toxic dimethylarsonic acid.

    • Synonyms

      N-6 Adenine-Specific DNA Methyltransferase 1 (Putative), N(6)-Adenine-Specific DNA Methyltransferase 1, HemK Methyltransferase Family Member 2, M.HsaHemK2P, C21orf127, HEMK2, Chromosome 21 Open Reading Frame 127, N6-DNA-Methyltransferase, EC 2.1.1.- , PRED28, N6AMT, MTQ2, HemK methyltransferase family member 2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAGENFA TPFHGHVGRG AFSDVYEPAE DTFLLLNALE AAAAELAGVE ICLEVGSGSG VVSAFLASMI GPQALYMCTD INPEAAACTL ETARCNKVHI QPVITDLVKG LLPRLTEKVD LLVFNPPYVV TPPQEVGSHG IEAAWAGGRN GREVMDRFFP LVPDLLSPRG LFYLVTIKEN NPEEILKIMK TKGLQGTTAL SRQAGQETLS VLKFTKS.

    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.

    N6Amt1 Human
  • View Data Sheet

    Name :

    PRDX6 Antibody

    Description:

    Peroxiredoxin-6, Mouse Anti Human

    Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    Product # :

    ANT-581

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    • More Info

    Formulation

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

    More Info

    • Introduction

      Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
      At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

    • Synonyms

      Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PRDX6 mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human PRDX6 amino acids 1-224 purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT22E7AT.

    • Applications

      PRDX6 antibody has been tested by ELISA, Western blot analysis, ICC/IF and Flow cytometry to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • 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

      PRDX6 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.

    Prdx6 Antibody
  • View Data Sheet

    Name :

    LYPLAL1 Human

    Description:

    Lysophospholipase Like I Human Recombinant

    Lysophospholipase-like protein 1, LYPLAL1.

    Product # :

    ENZ-644

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    Description

    LYPLAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.9kDa.LYPLAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLAL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysophospholipase-like protein 1 (LYPLAL1) is a member of the AB hydrolase 2 family. LYPLAL1 doesn’t exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates as a result of its shallow active site.

    • Synonyms

      Lysophospholipase-like protein 1, LYPLAL1.

    • 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 MGSHMAAASG SVLQRCIVSP AGRHSASLIF LHGSGDSGQG LRMWIKQVLN QDLTFQHIKI IYPTAPPRSY TPMKGGISNV WFDRFKITND CPEHLESIDV MCQVLTDLID EEVKSGIKKN RILIGGFSMG GCMAMHLAYR NHQDVAGVFA LSSFLNKASA VYQALQKSNG VLPELFQCHG TADELVLHSW AEETNSMLKS LGVTTKFHSF PNVYHELSKT ELDILKLWIL TKLPGEMEKQ K.

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    Lypla1 Human
  • View Data Sheet

    Name :

    IDH1

    Description:

    Isocitrate Dehydrogenase-1 Yeast Recombinant

    Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    Product # :

    ENZ-289

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    Description

    Recombinant Saccharomyces Cerevisiae ICDH (NADP) derived from yeast host cells by using over-expression system, is full length same as designated ICD1 from Saccharomyces Cerevisiae. The N-terminal amino acid Phenylalanine residue next to Met is substituted with Alanine for overexpression. The ICDH is purified by proprietary chromatographic techniques.

    Source

    Yeast cells.

    Formulation

    One ml of solution contains 0.075 mol/l KPO4, 50% Glycerol, pH 7.1.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 115 U/mg.

    More Info

    • Introduction

      Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

    • Synonyms

      Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    • 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.

    • Unit Definition

      One unit is defined as 1 µmol of NAD+ production per minute under the assay conditions (25°C, pH 7.5).

    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.

    Isocitrate Dehydrogenase
  • View Data Sheet

    Name :

    ldhA E. coli

    Description:

    Fermentative D-lactate Dehydrogenase, NAD-Dependent E.Coli Recombinant

    D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    Product # :

    ENZ-632

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    Description

    ldhA E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1kDa.ldhA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ldhA solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      D-lactate dehydrogenase (ldha) is a member of the D-isomer specific 2-hydroxyacid dehydrogenase family. In enzymology, an ldha (cytochrome) is an enzyme which catalyzes the chemical reaction. Therefore, the 2 substrates of the ldha enzyme are (D)-lactate and ferricytochrome c, whereas its 2 products are pyruvate and ferrocytochrome c.

    • Synonyms

      D-lactate dehydrogenase, D-LDH, Fermentative lactate dehydrogenase, ldhA, hslI, htpH, b1380, JW1375.

    • 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 MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV.

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    Ldha E Coli
  • View Data Sheet

    Name :

    G CSF Human, PEG

    Description:

    Granulocyte-Colony Stimulating Factor Pegylated Human Recombinant

    CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    Product # :

    CYT-018

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    Description

    Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8kDa. The Pegylated G-CSF is produced by attaching a 20kDa methoxypolyethylene glycol propionaldehyde (mPEG-ALD) to the N-terminal amino acid of G-CSF giving a total molecular mass of 38.8kDa. G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    G-CSF is supplied in solution (0.69mg/ml) containing 10mM Acetate Buffer (pH 4.0), and 0.004% Polysorbate 80.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for this gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.

    • Physical Appearance

      Colorless, clear and transparent solution.

    • Stability

      G-CSF PEG should be stored refrigerated at 2° to 8°C. Vials should be kept in theirpackaging to protect from light until the time of use. Shaking and freezing should be avoided.

    • Background

      What is the molecular weight/Mw of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein has a total Mw of 18.8kDa.

