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Search results

1000 results found for “ATPase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    PTPS Human

    Description:

    6-Pyruvoyltetrahydropterin Synthase Human Recombinant

    PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.

    Product # :

    ENZ-471

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    Description

    6-PyruvoylTetrahydropterin Synthase Human Recombinant produced in e.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-145) and having a molecular mass of 18.5kDa. 6-PyruvoylTetrahydropterin Synthase is fused to a 20 amino acid His Tag at N-terminus and purified using conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    6-PyruvoylTetrahydropterin Synthase is formulated in 20mM Tris-HCl buffer pH-8, 1mM DTT and 20% glycerol.

    Purity

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

    More Info

    • Introduction

      6-PyruvoylTetrahydropterin Synthase is part of the family of lyases, specifically those carbon-oxygen lyases acting on phosphates. 6-PyruvoylTetrahydropterin Synthase catalyzes the elimination of inorganic triphosphate from dihydroneopterin triphosphate, which is the second and irreversible step in the biosynthesis of tetrahydrobiopterin from GTP. Tetrahydrobiopterin, is a necessary cofactor and regulator of a range of enzyme activities, including enzymes involved in serotonin biosynthesis and NO synthase activity. Mutations in 6-PyruvoylTetrahydropterin Synthase gene result in hyperphenylalaninemia.

    • Synonyms

      PTP Synthase, 6-Pyruvoyl Tetrahydropterin Synthase, PTPS, PTS, FLJ97081.

    • 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 MSTEGGGRRC QAQVSRRISF SASHRLYSKF LSDEENLKLF GKCNNPNGHG HNYKVVVTVH GEIDPATGMV MNLADLKKYM EEAIMQPLDH KNLDMDVPYF ADVVSTTENV AVYIWDNLQK VLPVGVLYKV KVYETDNNIV VYKGE.

    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.

    Ptps Human
  • View Data Sheet

    Name :

    GSTZ1 Human

    Description:

    Glutathione Transferase Zeta 1 Human Recombinant

    MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    Product # :

    ENZ-494

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    Description

    GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.

    • Synonyms

      MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

    • 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 MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.

    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.

    Gstz1 Human
  • View Data Sheet

    Name :

    GOT2 Mouse

    Description:

    Glutamic-Oxaloacetic Transaminase 2 Mouse Recombinant

    Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.

    Product # :

    ENZ-1095

    Price :

    Quantity :

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    Description

    GOT2 Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 46.8kDa. Mouse GOT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT2 solution (0.5mg/ml) contains PBS, pH 7.4 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Activity is greater than 20 units/mg, and is defined as the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25℃.

    More Info

    • Introduction

      GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 takes part in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and demonstrate close homology.

    • Synonyms

      Transaminase A, KAT4, KATIV, KAT-4, KAT-IV,Kynurenine Aminotransferase 4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSSWWTHVEM GPPDPILGVT EAFKRDTNSK KMNLGVGAYR DDNGKPYVLP SVRKAEAQIA AKNLDKEYLP IGGLAEFCKA SAELALGENN EVLKSGRFVT VQTISGTGAL RVGASFLQRF FKFSRDVFLP KPSWGNHTPI FRDAGMQLQG YRYYDPKTCG FDFSGALEDI SKIPEQSVLL LHACAHNPTG VDPRPEQWKE IASVVKKKNL FAFFDMAYQG FASGDGDKDA WAVRHFIEQG INVCLCQSYA KNMGLYGERV GAFTVVCKDA EEAKRVESQL KILIRPLYSN PPLNGARIAA TILTSPDLRK QWLQEVKGMA DRIISMRTQL VSNLKKEGSS HNWQHITDQI GMFCFTGLKP EQVERLTKEF SVYMTKDGRI SVAGVTSGNV GYLAHAIHQV.

    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.

    Got2 Mouse
  • View Data Sheet

    Name :

    Staphylokinase

    Description:

    Staphylokinase Recombinant

    Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    Product # :

    ENZ-288

    Price :

    Quantity :

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    • sds-page

    Description

    Staphylokinase Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 136 amino acids and having a molecular weight of 16kDa.The Staphylokinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity measured by the ability of fibrin lysis in agarose plate was found to be 50,000IU/mg.

    sds-page

    Staphylokinase sds-page - Product image 1

    More Info

    • Introduction

      Staphylokinase (SAK) is a 136-amino acidenzymefrom Staphylococcus aureus. It is positively regulated by the "agr" gene regulator. It activates plasminogen, which in turn can degrade various host proteins during infection.

