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Search results

1000 results found for “Glyoxalase”

Name

Description

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  • View Data Sheet

    Name :

    AKR1D1 Human

    Description:

    Aldo-Keto Reductase Family 1 Member D1 Human Recombinant

    3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.

    Product # :

    ENZ-931

    Price :

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    Description

    AKR1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 326 amino acids (1-326 a.a.) and having a molecular mass of 37.3kDa. The AKR1D1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1D1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.

    • Synonyms

      3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.

    • 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

      MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.

    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.

    Human Akr1D1
  • View Data Sheet

    Name :

    LYPLA2 Human

    Description:

    Lysophospholipase II Human Recombinant

    Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    Product # :

    ENZ-076

    Price :

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    Description

    LYPLA2 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 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLA2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.

    • Synonyms

      Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    • 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 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V.

    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.

    Lypla2 Human
  • View Data Sheet

    Name :

    Carbonic Anhydrase II E.coli

    Description:

    Carbonic Anhydrase II E.coli Recombinant

    Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    Product # :

    ENZ-373

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    Description

    Carbonic anhydrase II is an E.coli Recombinant protein produced in E.Coli containing 240 amino acids (1-220) and having a molecular mass of 27 kDa. Carbonic anhydrase is expressedwith an amino-terminal hexahistidine tag.The Carbonic anhydrase 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Carbonic Anhydrase 2 enzyme is supplied in 20mM Tris pH-8 and 1mM DTT.

    Purity

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

    More Info

    • Introduction

      The enzyme Carbonic anhydrase II having an accession number of NP_414668 is also called carbonate dehydratase which is part of the enzyme family that catalyses rapid inter-conversion of carbon dioxide & water to bicarbonate, carbonic acid and protons (CO2 + H2O ? HCO3? + H+), a reaction that occurs rather slowly in the absence of a catalyst. The majority of carbonic anhydrases enclose a zinc ion in their active site and therefore is classified as metalloenzymes.
      The most important function of Carbonic anhydrase is known to preserve acid-base balance in blood and other tissues, and to help transport carbon dioxide of tissues. Carbonic anhydrases have been found in all kingdoms of life. Carbonic anhydrase has 3 different classes: alpha, beta and gamma which share very little sequence or structural similarity, thus far they all perform the same function and require a zinc ion at the active site. Mammalian carbonic anhydrase is monomeric and belongs to the alpha class. Plant carbonic anhydrase is dimeric and belongs to the beta class.
      Methane-producing bacteria carbonic anhydrase is trimeric and grows in hot springs which forms the gamma class.

    • Synonyms

      Carbonic anhydrase 2, Carbonate dehydratase 2, can, cynT2, yadF, b0126, JW0122, Carbonic Anhydrase II.

    • 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 MKDIDTLISN NALWSKMLVE EDPGFFEKLAQAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL HIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

    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.

    Carbonic Anhydrase Ii
  • View Data Sheet

    Name :

    FARS2 Human

    Description:

    Phenylalanyl-tRNA Synthetase 2 Human Recombinant

    Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    Product # :

    ENZ-111

    Price :

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    Description

    FARS2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (37-451 a.a.) and having a molecular mass of 50.6kDa.FARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FARS2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol, 1mM EDTA and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phenylalanyl-tRNA synthetase 2 mitochondrial (FARS2) is a member of the class II aminoacyl- tRNA synthetase family. FARS2 is a mitochondrial matrix protein. FARS2 when acting as a monomer, catalyzes the ATP-dependent conversion of L-phenylalanine and tRNA (Phe) to L-phenlalanyltRNA (Phe), an event which is vital for proper translation and protein expression.

    • Synonyms

      Phenylalanyl-tRNA synthetase mitochondrial, Phenylalanine--tRNA ligase, PheRS, FARS2, FARS1, HSPC320, dJ520B18.2.

