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Search results

1000 results found for “Enolase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    Luciferase Firefly

    Description:

    Luciferin 4-Monooxygenase Firefly Recombinant

    Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    Product # :

    ENZ-553

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    Description

    Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-550 a.a.) and having a molecular mass of 62.9kDa.Luciferase is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Luciferase protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

    • Synonyms

      Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    • 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 MMEDAKNIKK GPAPFYPLED GTAGEQLHKA MKRYALVPGT IAFTDAHIEV DITYAEYFEM SVRLAEAMKR YGLNTNHRIV VCSENSLQFF MPVLGALFIG VAVAPANDIY NERELLNSMG ISQPTVVFVS KKGLQKILNV QKKLPIIQKI IIMDSKTDYQ GFQSMYTFVT SHLPPGFNEY DFVPESFDRD KTIALIMNSS GSTGLPKGVA LPHRTACVRF SHARDPIFGN QIIPDTAILS VVPFHHGFGM FTTLGYLICG FRVVLMYRFE EELFLRSLQD YKIQSALLVP TLFSFFAKST LIDKYDLSNL HEIASGGAPL SKEVGEAVAK RFHLPGIRQG YGLTETTSAI LITPEGDDKP GAVGKVVPFF EAKVVDLDTG KTLGVNQRGE LCVRGPMIMS GYVNNPEATN ALIDKDGWLH SGDIAYWDED EHFFIVDRLK SLIKYKGYQV APAELESILL QHPNIFDAGV AGLPDDDAGE LPAAVVVLEH GKTMTEKEIV DYVASQVTTA KKLRGGVVFV DEVPKGLTGK LDARKIREIL IKAKKGGKIA 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.

    Luciferase Firefly
  • View Data Sheet

    Name :

    Luciferase Firefly, Active

    Description:

    Luciferin 4-Monooxygenase Firefly Recombinant, Active

    Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    Product # :

    ENZ-1035

    Price :

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    Description

    Luciferase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 335 amino acids (1-311 a.a) and having a molecular mass of 38.5kDa. Luciferase is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >1x109 light units/mg. One luciferase enzyme units will produce one Relative Light Unit (RLU) at pH7.5 at 25°C. 

    More Info

    • Introduction

      Luciferase is a general term for the class of oxidative enzymes used in bioluminescence and is distinct from a photoprotein. Luciferase catalyzes a bioluminescent reaction which involves the substrate luciferin as well as Mg2+ and ATP, produces green light with a wavelength of 562 nm. Luciferase from firefly is broadly used as a reporter for studying gene regulation and function, and for pharmaceutical screening.

    • Synonyms

      Luciferase-like monooxygenase, LUC, EC 1.13.12.7.

    • 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 MGSHMTSKVY DPEQRKRMIT GPQWWARCKQ MNVLDSFINY YDSEKHAENA VIFLHGNAAS SYLWRHVVPH IEPVARCIIP DLIGMGKSGK SGNGSYRLLD HYKYLTAWFE LLNLPKKIIF VGHDWGACLA FHYSYEHQDK IKAIVHAESV VDVIESWDEW PDIEEDIALI KSEEGEKMVL ENNFFVETML PSKIMRKLEP EEFAAYLEPF KEKGEVRRPT LSWPREIPLV KGGKPDVVQI VRNYNAYLRA SDDLPKMFIE SDPGFFSNAI VEGAKKFPNT EFVKVKGLHF SQEDAPDEMG KYIKSFVERV LKNEQ.

    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.

    Luciferase Firefly Active
  • View Data Sheet

    Name :

    ADAL Human

    Description:

    Adenosine Deaminase-Like Human Recombinant

    Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.

    Product # :

    ENZ-788

    Price :

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    Description

    ADAL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-267) and having a molecular mass of 32.7kDa.ADAL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADAL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.

    • Synonyms

      Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.

