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Search results

1000 results found for “glyoxalase”

Name

Description

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  • View Data Sheet

    Name :

    KARS Human

    Description:

    Lysyl-tRNA Synthetase Human Recombinant

    Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.

    Product # :

    ENZ-161

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    Description

    KARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 558 amino acids (63-597 a.a.) and having a molecular mass of 63.7kDa.KARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysyl-tRNA synthetase (KARS) is a member of the class-II aminoacyl-tRNA synthetase family. KARS exists as both mitochondrial and cytoplasmic isoforms produced by alternative splicing, and believed to have a role in autoimmune diseases, such as polymyositis or dermatomyositis. The KARS protein functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids, so linking amino acids with tRNA-contained nucleotide triplets.

    • Synonyms

      Lysine--tRNA ligase, Lysyl-tRNA synthetase, LysRS, KARS, KIAA0070, KRS, KARS2, CMTRIB.

    • 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 MGSGVGPEEE SVDPNQYYKI RSQAIHQLKV NGEDPYPHKF HVDISLTDFI QKYSHLQPGD HLTDITLKVA GRIHAKRASG GKLIFYDLRG EGVKLQVMAN SRNYKSEEEF IHINNKLRRG DIIGVQGNPG KTKKGELSII PYEITLLSPC LHMLPHLHFG LKDKETRYRQ RYLDLILNDF VRQKFIIRSK IITYIRSFLD ELGFLEIETP MMNIIPGGAV AKPFITYHNE LDMNLYMRIA PELYHKMLVV GGIDRVYEIG RQFRNEGIDL THNPEFTTCE FYMAYADYHD LMEITEKMVS GMVKHITGSY KVTYHPDGPE GQAYDVDFTP PFRRINMVEE LEKALGMKLP ETNLFETEET RKILDDICVA KAVECPPPRT TARLLDKLVG EFLEVTCINP TFICDHPQIM SPLAKWHRSK EGLTERFELF VMKKEICNAY TELNDPMRQR QLFEEQAKAK AAGDDEAMFI DENFCTALEY GLPPTAGWGM GIDRVAMFLT DSNNIKEVLL FPAMKPEDKK ENVATTDTLE STTVGTSV.

    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.

    Kars Human
  • View Data Sheet

    Name :

    PPA Yeast

    Description:

    Inorganic Pyrophosphatase Yeast Recombinant

    Inorganic pyrophosphatase, PPA.

    Product # :

    ENZ-1181

    Price :

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    Description

    PPA Yeast Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 35kDa. Inorganic Pyrophosphatase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Inorganic pyrophosphatase protein solution (100U/ml) containing 20mM Tris-HCl (25℃, pH 8.0), 100mM KCl, 0.1mM EDTA, 1mM DTT and 50% glycerol.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

    • Synonyms

      Inorganic pyrophosphatase, PPA.

    • 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. Do not store at -70C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.

    • Unit Definition

      Under standard conditions, 1U is defined as the amount of enzyme required to catalyze the hydrolysis of pyrophosphate (PPi)/min. to produce 1μmol of orthophosphate (Pi). Optimal reaction temp. is 25℃ , activity at 16 ~ 37℃. Cofactor: Mg+2

    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.

    Ppa Yeast
  • View Data Sheet

    Name :

    GNMT Human, Active

    Description:

    Glycine N-Methyltransferase Human Recombinant , Active

    Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    Product # :

    ENZ-1059

    Price :

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    Description

    GNMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-295 a.a) and having a molecular mass of 34.9kDa.GNMT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 nmol/min/mg, and is defined as the amount of enzyme that transfer 1.0 nmole of methyl group per minute at 37C.

    More Info

    • Introduction

      GNMT is an enzyme that catalyzes the conversion of S-adenosyl-L-methionine with glycine to S-adenosyl-L-homocysteine and sarcosine. GNMT is located in the cytoplasm and acts as a homotetramer. Defects in the GNMT gene causes of GNMT deficiency (hypermethioninemia). GNMT affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine and is involved in the detoxification pathway in liver cells. GNMT expression is diminished in human hepatocellular carcinoma (HCC). GNMT catalyzes the methylation of glycine by using s- adenosylmethionine (adomet) to form n-methylglycine (sarcosine) with the concomitant production of s-adenosylhomocysteine (adohcy). GNMT plays an essential role in the regulation of tissue concentration of adomet and of metabolism of methionine.