    • 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 MPAAECATQR APGSVVELLG KSYPQDDHSN LTRKVLTRVG RNLHNQQHHP LWLIKERVKE HFYKQYVGRF GTPLFSVYDN LSPVVTTWQN FDSLLIPADH PSRKKGDNYY LNRTHMLRAH TSAHQWDLLH AGLDAFLVVG DVYRRDQIDS QHYPIFHQLE AVRLFSKHEL FAGIKDGESL QLFEQSSRSA HKQETHTMEA VKLVEFDLKQ TLTRLMAHLF GDELEIRWVD CYFPFTHPSF EMEINFHGEW LEVLGCGVME QQLVNSAGAQ DRIGWAFGLG LERLAMILYD IPDIRLFWCE DERFLKQFCV SNINQKVKFQ PLSKYPAVIN DISFWLPSEN YAENDFYDLV RTIGGDLVEK VDLIDKFVHP KTHKTSHCYR ITYRHMERTL SQREVRHIHQ ALQEAAVQLL GVEGRF.

    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.

    Fars2 Human
  • View Data Sheet

    Name :

    PRDX4 Human

    Description:

    Peroxiredoxin-4 Human Recombinant

    EC 1.11.1.15, AOE37-2, Peroxiredoxin-IV, Prx-IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Antioxidant enzyme AOE372.

    Product # :

    ENZ-513

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    Description

    PRDX4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 255 amino acids (38-271 a.a.) and having a molecular mass of 28.8kDa. PRDX4 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PRDX4 Human solution containing 20mM Tris-HCl pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: approximately 230-310 pmole/min/µg.
    Enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX4 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25 C for 1 minute.

    More Info

    • Introduction

      PRDX4 is an antioxidant enzyme that is part of the peroxiredoxin family. PRDX4 is localized to the cytoplasm. PRDX4 reduces hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. PRDX4 has a regulatory part in the activation of the transcription factor NF-kappaB. PRDX4 participates in redox regulation of the cell. PRDX4 regulates the activation of NF-kappa-B in the cytosol by a modulation of I-kappa-B-alpha phosphorylation.

    • Synonyms

      EC 1.11.1.15, AOE37-2, Peroxiredoxin-IV, Prx-IV, Thioredoxin peroxidase AO372, Thioredoxin-dependent peroxide reductase A0372, Antioxidant enzyme AOE372.

    • 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 MWETEERPRT REEECHFYAG GQVYPGEASR VSVADHSLHL SKAKISKPAP YWEGTAVIDG EFKELKLTDY RGKYLVFFFY PLDFTFVCPT EIIAFGDRLE EFRSINTEVV ACSVDSQFTH LAWINTPRRQ GGLGPIRIPL LSDLTHQISK DYGVYLEDSG HTLRGLFIID DKGILRQITL NDLPVGRSVD ETLRLVQAFQ YTDKHGEVCP AGWKPGSETI IPDPAGKLKY FDKLN.

    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.

    Prdx4 Human
  • View Data Sheet

    Name :

    ALDH1A1 Human

    Description:

    Aldehyde Dehydrogenase 1A1 Human Recombinant

    ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    Product # :

    ENZ-453

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    Description

    The ALDH1A1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 54.8kDa and containing 501 amino acids (1-501 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ALDH1A1 protein solution is formulated in 50mM Tris-HCl pH-7.5 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ALDH1A1 is part of the aldehyde dehydrogenases family.
      Aldehyde dehydrogenase is the 2nd protein of the main oxidative pathway of alcohol metabolism. Cytosolic and mitochondrial are 2 main liver isoforms of ALDH that are differentiateed by their electrophoretic mobility, kinetic property, & subcellular localization. The majority of Caucasians have two main isozymes, whereas just about 50% of Orientals have only the cytosolic form, excluding the mitochondrial form. ALDH1A1 is also a member of the group of corneal crystallins that assist the transparency of the cornea.
      (Retinal + NAD+ + H2O = retinoate + NADH).

    • Synonyms

      ALDC, Aldehyde dehydrogenase cytosolic, Aldehyde dehydrogenase family 1 member A1, ALDH1, ALDH11, ALDH-E1, ALHDII, MGC2318, PUMB1, RalDH1, RALDH1, RALDH 1, Retinal dehydrogenase 1, ALDH1A1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLYKLADLIERDR LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN FFTYTRHEPI GVCGQIIPWN FPLVMLIWKIGPALSCGNTV VVKPAEQTPL TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN S.

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

    Aldh1A1 Human
  • View Data Sheet

    Name :

    DDT Human

    Description:

    D-Dopachrome Tautomerase Human Recombinant

    EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.