    • Synonyms

      Staphylokinase, SakSTAR, Neutral proteinase, Protease III, SAK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SAK should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    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.

    Staphylokinase
  • View Data Sheet

    Name :

    ACADM Human

    Description:

    Acyl-Coenzyme A Dehydrogenase, C-4 to C-12 Human Recombinant

    ACADM, ACAD1, CAD, MCADH, MCAD, EC=1.3.99.3, Medium-chain specific acyl-CoA dehydrogenase, mitochondrial, FLJ18227, FLJ93013, FLJ99884.

    Product # :

    ENZ-529

    Price :

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    Description

    ACADM Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 417 amino acids (26-421 a.a.) and having a molecular mass of 45.9 kDa. The ACADM is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACADM (0.5mg/ml) protein solution containing 20mM Tris-HCl pH-7.5, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACADM enzyme is essential for the degradation a certain group of fats called medium-chain fatty acids. ACADM is essential for converting specific fatty acids to energy, mainly during fasting periods. ACADM functions in mitochondria, the energy-producing centers within cells. ACADM is localized in the mitochondria of numerous tissue types, predominantly the liver.

    • Synonyms

      ACADM, ACAD1, CAD, MCADH, MCAD, EC=1.3.99.3, Medium-chain specific acyl-CoA dehydrogenase, mitochondrial, FLJ18227, FLJ93013, FLJ99884.

    • 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 MKANRQREPG LGFSFEFTEQ QKEFQATARK FAREEIIPVA AEYDKTGEYP VPLIRRAWEL GLMNTHIPEN CGGLGLGTFD ACLISEELAY GCTGVQTAIE GNSLGQMPII IAGNDQQKKK YLGRMTEEPL MCAYCVTEPG AGSDVAGIKT KAEKKGDEYI INGQKMWITN GGKANWYFLL ARSDPDPKAP ANKAFTGFIV EADTPGIQIG RKELNMGQRC SDTRGIVFED VKVPKENVLI GDGAGFKVAM GAFDKTRPVV AAGAVGLAQR ALDEATKYAL ERKTFGKLLV EHQAISFMLA EMAMKVELAR MSYQRAAWEV DSGRRNTYYA SIAKAFAGDI ANQLATDAVQ ILGGNGFNTE YPVEKLMRDA KIYQIYEGTS QIQRLIVARE HIDKYKN.

    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.

    Acadm Human
  • 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

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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 :

    ADPRH Human

    Description:

    ADP-Ribosylarginine Hydrolase Human Recombinant

    [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

    Product # :

    ENZ-631

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    Description

    ADPRH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-357) and having a molecular mass of 42.1kDa.ADPRH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADPRH solution (0.5mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADP-ribosylarginine hydrolase (ADPRH) is a member of the ADP-ribosylglycohydrolase family. ADPRH catalyzes the removal of mono-ADP-ribose from arginine residues of proteins in the ADP-ribosylation cycle. The human ADPRH enzyme is DTT-independent as opposed to the rat and mouse enzymes, which require DTT for maximal activity.

    • Synonyms

      [Protein ADP-ribosylarginine] hydrolase, ADP-ribosylarginine hydrolase, ADP-ribose-L-arginine cleaving enzyme, ADPRH, ARH1.

    • 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 MGSHMEKYVA AMVLSAAGDA LGYYNGKWEF LQDGEKIHRQ LAQLGGLDAL DVGRWRVSDD TVMHLATAEA LVEAGKAPKL TQLYYLLAKH YQDCMEDMDG RAPGGASVHN AMQLKPGKPN GWRIPFNSHE GGCGAAMRAM CIGLRFPHHS QLDTLIQVSI ESGRMTHHHP TGYLGALASA LFTAYAVNSR PPLQWGKGLM ELLPEAKKYI VQSGYFVEEN LQHWSYFQTK WENYLKLRGI LDGESAPTFP ESFGVKERDQ FYTSLSYSGW GGSSGHDAPM IAYDAVLAAG DSWKELAHRA FFHGGDSDST AAIAGCWWGV MYGFKGVSPS NYEKLEYRNR
      LEETARALYS LGSKEDTVIS L.

    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.