    • Synonyms

      Glycine N-methyltransferase, GNMT, Glycine N-Methyltransferase, EC 2.1.1.20
      Epididymis Secretory Sperm Binding Protein Li 182mP, HEL-S-182mP.

    • 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 MVDSVYRTRS LGVAAEGLPD QYADGEAARV WQLYIGDTRS RTAEYKAWLL GLLRQHGCQR VLDVACGTGV DSIMLVEEGF SVTSVDASDK MLKYALKERW NRRHEPAFDK WVIEEANWMT LDKDVPQSAE GGFDAVICLG NSFAHLPDCK GDQSEHRLAL KNIASMVRAG GLLVIDHRNY DHILSTGCAP PGKNIYYKSD LTKDVTTSVL IVNNKAHMVT LDYTVQVPGA GQDGSPGLSK FRLSYYPHCL ASFTELLQAA FGGKCQHSVL GDFKPYKPGQ TYIPCYFIHV LKRTD.

    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.

    Gnmt Human Active
  • View Data Sheet

    Name :

    CMBL Human

    Description:

    Carboxymethylenebutenolidase Human Recombinant

    Carboxymethylenebutenolidase homolog, CMBL, JS-1.

    Product # :

    ENZ-634

    Price :

    Quantity :

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    Description

    CMBL Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-245) and having a molecular mass of 30.6kDa.CMBL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CMBL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carboxymethylenebutenolidase homolog (CMBL) is a cysteine hydrolase of the dienelactone hydrolase family which is highly expressed in the liver cytosol. CMBL is the human homolog of Pseudomonas dienelactone hydrolase, which is a protein that participates in the bacterial halocatechol degradation pathway. CMBL which preferentially cleaves cyclic esters activates medoxomil-ester prodrugs in which the medoxomil moiety is coupled with an oxygen atom. CMBL is inhibited by PCMB (p-chloromercuribenzoate) and is encoded by a gene which maps to human chromosome 5p15.2. CMBL can also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. CMBL is widely expressed, with the highest levels in the liver, followed by the kidney, small intestine and the colon.

    • Synonyms

      Carboxymethylenebutenolidase homolog, CMBL, JS-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMANEAY PCPCDIGHRL EYGGLGREVQ VEHIKAYVTK SPVDAGKAVI VIQDIFGWQL PNTRYIADMI SGNGYTTIVP DFFVGQEPWD PSGDWSIFPE WLKTRNAQKI DREISAILKY LKQQCHAQKI GIVGFCWGGT AVHHLMMKYS EFRAGVSVYG IVKDSEDIYN LKNPTLFIFA ENDVVIPLKD VSLLTQKLKE HCKVEYQIKT FSGQTHGFVH RKREDCSPAD KPYIDEARRN LIEWLNKYM.

    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.

    Cmbl Human
  • View Data Sheet

    Name :

    GLU-C S.aureus

    Description:

    Glutamyl endopeptidase Staphylococcal Recombinant

    Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    Product # :

    ENZ-955

    Price :

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    Description

    Recombinant Staphylococcal GLU-C produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 267 amino acids and having a molecular mass of 28.9kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 10mM sodium phosphate, pH 7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

    • Synonyms

      Glutamyl endopeptidase (EC:3.4.21.19), Endoproteinase Glu-C, Staphylococcal serine proteinase, V8 protease, V8 proteinase, sspA.

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized GLU-C although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLU-C should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      MLPNNDRHQI TDTTNGHYAP VTYIQVEAPT GTFIASGVVV GKDTLLTNKH VVDATHGDPH ALKAFPSAIN QDNYPNGGFT AEQITKYSGE GDLAIVKFSP NEQNKHIGEV VKPATMSNNA ETQVNQNITV TGYPGDKPVA TMWESKGKIT YLKGEAMQYD LSTTGGNSGS PVFNEKNEVI GIHWGGVPNE FNGAVFINEN VRNFLKQNIE DIHFANDDQP NNPDNPDNPN NPDNPNNPDE PNNPDNPNNP DNPDNGDNNN SDNPDAA.