      What is the source or expression system of G CSF HUMAN, PEG Protein?
      Escherichia Coli.

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

      What is the Biological Activity of G CSF HUMAN, PEG Protein?
      The ED50, calculated by the dose-dependent proliferation of murine NFS-60 indicator cells is less than 0.1 ng/ml, corresponding to a Specific Activity of 10,000,000IU/mg.

      What is the amino acid sequence of G CSF HUMAN, PEG Protein?
      G CSF HUMAN, PEG Protein is composed from 175 amino acids.

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

      What is the endotoxin level for G CSF HUMAN, PEG Protein?
      The endotoxin level is minimal, G CSF HUMAN, PEG 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.

    G Csf Human Pegylated
  • View Data Sheet

    Name :

    GSTM2 Human

    Description:

    Glutathione S-Transferase MU 2 Human Recombinant

    Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    Product # :

    ENZ-003

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    Description

    GSTM2 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 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 25 units/mg, and is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. 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 structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

    • Synonyms

      Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    • 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 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

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    Gstm2 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.

    More Info

    • 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 :

    KEL Mouse

    Description:

    Kell Metallo-Endopeptidase Mouse Recombinant

    kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    Product # :

    ENZ-1158

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    Description

    KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The KEL 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

      Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.

    • Synonyms

      kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    • 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

      ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.

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    Cd238 Mouse
  • 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.

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    Gstm1 Human
  • View Data Sheet

    Name :

    BCAT1 Human

    Description:

    Branched Chain Amino-Acid Transaminase 1 Human Recombinant

    Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.

    Product # :

    ENZ-597

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    • More Info

    Description

    BCAT1 Recombinant produced in E. coli is a single polypeptide chain containing 409 amino acids (1-386) and having a molecular mass of 45.4kDa.BCAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BCAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      BCAT1 catalyzes the leading reaction in the catabolism of the indispensable branched chain amino acids isoleucine, leucine and valine.

    • Synonyms

      Branched chain amino-acid transaminase 1 cytosolic, BCT1, BCATC, Protein ECA39, placental protein 18, PP18, PNAS121, MECA39, EC 2.6.1.42.

    • 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 MGSMKDCSNG CSAECTGEGG SKEVVGTFKA KDLIVTPATI LKEKPDPNNL VFGTVFTDHM LTVEWSSEFG WEKPHIKPLQ NLSLHPGSSA LHYAVELFEG LKAFRGVDNK IRLFQPNLNM DRMYRSAVRA TLPVFDKEEL LECIQQLVKL DQEWVPYSTS ASLYIRPTFI GTEPSLGVKK PTKALLFVLL SPVGPYFSSG TFNPVSLWAN PKYVRAWKGG TGDCKMGGNY GSSLFAQCEA VDNGCQQVLW LYGEDHQITE VGTMNLFLYW INEDGEEELA TPPLDGIILP GVTRRCILDL AHQWGEFKVS ERYLTMDDLT TALEGNRVRE MFGSGTACVV CPVSDILYKG ETIHIPTMEN GPKLASRILS KLTDIQYGRE ESDWTIVLS.

    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.

    Bcat1 Human
  • View Data Sheet

    Name :

    GSTP1 Human

    Description:

    Glutathione S-Transferase pi 1 Human Recombinant

    Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.

    Product # :

    ENZ-427

    Price :

    Quantity :

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    More Info

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

    Description

    GSTP1 Human Recombinant fused with 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (1-210 a.a.) And having a molecular mass of 27.4kDa. The GSTP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTP1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH7.0), 30% glycerol, 1mM EDTA and 0.1mM PMSF.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 80 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

    More Info

    • Introduction

      GSTP1 is a polymorphic gene encoding active, functionally different GSTP1 variant proteins that are believed to function in xenobiotic metabolism and have a part in susceptibility to cancer, and other diseases. GSTP1 is a glutathione S-transferase belonging to the pi class. GST family enzymes play a significant role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. Based upon the biochemical, immunologic and structural properties of the soluble GSTs they are grouped into 4 main classes: alpha, mu, pi, and theta. The GSTP1 enzyme acts by catalyzing the reaction of glutathione with an acceptor molecule to form a Sulfur-substituted glutathione. The reactions employing glutathione contribute the transformation of a broad range of electrophiles, including reactive products of lipid, protein, carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress.
      The GSTP1 inactivation through CpG hypermethylation is frequent in pituitary adenomas and may be a factor in aggressive pituitary tumor behavior. GSTP1 is may be a transcriptional target of the p53 tumor suppressor gene. Single-nucleotide polymorphism in GSTP1 is linked to modified protein binding, which influence GSTP1's contribution to carcinogen and drug metabolism, and possibly disease pathogenesis and/or drug response. GST-pi might have central roles in proliferation of androgen-independent human prostate cancer cells.

    • Synonyms

      Glutathione S-transferase P, GST class-pi, GSTP1-1, GSTP1, FAEES3, GST3, PI, DFN7.

    • 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 KDRWGSMPPY TVVYFPVRGR CAALRMLLAD QGQSWKEEVV TVETWQEGSL KASCLYGQLP KFQDGDLTLY QSNTILRHLG RTLGLYGKDQ QEAALVDMVN DGVEDLRCKY ISLIYTNYEA GKDDYVKALP GQLKPFETLL SQNQGGKTFI VGDQISFADY NLLDLLLIHE VLAPGCLDAF PLLSAYVGRL SARPKLKAFL ASPEYVNLPI NGNGKQ.

    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.

    Gstp1 Human
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