    Adprh Human
  • View Data Sheet

    Name :

    NDUFS5 Human

    Description:

    Histidine NADH Dehydrogenase Fe-S Protein 5 Human Recombinant

    CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    Product # :

    ENZ-771

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    Description

    NDUFS5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 129 amino acids (1-106a.a) and having a molecular mass of 14.9kDa. NDUFS5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NDUFS5 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Histidine NADH Dehydrogenase Fe-S Protein 5 (NDUFS5) belongs to the NADH dehydrogenase (ubiquinone) iron-sulfur protein family. NDUFS5 is a subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which doesn’t take part in catalysis. Complex I is transferring the electrons from NADH to the respiratory chain.

    • Synonyms

      CI-15k, CI15K, NADH dehydrogenase [ubiquinone] iron-sulfur protein 5, Complex I-15 kDa, NADH-ubiquinone oxidoreductase 15 kDa subunit, CI-15 kDa, NDUFS5.

    • 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 MGSMPFLDIQ KRFGLNIDRW LTIQSGEQPY KMAGRCHAFE KEWIECAHGI GYTRAEKECK IEYDDFVECL LRQKTMRRAG TIRKQRDKLI KEGKYTPPPH HIGKGEPRP.

    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.

    Ndufs5 Human
  • View Data Sheet

    Name :

    AS3MT Human

    Description:

    Arsenic Methyltransferase Human Recombinant

    Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.

    Product # :

    ENZ-615

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    Description

    AS3MT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 399 amino acids (1-375 a.a.) and having a molecular mass of 44.3kDa.AS3MT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AS3MT protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.15M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Arsenic Methyltransferase (AS3MT) catalyzes the transfer of a methyl group from S-adenosyl-L-methionine (AdoMet) to trivalent arsenical and may have a role in arsenic metabolism. AS3MT methylates arsenite to produce methylarsonate, Me-AsO3H2, which is reduced by methylarsonate reductase to methylarsonite, Me-As(OH)2. Methylarsonite which is also a substrate, is transformed into the much less toxic complex dimethylarsinate (cacodylate), Me2As(O)-OH.

    • Synonyms

      Arsenite methyltransferase, Methylarsonite methyltransferase, S-adenosyl-L-methionine:arsenic(III) methyltransferase, AS3MT, CYT19, RP11-753C18.6.

    • 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 MGSHMAALRD AEIQKDVQTY YGQVLKRSAD LQTNGCVTTA RPVPKHIREA LQNVHEEVAL RYYGCGLVIP EHLENCWILD LGSGSGRDCY VLSQLVGEKG HVTGIDMTKG QVEVAEKYLD YHMEKYGFQA SNVTFIHGYI EKLGEAGIKN ESHDIVVSNC
      VINLVPDKQQ VLQEAYRVLK HGGELYFSDV YTSLELPEEI RTHKVLWGEC LGGALYWKEL AVLAQKIGFC PPRLVTANLI TIQNKELERV IGDCRFVSAT FRLFKHSKTG PTKRCQVIYN GGITGHEKEL MFDANFTFKE GEIVEVDEET AAILKNSRFA QDFLIRPIGE KLPTSGGCSA
      LELKDIITDP FKLAEESDSM KSRCVPDAAG GCCGTKKSC.

    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.

    As3Mt Human
  • View Data Sheet

    Name :

    PARP1 Human

    Description:

    Poly (ADP-Ribose) Polymerase 1 Human Recombinant

    ADPRT, ADPRT1, pADPRT, pADPRT-1, PARP, PARP-1, PPOL, Poly [ADP-ribose] polymerase 1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, PARP1.

    Product # :

    ENZ-477

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    Description

    PARP1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 354 amino acids (662-1014a.a.) and having a molecular mass of 39.6 kDa. PARP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PARP1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PARP1 takes part in the base excision repair pathway, by catalyzing the poly ADP-ribosyl of a restricted number of acceptor proteins involved in chromatin architecture and in DNA metabolism.. PARP1 mediates the poly ADP-ribosy of APLF and CHFR. PARP1 positively regulates the transcription of MTUS1 and negatively regulates the transcription of MTUS2/TIP150. PARP1 is a chromatin-associated enzyme, poly (ADP-ribosyl) transferase, which modifies various nuclear proteins by poly ADP-ribosyl. PARP1 takes part in the regulation of various significant cellular processes such as differentiation, proliferation, and tumor transformation and also in the regulation of the molecular events involved in the recovery of cell from DNA damage. PARP1 is a site of mutation in Fanconi anemia, and is involved in the pathophysiology of type I diabetes.

    • Synonyms

      ADPRT, ADPRT1, pADPRT, pADPRT-1, PARP, PARP-1, PPOL, Poly [ADP-ribose] polymerase 1, NAD(+) ADP-ribosyltransferase 1, Poly[ADP-ribose] synthase 1, PARP1.