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    Glu C Saureus
  • View Data Sheet

    Name :

    GALM Human

    Description:

    Galactose Mutarotase Human Recombinant

    Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    Product # :

    ENZ-541

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    Description

    GALM Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-342 a.a.) and having a molecular mass of 39.9 kDa. The GALM is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALM is a main enzyme of carbohydrate metabolism catalysing the translation of beta-D-galactose to alpha-D-galactose. GALM is needed for normal galactose metabolism by preserveing the equilibrium of alpha and beta anomers of galactose. GALM is required for the production of complex oligosaccharides.

    • Synonyms

      Aldose 1-epimerase, BLOCK25, IBD1, EC=5.1.3.3, GALM, galactose mutarotase.

    • 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 MASVTRAVFG ELPSGGGTVE KFQLQSDLLR VDIISWGCTI TALEVKDRQG RASDVVLGFA ELEGYLQKQP YFGAVIGRVA NRIAKGTFKV DGKEYHLAIN KEPNSLHGGV RGFDKVLWTP RVLSNGVQFS RISPDGEEGY PGELKVWVTY TLDGGELIVN YRAQASQATP VNLTNHSYFN LAGQASPNIN DHEVTIEADT YLPVDETLIP TGEVAPVQGT AFDLRKPVEL GKHLQDFHLN GFDHNFCLKG SKEKHFCARV HHAASGRVLE VYTTQPGVQF YTGNFLDGTL KGKNGAVYPK HSGFCLETQN WPDAVNQPRF PPVLLRPGEE YDHTTWFKFS VA.

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    Galm Human
  • View Data Sheet

    Name :

    PNPO Human

    Description:

    Pyridoxamine 5'-Phosphate Oxidase Human Recombinant

    Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.

    Product # :

    ENZ-030

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    Description

    PNPO Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (57-261 a.a.) and having a molecular mass of 25.9kDa. The PNPO is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pyridoxine-5'-phosphate oxidase (PNPO) is the rate-limiting enzyme in vitamin B6 synthesis. Vitamin B6 (Pyridoxal 5-prime-phosphate or PLP) is vital for normal cellular function, and some cancer cells have notable differences in vitamin B6 metabolism compared to their normal counterparts.Vitamin B6 is an essential co-factor for enzymes involved in both homocysteine metabolism and synthesis of neurotransmitters such as catecholamine. Mutations in the PNPO gene result in PNPO deficiency, a form of neonatal epileptic encephalopathy.

    • Synonyms

      Pyridoxine-5'-phosphate oxidase, Pyridoxamine-phosphate oxidase, PNPO, PDXPO, FLJ10535.

    • 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 MDPVKQFAAW FEEAVQCPDI GEANAMCLAT CTRDGKPSAR MLLLKGFGKD GFRFFTNFES RKGKELDSNP FASLVFYWEP LNRQVRVEGP VKKLPEEEAE CYFHSRPKSS QIGAVVSHQS SVIPDREYLR KKNEELEQLY QDQEVPKPKS WGGYVLYPQV MEFWQGQTNR LHDRIVFRRG LPTGDSPLGP MTHRGEEDWL YERLAP.

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    Pnpo Human
  • View Data Sheet

    Name :

    PPA E.Coli

    Description:

    Inorganic Pyrophosphatase E.Coli Recombinant

    Inorganic pyrophosphatase, Pyrophosphate phospho-hydrolase, PPase, ppa, b4226, JW4185.

    Product # :

    ENZ-149

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    Description

    PPA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 196 amino acids (1-176 a.a.) and having a molecular mass of 21.9kDa.PPA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PPA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Inorganic pyrophosphatase (ppa) is a member of the Ppase family. PPA is an enzyme which catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Since this is a highly exergonic reaction, it can therefore be coupled to unfavorable biochemical transformations in order to drive these transformations to completion. The role of the PPA enzyme is a critical one in the lipid metabolism (including lipid synthesis and degradation), calcium absorption and bone formation, DNA synthesis, as well as other biochemical transformations.