    Product # :

    ENZ-527

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    Description

    DDT Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-118 a.a.) and having a molecular mass of 14.8 kDa. The DDT is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

    • Synonyms

      EC 4.1.1.84, DDCT, D-dopachtome decarboxylase, D-Dopachrome Tautomerase.

    • 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 MPFLELDTNL PANRVPAGLE KRLCAAAASI LGKPADRVNV TVRPGLAMAL SGSTEPCAQL SISSIGVVGT AEDNRSHSAH FFEFLTKELA LGQDRILIRF FPLESWQIGK IGTVMTFL.

    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.

    Ddt Human
  • View Data Sheet

    Name :

    ACKA E.Coli

    Description:

    Acetate Kinase E.Coli Recombinant

    Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    Product # :

    PKA-063

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    Description

    Recombinant ACKA produced in E.coli is a single, non-glycosylated polypeptide chain containing 423 amino acids (1-400) and having a molecular mass of 45.7 kDa.The ACKA is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E.Coli Acetate Kinase, also knowns as ACKA, catalyzes the formation of acetyl phosphate from acetate and ATP and also catalyzes the reverse reaction. ACKA takes part in synthesis of various ATP formed catabolically during anaerobic growth of the organism.

    • Synonyms

      Acetate kinase, Acetokinase, ackA, ack, ACKA, Acetate kinase A and propionate kinase 2.

    • 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 MGSMSSKLVL VLNCGSSSLK FAIIDAVNGE EYLSGLAECF HLPEARIKWK MDGNKQEAAL GAGAAHSEAL NFIVNTILAQ KPELSAQLTA IGHRIVHGGE KYTSSVVIDE SVIQGIKDAA SFAPLHNPAH LIGIEEALKS FPQLKDKNVA VFDTAFHQTM PEESYLYALP YNLYKEHGIR RYGAHGTSHF YVTQEAAKML NKPVEELNII TCHLGNGGSV SAIRNGKCVD TSMGLTPLEG LVMGTRSGDI DPAIIFHLHD TLGMSVDAIN KLLTKESGLL GLTEVTSDCR YVEDNYATKE DAKRAMDVYC HRLAKYIGAY TALMDGRLDA VVFTGGIGEN AAMVRELSLG KLGVLGFEVD HERNLAARFG KSGFINKEGT RPAVVIPTNE ELVIAQDASR LTA.

    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.

    Acka Ecoli
  • View Data Sheet

    Name :

    CA1 E.Coli

    Description:

    Carbonic Anhydrase-1 E.Coli Recombinant

    Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.

    Product # :

    ENZ-1138

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    Description

    CA1 E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-220) and having a molecular mass of 27.0 kDa. CA1 E.Coli is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CA1 E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CA, also known as carbonic anhydrase is an enzyme that functions around the involvement of CO2 + H2O to HCO3- + H+ (conversion of CO2 to bicarbonate & protons). This enzyme holds a Zn ion as part of its active site. The central function of CA is to preserve the acid-base homeostasis within the blood and various organs. carbonic anhydrase assists Carbonic Anhydrase I to move CO2 to and from tissues.

    • Synonyms

      Carbonate dehydratase, CAN, ECK0125, JW0122, yadF, CA 1, CA I, CA1, CAI, Car 1, Car1, Carbonate dehydratase I, Carbonic anhydrase 1, Carbonic anhydrase B.

    • 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 MKDIDTLISN NALWSKMLVE EDPGFFEKLA QAQKPRFLWI GCSDSRVPAE RLTGLEPGEL FVHRNVANLV IHTDLNCLSV VQYAVDVLEV EHIIICGHYG CGGVQAAVEN PELGLINNWL LHIRDIWFKH SSLLGEMPQE RRLDTLCELN VMEQVYNLGH STIMQSAWKR GQKVTIHGWA YGIHDGLLRD LDVTATNRET LEQRYRHGIS NLKLKHANHK.

    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.

    Ca1 Protein
  • View Data Sheet

    Name :

    HMBS Human

    Description:

    Hydroxymethylbilane Synthase Human Recombinant

    Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    Product # :

    ENZ-581

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    Description

    HMBS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 385 amino acids (1-361) and having a molecular mass of 41.9kDa.HMBS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Porphobilinogen deaminase (HMBS) belongs to the hydroxymethylbilane synthase superfamily. HMBS is a cytoplasmic enzyme found in the heme synthesis pathway. HMBS is the 3rd enzyme of the heme biosynthetic pathway and catalyzes the head to tail condensation of 4 porphobilinogen molecules into the linear hydroxymethylbilane. HMBS gene mutations cause errors in pyrrole metabolism which in turn lead to the autosomal dominant disease acute intermittent porphyria.