    • 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 MGSEFMIEAE EQQPCKTDFY SELPKVELHA HLNGSISSHT MKKLIAQKPD LKIHDQMTVI DKGKKRTLEE CFQMFQTIHQ LTSSPEDILM VTKDVIKEFA DDGVKYLELR STPRRENATG MTKKTYVESI LEGIKQSKQE NLDIDVRYLI AVDRRGGPLV AKETVKLAEE FFLSTEGTVL GLDLSGDPTV GQAKDFLEPL LEAKKAGLKL ALHLSEIPNQ KKETQILLDL LPDRIGHGTF LNSGEGGSLD LVDFVRQHRI PLGKAWSFRS SR.

    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.

    Adal Human
  • View Data Sheet

    Name :

    Ecotin E.Coli

    Description:

    Ecotin E.Coli Recombinant

    E. coli serine protease inhibitor.

    Product # :

    ENZ-058

    Price :

    Quantity :

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    Description

    Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Ecotin protein solution (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 50mM NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ecotin inhibits pancreatic serine proteases. Ecotin protein inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The power of inhibition is not linked to a specific protease specificity.

    • Synonyms

      E. coli serine protease inhibitor.

    • 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

      MGSSHHHHHH SSGLVPRGSH MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR

    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.

    Ecotin Ecoli
  • View Data Sheet

    Name :

    GLUL Human, Active

    Description:

    Glutamine Synthetase Human Recombinant, Active

    Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    Product # :

    ENZ-974

    Price :

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 373 amino acids (1-373) and having a molecular mass of 42kDa.

    Source

    Escherichia Coli.

    Formulation

    GLUL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2.000 pmol/min/ug, and is defined as the amount of enzyme that convert L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

    More Info

    • Introduction

      GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

    • Synonyms

      Glutamine synthetase, GLUL Active, GLUL, Glutamine Synthetase, Active, GLNS, GS, PIG43, PIG59, Glutamate decarboxylase (EC:4.1.1.15), Glutamate--ammonia ligase.

    • 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

      MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.

    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.

    Glul Human Active
  • View Data Sheet

    Name :

    DHRS4 Human

    Description:

    Dehydrogenase/Reductase Member 4 Human Recombinant

    Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    Product # :

    ENZ-207

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    Description

    DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHRS4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.

    • Synonyms

      Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    • 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 MGSHMHKAGL LGLCARAWNS VRMASSGMTR RDPLANKVAL VTASTDGIGF AIARRLAQDG AHVVVSSRKQ QNVDQAVATL QGEGLSVTGT VCHVGKAEDR ERLVATAVKL HGGIDILVSN AAVNPFFGSI MDVTEEVWDK TLDINVKAPA LMTKAVVPEM EKRGGGSVVI VSSIAAFSPS PGFSPYNVSK TALLGLTKTL AIELAPRNIR VNCLAPGLIK TSFSRMLWMD KEKEESMKET LRIRRLGEPE DCAGIVSFLC SEDASYITGE TVVVGGGTPS RL.

    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.

    Dhrs4 Human
  • View Data Sheet

    Name :

    NANP Human

    Description:

    N-Acetylneuraminic Acid Phosphatase Human Recombinant

    N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.

    Product # :

    ENZ-009

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    Description

    NANP Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 284 amino acids (1-248 a.a.) and having a molecular mass of 31.9kDa. The NANP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.

    • Synonyms

      N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGLS RVRAVFFDLD NTLIDTAGAS RRGMLEVIKL LQSKYHYKEE AEIICDKVQV KLSKECFHPY NTCITDLRTS HWEEAIQETK GGAANRKLAE ECYFLWKSTR LQHMTLAEDV KAMLTELRKE VRLLLLTNGD RQTQREKIEA CACQSYFDAV VVGGEQREEK PAPSIFYYCC NLLGVQPGDC VMVGDTLETD IQGGLNAGLK ATVWINKNGI VPLKSSPVPH YMVSSVLELP ALLQSIDCKV SMST.

    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.