    • Synonyms

      Inorganic pyrophosphatase, Pyrophosphate phospho-hydrolase, PPase, ppa, b4226, JW4185.

    • 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 MSLLNVPAGK DLPEDIYVVI EIPANADPIK YEIDKESGAL FVDRFMSTAM FYPCNYGYIN HTLSLDGDPV DVLVPTPYPL QPGSVIRCRP VGVLKMTDEA GEDAKLVAVP HSKLSKEYDH IKDVNDLPEL LKAQIAHFFE HYKDLEKGKW VKVEGWENAE AAKAEIVASF ERAKNK.

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    Ppa Ecoli
  • View Data Sheet

    Name :

    GSR Human

    Description:

    Glutathione Reductase Human Recombinant

    Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.

    Product # :

    ENZ-202

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    Description

    GSR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 504 amino acids (43-522) and having a molecular mass of 54.3kDa.GSR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSR 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.

    Biological Activity

    Specific activity: > 29 unit/ml.
    One unit will reduce 1.0 umol of oxidized glutathione per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      Glutathione reductase (GSR) belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. The GSR enzyme is a homodimeric flavoprotein and has a role in maintaining glutathione (GSH) in its reduced form by catalyzing the reduction of glutathione disulfide (GSSG): GSSG + NADPH + H+ ->2GSH + NADP+. In the majority of eukaryotic cells, GSR upholds the ratio of [GSH] / [GSSG], and partakes in quite a few critical functions such as the detoxification of reactive oxygen species as well as protein and DNA biosynthesis.

    • Synonyms

      Glutathione reductase mitochondrial, GR, GRase, GSR, GLUR, GRD1.

    • 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 MGSMAMACRQ EPQPQGPPPA AGAVASYDYL VIGGGSGGLA SARRAAELGA RAAVVESHKL GGTCVNVGCV PKKVMWNTAV HSEFMHDHAD YGFPSCEGKF NWRVIKEKRD AYVSRLNAIY QNNLTKSHIE IIRGHAAFTS DPKPTIEVSG KKYTAPHILI
      ATGGMPSTPH ESQIPGASLG ITSDGFFQLE ELPGRSVIVG AGYIAVEMAG ILSALGSKTS LMIRHDKVLR SFDSMISTNC TEELENAGVE VLKFSQVKEV KKTLSGLEVS MVTAVPGRLP VMTMIPDVDC LLWAIGRVPN TKDLSLNKLG IQTDDKGHII VDEFQNTNVK GIYAVGDVCG
      KALLTPVAIA AGRKLAHRLF EYKEDSKLDY NNIPTVVFSH PPIGTVGLTE DEAIHKYGIE NVKTYSTSFT PMYHAVTKRK TKCVMKMVCA NKEEKVVGIH MQGLGCDEML QGFAVAVKMG ATKADFDNTV AIHPTSSEEL VTLR.

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    Gsr Human
  • View Data Sheet

    Name :

    ACADVL Human

    Description:

    Acyl-CoA Dehydrogenase, Very Long Chain Human Recombinant

    ACAD6, LCACD, VLCAD.

    Product # :

    ENZ-250

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    Description

    ACADVL Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing 636 amino acids (41-655 a.a.) and having a molecular mass of 68.5 kda. ACADVL contains 21 amino acid His-Tag at the N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The 0.5mg/ml protein solution contains 20mM Tris-HCl buffer pH-8, 1mM DTT, 1mM EDTA, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACADVL is an inner mitochondrial membrane enzyme that is part of the family of acyl-CoA dehydrogenases. ACADVL protein participates in lipid metabolism and has catalytic activity toward esters of long chain and very long chain fatty acids such as palmitoyl-CoA and stearoyl-CoA, and is involved in the first step of the fatty acid β-oxidation pathway. ACADVL deficiency in reduces myocardial fatty acid beta-oxidation and is related with cardiomyopathy.