    • Synonyms

      Porphobilinogen deaminase, PBG-D, Hydroxymethylbilane synthase, HMBS, Pre-uroporphyrinogen synthase, HMBS, PBGD, UPS, PORC.

    • 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 MGSHMSGNGN AAATAEENSP KMRVIRVGTR KSQLARIQTD SVVATLKASY PGLQFEIIAM STTGDKILDT ALSKIGEKSL FTKELEHALE KNEVDLVVHS LKDLPTVLPP GFTIGAICKR ENPHDAVVFH PKFVGKTLET LPEKSVVGTS SLRRAAQLQR
      KFPHLEFRSI RGNLNTRLRK LDEQQEFSAI ILATAGLQRM GWHNRVGQIL HPEECMYAVG QGALGVEVRA KDQDILDLVG VLHDPETLLR CIAERAFLRH LEGGCSVPVA VHTAMKDGQL YLTGGVWSLD GSDSIQETMQ ATIHVPAQHE DGPEDDPQLV GITARNIPRG PQLAAQNLGI
      SLANLLLSKG AKNILDVARQ LNDAH.

    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.

    Hmbs Human
  • View Data Sheet

    Name :

    CS Human

    Description:

    Citrate Synthase Human Recombinant

    Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    Product # :

    ENZ-824

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    Description

    CS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (28-466 a.a) and having a molecular mass of 51.4kDa. CS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Citrate synthase also known as CS is a Krebs tricarboxylic acid cycle enzyme which catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. CS is present in almost all cells capable of oxidative metabolism. CS is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. The diseases related to CS are: critical illness polyneuropathy and mitochondrial cardiomyopathy.

    • Synonyms

      Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    • 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 MGSASSTNLK DILADLIPKE QARIKTFRQQ HGKTVVGQIT VDMMYGGMRG MKGLVYETSV LDPDEGIRFR GFSIPECQKL LPKAKGGEEP LPEGLFWLLV TGHIPTEEQV SWLSKEWAKR AALPSHVVTM LDNFPTNLHP MSQLSAAVTA LNSESNFARA YAQGISRTKY WELIYEDSMD LIAKLPCVAA KIYRNLYREG SGIGAIDSNL DWSHNFTNML GYTDHQFTEL TRLYLTIHSD HEGGNVSAHT SHLVGSALSD PYLSFAAAMN GLAGPLHGLA NQEVLVWLTQ LQKEVGKDVS DEKLRDYIWN TLNSGRVVPG YGHAVLRKTD PRYTCQREFA LKHLPNDPMF KLVAQLYKIV PNVLLEQGKA KNPWPNVDAH SGVLLQYYGM TEMNYYTVLF GVSRALGVLA QLIWSRALGF PLERPKSMST EGLMKFVDSK SG.

    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.

    Cs 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.

    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.

    Dhrs9 Human
  • View Data Sheet

    Name :

    YWHAG Human, His

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant, His Tag

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-262

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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 246 amino acids (2-247) and having a molecular mass of 36 kDa. YWHAG is fused to His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 1x PBS and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • 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. Avoid multiple freeze-thaw cycles.

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

    Ywhag Human His
  • View Data Sheet

    Name :

    PMM1 Human

    Description:

    Phosphomannomutase 1 Human Recombinant

    Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    Product # :

    ENZ-023

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    Description

    PMM1 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 282 amino acids (1-262 a.a.) and having a molecular mass of 31.9kDa. The PMM1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PMM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.

    • Synonyms

      Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.

    • 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 MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC REIFFPETAH EA.

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    Pmm1 Human
  • View Data Sheet

    Name :

    RPIA Human

    Description:

    Ribose 5-Phosphate Isomerase A Human Recombinant

    Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.