    Nanp Human
  • View Data Sheet

    Name :

    NDUFB4 Human

    Description:

    NADH Dehydrogenase 1 Beta Subcomplex 4 Human Recombinant

    B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.

    Product # :

    ENZ-699

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    Description

    NDUFB4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87) and having a molecular mass of 12.6kDa.NDUFB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The NDUFB4 solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M Urea And 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH Dehydrogenase 1 Beta Subcomplex 4 (NDUFB4) is a member of the complex I NDUFB4 subunit family. NDUFB4 is a non-catalytic subunit of the multisubunit NADH:ubiquinone oxidoreductase, which is the first enzyme complex in the mitochondrial electron transport chain (complex I). Mammalian complex I is comprised of 45 different subunits and transfers electrons from NADH to ubiquinone.

    • Synonyms

      B15, CI-B15, Complex I-B15, NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 4, NADH-ubiquinone oxidoreductase B15 subunit.

    • 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 MGSMSFPKYK PSSLRTLPET LDPAEYNISP ETRRAQAERL AIRAQLKREY LLQYNDPNRR GLIENPALLR WAYARTINVY PNFRPTPKNS.

    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.

    Ndufb4 Human
  • View Data Sheet

    Name :

    GALE Human

    Description:

    UDP-Galactose-4-Epimerase Human Recombinant

    UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    Product # :

    ENZ-537

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    Description

    GALE Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-348 a.a.) and having a molecular mass of 40.4 kDa. The GALE is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GALE Human solution containing 20mM Tris pH-8, 5mM DTT, 0.1M NaCl, 1mM EDTA & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GALE is an enzyme that participates as the third enzyme in the Leloir pathway of galactose metabolism. GALE is a homodimeric epimerase localized in bacterial, plant, and mammalian cells. GALE inhances the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose. UDP-galactose builds galactose-containing proteins and fats, which have a crucial part in chemical signaling, building cellular structures, transporting molecules, and producing energy.

    • Synonyms

      UDP-glucose 4-epimerase, EC=5.1.3.2, Galactowaldenase, UDP-galactose 4 epimerase, GALE, SDR1E1, FLJ95174, FLJ97302.

    • 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 MAEKVLVTGG AGYIGSHTVL ELLEAGYLPV VIDNFHNAFR GGGSLPESLR RVQELTGRSV EFEEMDILDQ GALQRLFKKY SFMAVIHFAG LKAVGESVQK PLDYYRVNLT GTIQLLEIMK AHGVKNLVFS SSATVYGNPQ YLPLDEAHPT GGCTNPYGKS KFFIEEMIRD LCQADKTWNA VLLRYFNPTG AHASGCIGED PQGIPNNLMP YVSQVAIGRR EALNVFGNDY DTEDGTGVRD YIHVVDLAKG HIAALRKLKE QCGCRIYNLG TGTGYSVLQM VQAMEKASGK KIPYKVVARR EGDVAACYAN PSLAQEELGW TAALGLDRMC EDLWRWQKQN PSGFGTQA.

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    Gale Human
  • View Data Sheet

    Name :

    HARS Human, Sf9

    Description:

    Histidyl-tRNA Synthetase Human Recombinant, Sf9

    Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1.

    Product # :

    ENZ-335

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    Description

    Histidyl-tRNA Synthetase Human Recombinant produced in baculovirus is a single, glycosylated, polypeptide chain having a molecular mass of 58.3 kDa.The Histidyl-tRNA Synthetase is fused to 6x His Tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 Insect Cells.

    Formulation

    The protein solution contains 20mM HEPES, 250mM sodium chloride 0.1% and 20% Glycerol, (pH 7.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.

    • Synonyms

      Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.

    • Applications

      Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.

    • Protein content

      Protein quantitation was carried out by using 0.25 - 2.0 mg/ml Bradford assay vs. BSA.

    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.