    • Synonyms

      ACAD6, LCACD, VLCAD.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store ACADVL 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 MAGGAAQLAL DKSDSHPSDA LTRKKPAKAE SKSFAVGMFK GQLTTDQVFP YPSVLNEEQT QFLKELVEPV SRFFEEVNDP AKNDALEMVE ETTWQGLKEL GAFGLQVPSE LGGVGLCNTQ YARLVEIVGM HDLGVGITLG AHQSIGFKGI LLFGTKAQKE KYLPKLASGE TVAAFCLTEP SSGSDAASIR TSAVPSPCGK YYTLNGSKLW ISNGGLADIF TVFAKTPVTD PATGAVKEKI TAFVVERGFG GITHGPPEKK MGIKASNTAE VFFDGVRVPS ENVLGEVGSG FKVAMHILNN GRFGMAAALA GTMRGIIAKA VDHATNRTQF GEKIHNFGLI QEKLARMVML QYVTESMAYM VSANMDQGAT DFQIEAAISK IFGSEAAWKV TDECIQIMGG MGFMKEPGVE RVLRDLRIFR IFEGTNDILR LFVALQGCMD KGKELSGLGS ALKNPFGNAG LLLGEAGKQL RRRAGLGSGL SLSGLVHPEL SRSGELAVRA LEQFATVVEA KLIKHKKGIV NEQFLLQRLA DGAIDLYAMV VVLSRASRSL SEGHPTAQHE KMLCDTWCIE AAARIREGMA ALQSDPWQQE LYRNFKSISK ALVERGGVVT SNPLGF.

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    Acadvl Human
  • View Data Sheet

    Name :

    ST3GAL5 Human

    Description:

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    Product # :

    ENZ-755

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    Description

    ST3GAL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (83-418a.a) and having a molecular mass of 41kDa. ST3GAL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ST3GAL5 protein solution (1mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    • 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 MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF

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    St3Gal5 Human
  • View Data Sheet

    Name :

    Benzonase Nuclease, 90%

    Description:

    Benzonase Nuclease Serratia Marcescens Recombinant, 90%

    Product # :

    ENZ-1150

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    Description

    Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds. Benzonase Nuclease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Benzonase Nuclease solution contains 50% glycerol, 50 mM Tris-HCl pH 8.0, 20 mM NaCl and 2 mM MgCl2.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.

    • 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.

    • Specificity

      Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product: 5’-mono-phosphate terminated oligonucleotides (3-5 bases). Protease Activity: Not detectable

    • Unit Definition

      1U Benzonase Nuclease is defined as the amount of enzyme that causes a ΔA260 of 1 in 30 min, which corresponds to complete digestion of 37μg DNA. Standard reaction conditions are 1mg/ml sonicated DNA substrate in 50mM Tris-HCl pH 8.0, 0.1mg/ml BSA, 1mM MgCl2, incubated at 37°C.

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    Benzonase Nuclease Enzyme
  • View Data Sheet

    Name :

    UPP1 E.coli

    Description:

    Uridine Phosphorylase E.coli Recombinant

    UPASE, UDRPASE, UPP, UDP.

    Product # :

    ENZ-258

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    Description

    UPP1 E.Coli Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPP1 solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

    • Synonyms

      UPASE, UDRPASE, UPP, UDP.

    • 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 MSKSDVFHLG LTKNDLQGAT LAIVPGDPDR VEKIAALMDK PVKLASHREF TTWRAELDGK PVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS LHFAPLEFPA VADFECTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRHF KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH AVKIVVEAAR RLL.

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    Upp1
  • View Data Sheet

    Name :

    DLST Human

    Description:

    Dihydrolipoamide S-Succinyltransferase Human Recombinant

    dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    Product # :

    ENZ-083

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    Description

    DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.

    Source

    Sf9 insect cells.

    Formulation

    DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.

    Purity

    DLST purity was found to be greater than 75% as determined by SDS-PAGE.

    More Info

    • Introduction

      DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).

    • Synonyms

      dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.

    • Stability

      Store DLST 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.

    • Immunological Functions

      1. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
      anti-hexa-His-tag antibody.

    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.