    • 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

      MKSKLPKPVQ DLIKMIFDVE SMKKAMVEYE IDLQKMPLGK LSKRQIQAAY SILSEVQQAV SQGSSDSQIL DLSNRFYTLI PHDFGMKKPP LLNNADSVQA KAEMLDNLLD IEVAYSLLRG GSDDSSKDPI DVNYEKLKTD IKVVDRDSEE AEIIRKYVKN THATTHNAYD LEVIDIFKIE REGECQRYKP FKQLHNRRLL WHGSRTTNFA GILSQGLRIA PPEAPVTGYM FGKGIYFADM VSKSANYCHT SQGDPIGLIL LGEVALGNMY ELKHASHISK LPKGKHSVKG LGKTTPDPSA NISLDGVDVP LGTGISSGVN DTSLLYNEYI VYDIAQVNLK YLLKLKFNFK TSLW.

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    Parp1 Human
  • View Data Sheet

    Name :

    MMP 1 Human

    Description:

    Matrix Metalloproteinase-1 Human Recombinant

    CLG, CLGN, Matrix metalloproteinase-1, MMP-1.

    Product # :

    ENZ-765

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    Description

    MMP 1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (100-469a.a) and having a molecular mass of 45kDa. MMP 1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-1 can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      CLG, CLGN, Matrix metalloproteinase-1, MMP-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 MGSFVLTEGN PRWEQTHLTY RIENYTPDLP RADVDHAIEK AFQLWSNVTP LTFTKVSEGQ ADIMISFVRG DHRDNSPFDG PGGNLAHAFQ PGPGIGGDAH FDEDERWTNN FREYNLHRVA AHELGHSLGL SHSTDIGALM YPSYTFSGDV QLAQDDIDGI QAIYGRSQNP VQPIGPQTPK ACDSKLTFDA ITTIRGEVMF FKDRFYMRTN PFYPEVELNF ISVFWPQLPN GLEAAYEFAD RDEVRFFKGN KYWAVQGQNV LHGYPKDIYS SFGFPRTVKH IDAALSEENT GKTYFFVANK YWRYDEYKRS MDPGYPKMIA HDFPGIGHKV DAVFMKDGFF YFFHGTRQYK FDPKTKRILT LQKANSWFNC RKN.

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    Mmp 1 Enzyme
  • View Data Sheet

    Name :

    Welqut Protease

    Description:

    Welqut Protease Staphylococcus aureus Recombinant

    Product # :

    ENZ-1113

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    Description

    Welqut Protease Recombinant is a single, non-glycosylated polypeptide chain containing 204 amino acids and having a molecular mass of 22kDa. The Welqut Protease is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Welqut Protease contains 10 mM Na2HPO4, 50% glycerol, 1.8 mM KH2PO4, pH 7.3, 140 mM NaCl and 2.7 mM KCl.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WELQut Protease is an extremely specific and recombinant serine protease from Staphylococcus aureus. The WELQut Protease identifies and accurately cleaves recombinant proteins that has a recognition sequence added to them, with the amino acid sequence Trp, Glu, Leu, Gln, X (any amino acid). WELQut Protease cut externally from the recognition sequence, therefor doesn’t leave extra amino acids bound to the target protein. The protease isn’t temperature sensitive (works in 4-30°C) or pH sensitive (pH 6.5-9.0), also, there is no need in any particular buffers.

    • 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.

    • Unit Definition

      Each unit is defined as the amount of enzyme required to cleave ≥99% of 100μg of a control protein in 16 h at 20°C. Enzyme activity is assayed in 100μl 100 mM Tris-HCl (pH 8.0).

    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.

    Welqut Protease
  • View Data Sheet

    Name :

    UGT8 Human

    Description:

    UDP Glycosyltransferase 8 Human Recombinant

    UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.

    Product # :

    ENZ-754

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    Description

    UGT8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 544 amino acids (21-541 a.a) and having a molecular mass of 61.6kDa.UGT8 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    UGT8 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      UDP Glycosyltransferase 8 (UGT8) is a member of the UDP-glycosyltransferase family. UGT8 catalyzes the transfer of galactose to ceramide, a crucial enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system.