    Jo 1 Human Sf9
  • View Data Sheet

    Name :

    Lysozyme Human

    Description:

    Lysozyme Human Recombinant

    EC 3.2.1.17, LYZ, Lysozyme.

    Product # :

    ENZ-1159

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    Description

    Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Purity as determined by SDS-PAGE is greater than 90%.

    Biological Activity

    1.6x105 U/mg.

    More Info

    • Introduction

      Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

    • Synonyms

      EC 3.2.1.17, LYZ, Lysozyme.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) off white powder.

    • Stability

      Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.

    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.

    Lysozyme Human
  • View Data Sheet

    Name :

    ENTPD3 Human, sf9

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9

    Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    Product # :

    ENZ-958

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    Description

    ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ENTPD3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

    • Synonyms

      Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.

    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.

    Entpd3 Human Sf9
  • View Data Sheet

    Name :

    NDUFA2 Human

    Description:

    NADH Dehydrogenase 1 Alpha Subcomplex 2 Human Recombinant

    NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.

    Product # :

    ENZ-660

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    Description

    NDUFA2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 122 amino acids (1-99) and having a molecular mass of 13.3kDa.NDUFA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFA2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5 (NDUFA5) is a member of the complex I NDUFA5 subunit family. The human NDUFA5 gene codes for the B13 subunit of complex I of the respiratory chain that transfers electrons from NADH to ubiquinone. The NDUFA5 protein localizes to the inner mitochondrial membrane as part of the seven component-containing, water soluble 'iron-sulfur protein' (IP) fraction of complex I, even though its exact role is undetermined.

    • Synonyms

      NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2, Complex I-B8, CI-B8, NADH-ubiquinone oxidoreductase B8 subunit, NDUFA2, CD14, CIB8.

    • 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 MGSMAAAAAS RGVGAKLGLR EIRIHLCQRS PGSQGVRDFI EKRYVELKKA NPDLPILIRE CSDVQPKLWA RYAFGQETNV PLNNFSADQV TRALENVLSG KA.

    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.

    Ndufa2 Human
  • View Data Sheet

    Name :

    HAO1 Mouse

    Description:

    Hydroxyacid Oxidase 1 Mouse Recombinant

    (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    Product # :

    ENZ-1104

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    Description

    HAO1 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-370) and having a molecular mass of 43.4 kDa.HAO1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HAO1 protein (1mg/ml) is containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.

    More Info

    • Introduction

      Hydroxyacid Oxidase 1 (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.

    • Synonyms

      (S)-2-hydroxy-acid oxidase; EC 1.1.3.15, Glycolate oxidase, GOX, GOX1MGC142227;
      GOXMGC142225, HAO1, HAO-1, HAOX1, hydroxyacid oxidase (glycolate oxidase) 1, hydroxyacid oxidase 1, Hydroxyacid Oxidase1, Hydroxyacid Oxidase-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMLPRLVC ISDYEQHVRS VLQKSVYDYY RSGANDQETL ADNIQAFSRW KLYPRMLRNV ADIDLSTSVL GQRVSMPICV GATAMQCMAH VDGELATVRA CQTMGTGMML SSWATSSIEE VAEAGPEALR WMQLYIYKDR EISRQIVKRA EKQGYKAIFV TVDTPYLGNR IDDVRNRFKL PPQLRMKNFE TNDLAFSPKG NFGDNSGLAE YVAQAIDPSL SWDDITWLRR LTSLPIVVKG ILRGDDAKEA VKHGVDGILV SNHGARQLDG VPATIDVLPE IVEAVEGKVE VFLDGGVRKG TDVLKALALG AKAVFVGRPI IWGLAFQGEK GVQDVLEILK EEFRLAMALS GCQNVKVIDK TLVRKNPLAV SKI.

    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.

    Hao1 Mouse
  • View Data Sheet

    Name :

    RPE Human

    Description:

    Ribulose-5-Phosphate-3-Epimerase Human Recombinant

    Ribulose-phosphate 3-epimerase, Ribulose-5-phosphate-3-epimerase, RPE, HUSSY-17, RPE2-1.