    Dlst Human
  • View Data Sheet

    Name :

    FAAH2 Human

    Description:

    Fatty Acid Amide Hydrolase 2 Human Recombinant

    Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

    Product # :

    ENZ-777

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    Description

    FAAH2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 524 amino acids (32-532a.a) and having a molecular mass of 57.4kDa. FAAH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FAAH2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fatty Acid Amide Hydrolase 2 (FAAH2) shares a conserved protein motif with the amidase signature family of enzymes. FAAH2 catalyzes the hydrolysis of a broad range of bioactive lipids, including those from the 3 main classes of fatty acid amides; N-acylethanolamines, fatty acid primary amides and N-acyl amino acids. FAAH2 is also degrades bioactive fatty acid amides to their corresponding acids, thus helping to end the signaling functions of these molecules. FAAH2 prefers monounsaturated acyl chains as a substrate.

    • Synonyms

      Fatty acid amide hydrolase 2, AMDD, Amidase domain-containing protein, Anandamide amidohydrolase 2, Oleamide hydrolase 2, FAAH2.

    • 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 MGSGGPKFAS KTPRPVTEPL LLLSGMQLAK LIRQRKVKCI DVVQAYINRI KDVNPMINGI VKYRFEEAMK EAHAVDQKLA EKQEDEATLE NKWPFLGVPL TVKEAFQLQG MPNSSGLMNR RDAIAKTDAT VVALLKGAGA IPLGITNCSE LCMWYESSNK IYGRSNNPYD LQHIVGGSSG GEGCTLAAAC SVIGVGSDIG GSIRMPAFFN GIFGHKPSPG VVPNKGQFPL AVGAQELFLC TGPMCRYAED LAPMLKVMAG PGIKRLKLDT KVHLKDLKFY WMEHDGGSFL MSKVDQDLIM TQKKVVVHLE TILGASVQHV KLKKMKYSFQ LWIAMMSAKG HDGKEPVKFV DLLGDHGKHV SPLWELIKWC LGLSVYTIPS IGLALLEEKL RYSNEKYQKF KAVEESLRKE LVDMLGDDGV FLYPSHPTVA PKHHVPLTRP FNFAYTGVFS ALGLPVTQCP LGLNAKGLPL GIQVVAGPFN DHLTLAVAQY LEKTFGGWVC PGKF.

    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.

    Faah2 Human
  • View Data Sheet

    Name :

    GOT1 Mouse

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

    Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.

    Product # :

    ENZ-872

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    Description

    GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.

    • Synonyms

      Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.

    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.

    Got1 Mouse
  • View Data Sheet

    Name :

    Ketohexokinase Human

    Description:

    Ketohexokinase Human Recombinant

    KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.

    Product # :

    PKA-359

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    Description

    Ketohexokinase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 298 amino acids and having a molecular mass of 32.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 1xPBS, pH 7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ketohexokinase catalyzes the phosphorylation of fructose to produce fructose-1-phosphate, resulting in the utilization of ATP and creation of AMP. Ketohexokinase commences initial step in the metabolism of dietary fructose and is a significant regulator of hepatic glucose metabolism. Ketohexokinase is found in liver, renal cortex, and small intestine. Its deficiency causes the benign hereditary metabolic disorder essential fructosuria, leading to fructose being excreted in the urine. Ketohexokinase-dependent metabolism of fructose induces proinflammatory mediators in proximal tubular cells. ketohexokinase plays an unknown physiologic function that remains intact in essential fructosuria. Ketohexokinase expression is reduceed in human clear cell type of renal cell carcinoma.

    • Synonyms

      KHK, Hepatic Fructokinase, Ketohexokinase, Fructokinase.

    • 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

      MEEKQILCVG LVVLDVISLV DKYPKEDSEI RCLSQRWQRG GNASNSCTIL SLLGAPCAFM GSMAPGHVAD FVLDDLRRYS VDLRYTVFQT TGSVPIATVI INEASGSRTI LYYDRSLPDV SATDFEKVDL TQFKWIHIEG RNASEQVKML QRIDAHNTRQ PPEQKIRVSV EVEKPREELF QLFGYGDVVF VSKDVAKHLG FQSAEEALRG LYGRVRKGAV LVCAWAEEGA DALGPDGKLL HSDAFPPPRV VDTLGAGDTF NASVIFSLSQ GRSVQEALRF GCQVAGKKCG LQGFDGIV.

    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.

    Ketohexokinase Human
  • View Data Sheet

    Name :

    GPT Human, His Active

    Description:

    Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-1000

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    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • 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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

    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.