    Product # :

    ENZ-228

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    Description

    RPIA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-311) and having a molecular mass of 35.4kDa.RPIA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPIA solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT,40% glycerol, 200mM NaCl, 2mM EDTA and 0.2mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribose-5-phosphate isomerase (RPIA) is a member of the ribose 5-phosphate isomerase family. RPIA is an enzyme which catalyzes the conversion between ribose-5-phosphate (R5P) and ribulose-5-phosphate (Ru5P). RPI occurs as 2 separate proteins forms, termed RPIA and RPIB. RPIA has a vital role in the metabolism of plants and animals, as it is involved in the Calvin cycle which takes place in plants, and the pentose phosphate pathway which occurs in plants as well as animals.

    • Synonyms

      Ribose-5-phosphate isomerase, Phosphoriboisomerase, RPIA, RPI.

    • 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 MQRPGPFSTL YGRVLAPLPG RAGGAASGGG GNSWDLPGSH VRLPGRAQSG TRGGAGNTST SCGDSNSICP APSTMSKAEE AKKLAGRAAV ENHVRNNQVL GIGSGSTIVH AVQRIAERVK QENLNLVCIP TSFQARQLIL QYGLTLSDLD RHPEIDLAID GADEVDADLN LIKGGGGCLT QEKIVAGYAS RFIVIADFRK DSKNLGDQWH KGIPIEVIPM AYVPVSRAVS QKFGGVVELR MAVNKAGPVV TDNGNFILDW KFDRVHKWSE VNTAIKMIPG VVDTGLFINM AERVYFGMQD GSVNMREKPF C.

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    Rpia Human
  • View Data Sheet

    Name :

    NT5C2 Human

    Description:

    5'-Nucleotidase Cytosolic II Human Recombinant

    Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    Product # :

    ENZ-173

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    Description

    NT5C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 581 amino acids (1-561 a.a.) and having a molecular mass of 67.1kDa.NT5C2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NT5C2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NT5C2 (NT5B/PNT5) has a vital role in the maintenance of purine/pyrimidine nucleotides. NT5C2 contains a phosphotransferase active site which catalyzes the dephosphorylation of 6-hydroxypurine nucleoside 5'-monophosphates. Furthermore, NT5C2 regulates the level of inosine monophosphate (IMP) and guanosine monophosphate (GMP) pools inside cells by way of hydrolysis.

    • Synonyms

      Cytosolic purine 5'-nucleotidase, Cytosolic 5'-nucleotidase II, NT5C2, NT5B, NT5CP, PNT5, GMP, cN-II.

    • 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 MSTSWSDRLQ NAADMPANMD KHALKKYRRE AYHRVFVNRS LAMEKIKCFG FDMDYTLAVY KSPEYESLGF ELTVERLVSI GYPQELLSFA YDSTFPTRGL VFDTLYGNLL KVDAYGNLLV CAHGFNFIRG PETREQYPNK FIQRDDTERF YILNTLFNLP ETYLLACLVD FFTNCPRYTS CETGFKDGDL FMSYRSMFQD VRDAVDWVHY KGSLKEKTVE NLEKYVVKDG KLPLLLSRMK EVGKVFLATN SDYKYTDKIM TYLFDFPHGP KPGSSHRPWQ SYFDLILVDA RKPLFFGEGT VLRQVDTKTG KLKIGTYTGP LQHGIVYSGG SSDTICDLLG AKGKDILYIG DHIFGDILKS KKRQGWRTFL VIPELAQELH VWTDKSSLFE ELQSLDIFLA ELYKHLDSSS NERPDISSIQ RRIKKVTHDM DMCYGMMGSL FRSGSRQTLF ASQVMRYADL YAASFINLLY YPFSYLFRAA HVLMPHESTV EHTHVDINEM ESPLATRNRT SVDFKDTDYK RHQLTRSISE IKPPNLFPLA PQEITHCHDE DDDEEEEEEE E.

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    Nt5C2 Human
  • View Data Sheet

    Name :

    GLRX5 Human

    Description:

    Glutaredoxin 5 Human Recombinant

    Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.

    Product # :

    ENZ-480

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    Description

    GLRX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-157 a.a.) and having a molecular mass of 18.8 kDa. GRX5 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLRX5 solution containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 0.1M NaCl.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLRX5 is small redox enzyme of approximately 100 amino acids which uses glutathione as a cofactor. GLRX5 is a mitochondrial protein, which is evolutionarily conserved. GLRX5 is oxidized by substrates, and reduced non-enzymatically by glutathione. GLRX5 is involved in the biogenesis of iron-sulfur clusters that are required for normal iron homeostasis. GLRX5 is necessary for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. Defects in the GLRX5 gene are a cause of anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA).