    Product # :

    ENZ-584

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    Description

    RPE Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-228) and having a molecular mass of 27.5kDa.RPE is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RPE solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 30% glycerol and 200mM NaCl.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribulose-phosphate 3-epimerase (RPE) is a member of the ribulose-phosphate 3-epimerase family. RPE is the enzyme which converts D-ribulose 5-phosphate into D-xylulose 5-phosphate in Calvin's reductive pentose phosphate cycle. Therefore, the RPE enzyme has one substrate, D-ribulose 5-phosphate, and one product, D-xylulose 5-phosphate. RPE participates in three metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation.

    • Synonyms

      Ribulose-phosphate 3-epimerase, Ribulose-5-phosphate-3-epimerase, RPE, HUSSY-17, RPE2-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMASGCK IGPSILNSDL ANLGAECLRM LDSGADYLHL DVMDGHFVPN ITFGHPVVES LRKQLGQDPF FDMHMMVSKP EQWVKPMAVA GANQYTFHLE ATENPGALIK DIRENGMKVG LAIKPGTSVE YLAPWANQID MALVMTVEPG FGGQKFMEDM MPKVHWLRTQ FPSLDIEVDG GVGPDTVHKC AEAGANMIVS GSAIMRSEDP RSVINLLRNV CSEAAQKRSL DR.

    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.

    Rpe Human
  • View Data Sheet

    Name :

    DARS Human

    Description:

    Aspartyl-tRNA Synthetase Human Recombinant

    Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    Product # :

    ENZ-591

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    Description

    DARS Recombinant produced in E. coli is a single polypeptide chain containing 521 amino acids (1-501) and having a molecular mass of 59.3kDa.DARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DARS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM Nacl, 1mM DTT and 40% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      DARS uses a 2 step reaction to catalyze the specific attachment of an amino acid to its cognate tRNA: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

    • Synonyms

      Aspartyl-tRNA synthetase, Cell proliferation-inducing gene 40 protein, AspRS, aspartate tRNA ligase 1 cytoplasmic, EC 6.1.1.12.

    • 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 MPSASASRKS QEKPREIMDA AEDYAKERYG ISSMIQSQEK PDRVLVRVRD LTIQKADEVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIVDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAV RPEAEGEEEG RATVNQDTRL DNRVIDLRTS TSQAVFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP QLYKQMCICA DFEKVFSIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH EVMEEIADTM VQIFKGLQER FQTEIQTVNK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV EMGDEDDLST PNEKLLGHLV KEKYDTDFYI LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT P.

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    Dars Human
  • View Data Sheet

    Name :

    PCOLCE Human, Sf9

    Description:

    Procollagen C-Endopeptidase Enhancer Human Recombinant, Sf9

    Procollagen C-endopeptidase enhancer 1,  Procollagen COOH-terminal proteinase enhancer 1,  PCPE-1,  Procollagen C-proteinase enhancer 1,  Type 1 procollagen C-proteinase enhancer protein,  Type I procollagen COOH-terminal proteinase enhancer,  PCOLCE,  PCPE1,  Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1.

    Product # :

    ENZ-1075

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    Description

    PCOLCE produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 433 amino acids (26-449 a.a.) and having a molecular mass of 46.6kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PCOLCE is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    PCOLCE protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

    • Synonyms

      Procollagen C-endopeptidase enhancer 1, Procollagen COOH-terminal proteinase enhancer 1, PCPE-1, Procollagen C-proteinase enhancer 1, Type 1 procollagen C-proteinase enhancer protein, Type I procollagen COOH-terminal proteinase enhancer, PCOLCE, PCPE1, Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase, Enhancer 1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 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

      ADPQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQDHHH 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.

    Pcolce Protein
  • View Data Sheet

    Name :

    CES1 Human

    Description:

    Carboxylesterase 1 Human Recombinant

    Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    Product # :

    ENZ-1099

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    Description

    CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.