    • Synonyms

      UDP Glycosyltransferase 8, CGT, UDP-Galactose Ceramide Galactosyltransferase, 2-Hydroxyacylsphingosine 1-Beta-Galactosyltransferase, Ceramide UDP-Galactosyltransferase, Cerebroside Synthase, UGT4, UDP-Galactose-Ceramide Galactosyltransferase, Uridine Diphosphate Glycosyltransferase 8, EC 2.4.1.45, EC 2.4.1.

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSAKIIIVP PIMFESHMYI FKTLASALHE RGHHTVFLLS EGRDIAPSNH YSLQRYPGIF NSTTSDAFLQ SKMRNIFSGR LTAIELFDIL DHYTKNCDLM VGNHALIQGL KKEKFDLLLV DPNDMCGFVI AHLLGVKYAV FSTGLWYPAE VGAPAPLAYV PEFNSLLTDR MNLLQRMKNT GVYLISRLGV SFLVLPKYER IMQKYNLLPE KSMYDLVHGS SLWMLCTDVA LEFPRPTLPN VVYVGGILTK PASPLPEDLQ RWVNGANEHG FVLVSFGAGV KYLSEDIANK LAGALGRLPQ KVIWRFSGPK PKNLGNNTKL IEWLPQNDLL GHSKIKAFLS HGGLNSIFET MYHGVPVVGI PLFGDHYDTM TRVQAKGMGI LLEWKTVTEK ELYEALVKVI NNPSYRQRAQ KLSEIHKDQP GHPVNRTIYW IDYIIRHNGA HHLRAAVHQI SFCQYFLLDI AFVLLLGAAL LYFLLSWVTK FIYRKIKSLW SRNKHSTVNG HYHNGILNGK YKRNGHIKHE KKVK.

    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.

    Ugt8 Human
  • View Data Sheet

    Name :

    Esterase D Human

    Description:

    Esterase D,S-Formylglutathione Hydrolase Human Recombinant

    S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.

    Product # :

    ENZ-447

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    Description

    Esterase-D 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 302 amino acids (1-282 a.a.) and having a molecular mass of 33.6kDa.The Esterase-D is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Esterase-D solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.

    • Synonyms

      S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.

    • 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 MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEDYDH SYYFIATFIT DHIRHHAKYL NA.

    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.

    Esterase D Human
  • View Data Sheet

    Name :

    AK2 Human

    Description:

    Adenylate Kinase 2 Human Recombinant

    ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    Product # :

    PKA-260

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    Description

    AK2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 259 amino acids and having a molecular mass of 28.6 kDa. AK2 is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AK2 solution containing 20mM Tris pH-7.5, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity: > 1.5 units/ml. One unit will convert 2.0 umoles of ADP to ATP + AMP per minute at pH 7.5 at 25C.

    More Info

    • Introduction

      Adenylate kinases play a role in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. There are 3 types of adenylate kinase isozymes, AK1, AK2, and AK3 in vertebrates. Expression of these isozymes are tissue-specific and developmentally regulated. AK2 is localized in the mitochondrial intermembrane space and is involved in apoptosis. AK2 is mutated in individuals with reticular dysgenesis.

    • Synonyms

      ADK2, AK-2, Adenylate kinase isoenzyme 2 mitochondrial, ATP-AMP transphosphorylase 2, adenylate kinase 2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      AK2 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAPSVPAAEP EYPKGIRAVL LGPPGAGKGTQAPRLAENFC VCHLATGDML RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG FPRTVRQAEM LDDLMEKRKE KLDSVIEFSIPDSLLIRRIT GRLIHPKSGR SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI.

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    Ak2 Human
  • View Data Sheet

    Name :

    BHMT2 Human

    Description:

    Betaine-Homocysteine Methyltransferase 2 Human Recombinant

    BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.

    Product # :

    ENZ-798

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    Description

    BHMT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a.) and having a molecular mass of 42.7kDa. BHMT2 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    BHMT2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.

    • Synonyms

      BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.

    • 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 MGSMAPAGRP GAKKGILERL ESGEVVIGDG SFLITLEKRG YVKAGLWTPE AVIEHPDAVR QLHMEFLRAG SNVMQTFTFS ASEDNMESKW EDVNAAACDL AREVAGKGDA LVAGGICQTS IYKYQKDEAR IKKLFRQQLE VFAWKNVDFL IAEYFEHVEE AVWAVEVLKE SDRPVAVTMC IGPEGDMHDI TPGECAVRLV KAGASIVGVN CRFGPDTSLK TMELMKEGLE WAGLKAHLMV QPLGFHAPDC GKEGFVDLPE YPFGLESRVA TRWDIQKYAR EAYNLGVRYI GGCCGFEPYH IRAIAEELAP ERGFLPPASE KHGSWGSGLD MHTKPWIRAR ARREYWENLL PASGRPFCPS LSKPDF.