    • Synonyms

      Glutaredoxin-related protein 5 mitochondrial, Monothiol glutaredoxin-5, GLRX5, C14orf87, glutaredoxin 5, GRX5, FLB4739, PR01238, PRO1238, MGC14129.

    • 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 MSGSLGRAAA ALLRWGRGAG GGGLWGPGVR AAGSGAGGGG SAEQLDALVK KDKVVVFLKG TPEQPQCGFS NAVVQILRLH GVRDYAAYNV LDDPELRQGI KDYSNWPTIP QVYLNGEFVG GCDILLQMHQ NGDLVEELKK LGIHSALLDE KKDQDSK.

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    Glrx5 Human
  • View Data Sheet

    Name :

    GZMH Human

    Description:

    Granzyme-H Human Recombinant

    Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), CTSGL2, Cytotoxic T-Lymphocyte Proteinase, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Cathepsin G-Like 2, EC 3.4.21.79, EC 3.4.21, Granzyme H, EC 3.4.21, CGL-2, CTLA1, CGL2, GZMH.

    Product # :

    ENZ-896

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    Description

    GZMH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 248 amino acids (20-246 a.a) and having a molecular mass of 27.5kDa.GZMH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GZMH protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.

    • Synonyms

      Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), CTSGL2, Cytotoxic T-Lymphocyte Proteinase, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Cathepsin G-Like 2, EC 3.4.21.79, EC 3.4.21, Granzyme H, EC 3.4.21, CGL-2, CTLA1, CGL2, GZMH.

    • 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 MEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRL

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    Gzmh Human
  • View Data Sheet

    Name :

    RNASE2 Human

    Description:

    Ribonuclease 2 Human Recombinant

    EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.

    Product # :

    ENZ-1175

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    Description

    RNASE2 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 143 amino acids (28-161 a.a.) and having a molecular mass of 16.5kDa.RNASE2 is fused to a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    RNASE2 Human protein (1mg/ml) is formulated in 20% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RNASE2, also known as EDN, is best-known as one of the 4 major proteins found in the large specific granules of human eosinophilic leukocytes. This protein is also expressed constitutively in human liver tissue and its expression can be induced in macrophages by proinflammatory stimuli. RNASE2 is a non-secretory ribonuclease which belongs to the pancreatic ribonuclease family, a subset of the ribonuclease A superfamily. Diseases associated with EDN include Dermatitis, Atopic, 8 and Pulmonary Eosinophilia.

    • Synonyms

      EDN, RNS2, ribonuclease A family member 2, RAF3, non-secretory ribonuclease, Eosinophil-derived neurotoxin, RNase UpI-2, Ribonuclease 2, RNase 2, Ribonuclease US.

    • 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

      ADPKPPQFTW AQWFETQHIN MTSQQCTNAM QVINNYQRRC KNQNTFLLTT FANVVNVCGN PNMTCPSNKT RKNCHHSGSQ VPLIHCNLTT PSPQNISNCR YAQTPANMFY IVACDNRDQR RDPPQYPVVP VHLDRIIHHH HHH

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    Rnase2 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 :

    CTSZ Human, Sf9

    Description:

    Cathepsin-Z Human Recombinant, Sf9

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1097

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • 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

      GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
      HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
      AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
      AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
      GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH

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    Cathepsin Z Protein
  • View Data Sheet

    Name :

    LYPLA1 Mouse

    Description:

    Lysophospholipase I Mouse Recombinant

    Acyl-protein thioesterase 1, LYPLA1, APT-1, LPL1, LYSOPLA.

    Product # :

    ENZ-565

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    Description

    LYPLA1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-230a.a.) and having a molecular mass of 26.8kDa.LYPLA1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLA1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)0.1M NaCl,1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      LYPLA1 is lysophospholipase which performs on biological membranes to regulate the multifunctional lysophospholipids. LYPLA1 protein hydrolyzes fatty acids from S-acylated cysteine residues in proteins like trimeric G alpha proteins or HRAS and in addition has depalmitoylating activity.