    • Synonyms

      Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.

    • 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

      ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
      SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
      VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
      VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
      LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
      SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
      QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
      RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
      MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.

    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.

    Ces1 Human
  • View Data Sheet

    Name :

    LOX Human

    Description:

    Lysyl Oxidase Human Recombinant

    Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.

    Product # :

    ENZ-829

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    Description

    LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.

    • Synonyms

      Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.

    • 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 MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.

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    Lox Human
  • View Data Sheet

    Name :

    NARS Human

    Description:

    Asparaginyl-TRNA Synthetase Human Recombinant

    NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    Product # :

    ENZ-915

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    Description

    NARS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 571 amino acids (1-548 a.a) and having a molecular mass of 65.3kDa. NARS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NARS protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aminoacyl-tRNA synthetases are a class of enzymes which charge tRNAs with their cognate amino acids. Asparaginyl-tRNA synthetase (NARS) is localized to the cytoplasm and is a member of the class II family of tRNA synthetases. The N-terminal domain characterizes the signature sequence for the eukaryotic asparaginyl-tRNA synthetases.

    • Synonyms

      NARS, Asparaginyl-TRNA Synthetase, AsnRS, EC 6.1.1.22, Asparaginyl-TRNA Synthetase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, Asparagine--TRNA Ligase, Cytoplasmic, Asparagine TRNA Ligase 1, Cytoplasmic, NARS1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSMVLAELY VSDREGSDAT GDGTKEKPFK TGLKALMTVG KEPFPTIYVD SQKENERWNV ISKSQLKNIK KMWHREQMKS ESREKKEAED SLRREKNLEE AKKITIKNDP SLPEPKCVKI GALEGYRGQR VKVFGWVHRL RRQGKNLMFL VLRDGTGYLQ CVLADELCQC YNGVLLSTES SVAVYGMLNL TPKGKQAPGG HELSCDFWEL IGLAPAGGAD NLINEESDVD VQLNNRHMMI RGENMSKILK ARSMVTRCFR DHFFDRGYYE VTPPTLVQTQ VEGGATLFKL DYFGEEAFLT QSSQLYLETC LPALGDVFCI AQSYRAEQSR TRRHLAEYTH VEAECPFLTF DDLLNRLEDL VCDVVDRILK SPAGSIVHEL NPNFQPPKRP FKRMNYSDAI VWLKEHDVKK EDGTFYEFGE DIPEAPERLM TDTINEPILL CRFPVEIKSF YMQRCPEDSR LTESVDVLMP NVGEIVGGSM RIFDSEEILA GYKREGIDPT PYYWYTDQRK YGTCPHGGYG LGLERFLTWI LNRYHIRDVC LYPRFVQRCT P.

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

    Human Nars
  • View Data Sheet

    Name :

    YARS2 Human

    Description:

    Tyrosyl-tRNA Synthetase 2 Human Recombinant

    Tyrosine--tRNA ligase mitochondrial, Tyrosyl-tRNA synthetase, TyrRS, YARS2, CGI-04, TYRRS, MLASA2, MT-TYRRS.

    Product # :

    ENZ-614

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    Description

    YARS2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 482 amino acids (17-477 a.a.) and having a molecular mass of 53.7kDa.YARS2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YARS2 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tyrosyl-tRNA synthetase (YARS2) is a mitochondrial protein which catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and afterward transferred to the acceptor end of tRNA(Tyr). YARS2 gene mutations are linked with myopathy with lactic acidosis and sideroblastic anemia type 2 (MLASA2).

    • Synonyms

      Tyrosine--tRNA ligase mitochondrial, Tyrosyl-tRNA synthetase, TyrRS, YARS2, CGI-04, TYRRS, MLASA2, MT-TYRRS.