    Gpt Human His Active
  • View Data Sheet

    Name :

    ABO Human

    Description:

    ABO Blood Group Human Recombinant

    Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.

    Product # :

    ENZ-167

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    Description

    ABO Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (54-354 a.a) and having a molecular mass of 37.4kDa.ABO is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ABO protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAGAT (ABO) is a member of the glycosyltransferase 6 family. The ABO protein is the basis of the ABO blood group system and related to the first discovered blood group system, ABO. The allele that is present in an individual determines the blood group. The histo-blood group ABO is comprised of 3 carbohydrate antigens: A, B, and H. A, B, and AB individuals express a glycosyltransferase activity which converts the H antigen to the A antigen (by addition of UDP-GalNAc) or to the B antigen (by addition of UDP-Gal), whereas O individuals are deficient of such activity.

    • Synonyms

      Histo-blood group ABO system transferase, Fucosylglycoprotein 3-alpha-galactosyltransferase, Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase, Glycoprotein-fucosylgalactoside alpha-galactosyltransferase, Histo-blood group A transferase, A transferase, Histo-blood group B transferase, B transferase, NAGAT, ABO, GTB, A3GALNT, A3GALT1.

    • 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 MAVREPDHLQ RVSLPRMVYP QPKVLTPCRK DVLVVTPWLA PIVWEGTFNI DILNEQFRLQ NTTIGLTVFA IKKYVAFLKL FLETAEKHFM VGHRVHYYVF TDQPAAVPRV TLGTGRQLSV LEVRAYKRWQ DVSMRRMEMI SDFCERRFLS EVDYLVCVDV DMEFRDHVGV EILTPLFGTL HPGFYGSSRE AFTYERRPQS QAYIPKDEGD FYYLGGFFGG SVQEVQRLTR ACHQAMMVDQ ANGIEAVWHD ESHLNKYLLR HKPTKVLSPE YLWDQQLLGW PAVLRKLRFT AVPKNHQAVR NP.

    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.

    Abo Human
  • View Data Sheet

    Name :

    DERA Human

    Description:

    Deoxyribose-Phosphate Aldolase Human Recombinant

    Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.

    Product # :

    ENZ-170

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    Description

    DERA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 338 amino acids (1-318) and having a molecular mass of 37.3 kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DERA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.

    • Synonyms

      Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.

    • 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 MSAHNRGTEL DLSWISKIQV NHPAVLRRAE QIQARRTVKK EWQAAWLLKA VTFIDLTTLS GDDTSSNIQR LCYKAKYPIR EDLLKALNMH DKGITTAAVC VYPARVCDAV KALKAAGCNI PVASVAAGFP AGQTHLKTRL EEIRLAVEDG ATEIDVVINR SLVLTGQWEA LYDEIRQFRK ACGEAHLKTI LATGELGTLT NVYKASMIAM MAGSDFIKTS TGKETVNATF PVAIVMLRAI RDFFWKTGNK IGFKPAGGIR SAKDSLAWLS LVKEELGDEW LKPELFRIGA STLLSDIERQ IYHHVTGRYA AYHDLPMS

    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.

    Dera Human
  • View Data Sheet

    Name :

    FBP2 Human

    Description:

    Fructose-1,6-Bisphosphatase 2 Human Recombinant

    Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.

    Product # :

    ENZ-667

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    Description

    FBP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 362 amino acids (1-339) and having a molecular mass of 39kDa. FBP2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The FBP2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fructose-1,6-bisphosphatase isozyme 2 (FBP2) is a part of the FBPase class 1 family. FBP2 is a gluconeogenesis regulatory enzyme Which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.

    • Synonyms

      Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.

    • 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 MGSMTDRSPF ETDMLTLTRY VMEKGRQAKG TGELTQLLNS MLTAIKAISS AVRKAGLAHL YGIAGSVNVT GDEVKKLDVL SNSLVINMVQ SSYSTCVLVS EENKDAIITA KEKRGKYVVC FDPLDGSSNI DCLASIGTIF AIYRKTSEDE PSEKDALQCG RNIVAAGYAL YGSATLVALS TGQGVDLFML DPALGEFVLV EKDVKIKKKG KIYSLNEGYA KYFDAATTEY VQKKKFPEDG SAPYGARYVG SMVADVHRTL VYGGIFLYPA NQKSPKGKLR LLYECNPVAY IIEQAGGLAT TGTQPVLDVK PEAIHQRVPL ILGSPEDVQE YLTCVQKNQA GS.