    • Synonyms

      Acyl-protein thioesterase 1, LYPLA1, APT-1, LPL1, LYSOPLA.

    • 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 MCGNNMSAPM PAVVPAARKA TAAVIFLHGL GDTGHGWAEA FAGIKSPHIK YICPHAPVMP VTLNMNMAMP SWFDIVGLSP DSQEDESGIK QAAETVKALI DQEVKNGIPS NRIILGGFSQ GGALSLYTAL TTQQKLAGVT ALSCWLPLRA SFSQGPINSA NRDISVLQCH GDCDPLVPLM FGSLTVERLK ALINPANVTF KIYEGMMHSS CQQEMMDVKH FIDKLLPPID.

    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.

    Lypla1 Mouse
  • View Data Sheet

    Name :

    CPA4 Human

    Description:

    Carboxypeptidase A4 Human Recombinant

    Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.

    Product # :

    ENZ-942

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    Description

    CPA4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 413 amino acids (17-421a.a.) and having a molecular mass of 46.6kDa.CPA4 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CPA4 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carboxypeptidase A4 (CPA4) belongs to the carboxypeptidase A/B subfamily, and it is located in a cluster with 3 other family members on chromosome 7. CPA4 is a secreted, zinc-dependent metallocarboxypeptidase, which removes the C-terminal amino acid from peptides having a free C-terminal carboxyl group. CPA4 is a metalloprotease which may be involved in the histone hyperacetylation pathway. CPA4 are synthesized as zymogens which are activated by proteolytic cleavage.

    • Synonyms

      Carboxypeptidase A4, Carboxypeptidase A3, CPA3, EC 3.4.17.1, EC 3.4.17.-, EC 3.4.17, Carboxypeptidase A4, Carboxypeptidase A3.

    • 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

      GQEKFFGDQV LRINVRNGDE ISKLSQLVNS NNLKLNFWKS PSSFNRPVDV LVPSVSLQAF KSFLRSQGLE YAVTIEDLQA LLDNEDDEMQ HNEGQERSSN NFNYGAYHSL EAIYHEMDNI AADFPDLARR VKIGHSFENR PMYVLKFSTG KGVRRPAVWL NAGIHSREWI SQATAIWTAR KIVSDYQRDP AITSILEKMD IFLLPVANPD GYVYTQTQNR LWRKTRSRNP GSSCIGADPN RNWNASFAGK GASDNPCSEV YHGPHANSEV EVKSVVDFIQ KHGNFKGFID LHSYSQLLMY PYGYSVKKAP DAEELDKVAR LAAKALASVS GTEYQVGPTC TTVYPASGSS IDWAYDNGIK FAFTFELRDT GTYGFLLPAN QIIPTAEETW LGLKTIMEHV RDNLYLEHHH HHH.

    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.

    Cpa4 Human
  • View Data Sheet

    Name :

    GZMK Human, Sf9

    Description:

    Granzyme-K, Human Recombinant, sf9

    GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.

    Product # :

    ENZ-1031

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    GZMK Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 247 amino acids (27-264) and having a molecular mass of 26.9kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMK is fused to a 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GZMK protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      GZMK is a part of a group of related serine proteases from the cytoplasmic granules of cytotoxic lymphocytes. Cytolytic T lymphocytes and natural killer cells have the outstanding ability to bind, recognize and lyse specific target cells. They defend their host by lysing cells bearing on their surface 'nonself' antigens, usually peptides or proteins resulting from infection by intracellular pathogens.

    • Synonyms

      GZMK, TRYP2, Granzyme-K, Granzyme K, Fragmentin-3, Granzyme-3, NK-tryptase-2, NK-Tryp-2.

    • 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

      ADPIIGGKEV SPHSRPFMAS IQYGGHHVCG GVLIDPQWVL TAAHCQYRFT KGQSPTVVLG AHSLSKNEAS KQTLEIKKFI PFSRVTSDPQ SNDIMLVKLQ TAAKLNKHVK MLHIRSKTSL RSGTKCKVTG WGATDPDSLR PSDTLREVTV TVLSRKLCNS QSYYNGDPFI TKDMVCAGDA KGQKDSCKGD SGGPLICKGV FHAIVSGGHE CGVATKPGIY TLLTKKYQTW IKSNLVPPHT NHHHHHH.

    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.

    Gzmk Sf9
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