    • 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 MTLNLSVLLP LGLRKAHSGA QGLLAAQKAR GLFKDFFPET GTKIELPELF DRGTASFPQT IYCGFDPTAD SLHVGHLLAL LGLFHLQRAG HNVIALVGGA TARLGDPSGR TKEREALETE RVRANARALR LGLEALAANH QQLFTDGRSW GSFTVLDNSA WYQKQHLVDF LAAVGGHFRM GTLLSRQSVQ LRLKSPEGMS LAEFFYQVLQ AYDFYYLFQR YGCRVQLGGS DQLGNIMSGY EFINKLTGED VFGITVPLIT STTGAKLGKS AGNAVWLNRD KTSPFELYQF FVRQPDDSVE RYLKLFTFLP LPEIDHIMQL HVKEPERRGP QKRLAAEVTK LVHGREGLDS AKRCTQALYH SSIDALEVMS DQELKELFKE APFSEFFLDP GTSVLDTCRK ANAIPDGPRG YRMITEGGVS INHQQVTNPE SVLIVGQHIL KNGLSLLKIG KRNFYIIKWL QL.

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    Yars2 Human
  • View Data Sheet

    Name :

    TrxR Yeast

    Description:

    Thioredoxin Reductase (NADPH) Yeast Recombinant

    Thioredoxin Reductase (NADPH), NTR, TrxR.

    Product # :

    ENZ-278

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    Description

    Thioredoxin Reductase (NADPH) Yeast Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 36 kDa. Thioredoxin Reductase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Each mg of protein contains 20mM phosphate buffer pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The specific activity was found to be 5.8 IU/mg.

    More Info

    • Introduction

      Thioredoxin reductase (TrxR/NTR), an enzyme belonging to the flavoprotein family of pyridine nucleotide-disulfide oxidoreductases. Thioredoxin reductase (TrxR), a component of the thioredoxin system, including thioredoxin (Trx) and NADPH, catalyzes the transfer of electrons from NADPH to Trx, acts as a reductant of disulfide-containing proteins and participates in the defense system against oxidative stresses.

    • Synonyms

      Thioredoxin Reductase (NADPH), NTR, TrxR.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      NTR although stable at 4°C for 3 weeks, should be stored desiccated below -18°C. Please prevent freeze thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized NTR in sterile 18MΩ-cm H2O.

    • Unit Definition

      One unit equals the change in absorbance at 412 nm per minute at 25°C using 0.2mM NADPH containing 5mM DTNB (pH 7.0).

    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.

    Thioredoxin Reductase Yeast
  • 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.

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    Got1 Mouse
  • View Data Sheet

    Name :

    HYAL1

    Description:

    Hyaluronidase

    Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.

    Product # :

    ENZ-323

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    • More Info

    Description

    Hyaluronidase is an enzyme that temporarily and reversibly breaks down the polysaccharide, hyaluronic acid, which is found between the cells of connective tissue. Hyaluronic acid may be thought of as the "glue" that holds cells together. Hyaluronic acid is a mucopolysaccharide that exists in the human tissue matrix. It can constrain the diffusion of the extracellular fluid. Hyaluronidase makes the glucoseamine of the hyaluronic acid molecules hydrolyzed and depolymerized, thus decreases the viscosity of the body fluids and increases the flow and diffusion of the intercellular fluids. In this way the physic liquor, exudates or blood in local areas can be more easily diffused, and the drug can be more easily absorbed. Thus the local tissue tension and pains can be relieved. And it will also be easier for the edema and inflammatory exudates to be absorbed and dissolved. This product is a basic component of the articular cartilage. It can nourish, protect and maintain the functions of the joints.

    Source

    Bovine Testis.

    Formulation

    The enzyme was lyophilized 1xPBS and 2% sucrose.

    More Info

    • Synonyms

      Hyaluronidase-1, EC 3.2.1.35, Hyal-1, Hyaluronoglucosaminidase-1, LUCA-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Specific Activity

      300 IU/mg.

    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.

    Hyaluronidase
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