    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.

    Fbp2 Human
  • View Data Sheet

    Name :

    PGM2 Human

    Description:

    Phosphoglucomutase 2 Human Recombinant

    Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.

    Product # :

    ENZ-930

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    Description

    PGM2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 635 amino acids (1-612 a.a) and having a molecular mass of 70.7kDa. PGM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PGM2 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PGM2 or Phosphoglucomutase-2 is a protein of the alpha-d-phosphohexomutase family that shares about 20% similarity with mammalian phosphoglucomutase 1. PGM2 Has low glucose 1,6-bisphosphate synthase activity. Furthermore, PGM2 catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. In addition, PGM2 catalyzes the interconversion of glucose-1-phosphate and glucose-6-phosphate.

    • Synonyms

      Phosphoglucomutase 2, Glucose Phosphomutase 2, Phosphodeoxyribomutase, Phosphopentomutase, EC 5.4.2.2, PGM 2, Phosphoglucomutase-2, EC 5.4.2.7, EC 5.4.2, MSTP006.

    • 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 MGSMAAPEGS GLGEDARLDQ ETAQWLRWDK NSLTLEAVKR LIAEGNKEEL RKCFGARMEF GTAGLRAAMG PGISRMNDLT IIQTTQGFCR YLEKQFSDLK QKGIVISFDA RAHPSSGGSS RRFARLAATT FISQGIPVYL FSDITPTPFV PFTVSHLKLC AGIMITASHN PKQDNGYKVY WDNGAQIISP HDKGISQAIE ENLEPWPQAW DDSLIDSSPL LHNPSASINN DYFEDLKKYC FHRSVNRETK VKFVHTSVHG VGHSFVQSAF KAFDLVPPEA VPEQKDPDPE FPTVKYPNPE EGKGVLTLSF ALADKTKARI VLANDPDADR LAVAEKQDSG EWRVFSGNEL GALLGWWLFT SWKEKNQDRS ALKDTYMLSS TVSSKILRAI ALKEGFHFEE TLTGFKWMGN RAKQLIDQGK TVLFAFEEAI GYMCCPFVLD KDGVSAAVIS AELASFLATK NLSLSQQLKA IYVEYGYHIT KASYFICHDQ ETIKKLFENL RNYDGKNNYP KACGKFEISA IRDLTTGYDD SQPDKKAVLP TSKSSQMITF TFANGGVATM RTSGTEPKIK YYAELCAPPG NSDPEQLKKE LNELVSAIEE HFFQPQKYNL QPKAD.

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    Pgm2 Human
  • View Data Sheet

    Name :

    Gly m 4.0101

    Description:

    Stress-Induced Protein SAM22 Recombinant

    Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    Product # :

    PRO-2278

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    Description

    Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

    • Synonyms

      Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

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    Gly M 40101
  • View Data Sheet

    Name :

    NANS Human

    Description:

    N-acetylneuraminic acid synthase Human Recombinant

    Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    Product # :

    ENZ-024

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    • More Info

    Description

    NANS 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 379 amino acids (1-359 a.a.) and having a molecular mass of 42.4kDa. The NANS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NANS is a 359 amino acid protein that contains one AFP (antifreeze proteins)-like domain and functions in the biosynthesis of sialic acids. The ubiquitously expressed NANS enzymatically catalyzes the H2O-dependent formation of N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN), both of which are sialic acids. NANS uses N-acetylmannosamine 6-phosphate as a substrate for Neu5Ac synthesis and mannose 6-phosphate as a substrate for KDN synthesis.

    • Synonyms

      Sialic acid synthase, N-acetylneuraminate synthase, N-acetylneuraminate-9-phosphate synthase, N-acetylneuraminic acid phosphate synthase, N-acetylneuraminic acid synthase, NANS, SAS.

    • 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 MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS.

    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.

    Nans Human
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