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    Bhmt2 Human
  • View Data Sheet

    Name :

    DERA

    Description:

    Deoxyribose-Phosphate Aldolase E.Coli Recombinant

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

    Product # :

    ENZ-127

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    Description

    DERA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 29.9kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DERA solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.

    Purity

    Greater than 95.0% 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 MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH GDGKSASSY.

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    Dera Ecoli 259 Aa
  • 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 :

    PPA1 Human

    Description:

    Pyrophosphatase-1 Human Recombinant

    Pyrophosphatase (inorganic) 1, PP, PP1, IOPPP, SID6-8061, Pyrophosphate phospho-hydrolase, PPase, cytosolic inorganic pyrophosphatase, diphosphate phosphohydrolase, inorganic diphosphatase, EC 3.6.1.1.

    Product # :

    ENZ-241

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    Description

    PPA1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 313 amino acids (1-289) and having a molecular mass of 35.2kDa.PPA1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PPA1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPA1 is a member of the PPase family. PPA1 catalyzes the conversion of one molecule of pyrophosphate to two phosphate ions. Many biochemical pathways use the hydrolysis of PPi to two phosphate ions to make the reactions permanently irreversible. A prominent illustration of this phenomenon is the inorganic pyrophosphatase catalyzation in the hydrolysis reaction at the beginning of lipid degradation. Inorganic pyrophosphatase provides the motivation for the activation of fatty acids destined for oxidation by stimulating the rapid hydrolysis of pyrophosphate.

    • Synonyms

      Pyrophosphatase (inorganic) 1, PP, PP1, IOPPP, SID6-8061, Pyrophosphate phospho-hydrolase, PPase, cytosolic inorganic pyrophosphatase, diphosphate phosphohydrolase, inorganic diphosphatase, EC 3.6.1.1.

    • 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 MGSHMSGFST EERAAPFSLE YRVFLKNEKG QYISPFHDIP IYADKDVFHM VVEVPRWSNA KMEIATKDPL NPIKQDVKKG KLRYVANLFP YKGYIWNYGA IPQTWEDPGH NDKHTGCCGD NDPIDVCEIG SKVCARGEII GVKVLGILAM IDEGETDWKV IAINVDDPDA ANYNDINDVK RLKPGYLEAT VDWFRRYKVP DGKPENEFAF NAEFKDKDFA IDIIKSTHDH WKALVTKKTN GKGISCMNTT LSESPFKCDP DAARAIVDAL PPPCESACTV PTDVDKWFHH QKN.

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    Ppa1 Human
  • View Data Sheet

    Name :

    GPT Rat

    Description:

    Glutamic-Pyruvate Transaminase Rat Recombinant

    Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.

    Product # :

    ENZ-918

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    Description

    GPT Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 57.5kDa. GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    GPT protein solution (1mg/ml) 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 > 60units/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

      Alanine aminotransferase 1 (EC:2.6.1.2), ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, Gpt, Aat1, Gpt1.

    • 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 MGSMASRVND QSQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVSGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFKEGL FLMADEVYQD NVYAEGSQFH SFKKVLMEMG PPYSTQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMGKLMSVR LCPPVPGQAL MDMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ VQLPLKAVQR AQELGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RLLLEKLSHF HAKFTHEYS.

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    Gpt Rat
  • View Data Sheet

    Name :

    RNASE2 Human

    Description:

    Ribonuclease 2 Human Recombinant

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

    Product # :

    ENZ-1175

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Rnase2 Human
  • View Data Sheet

    Name :

    LCAT Human, HEK

    Description:

    Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK

    Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    Product # :

    ENZ-254

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    Description

    LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.

    Source

    Human Embryonic Kidney 293 cells

    Formulation

    The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.

    • Synonyms

      Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT 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

      Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE

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    Lcat Human Hek
  • View Data Sheet

    Name :

    HBsAg adw

    Description:

    Hepatitis B Surface Antigen, adw Recombinant

    Product # :

    HBS-872

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    Description

    HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.

    Source

    Pichia Pastoris.

    Formulation

    Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.

    • Physical Appearance

      Sterile Filtered pale solution.

    • Stability

      HBsAg Should be stored at 4°C.DO NOT FREEZE.

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    Hbsag Adw
  • View Data Sheet

    Name :

    MMP2 Mouse

    Description:

    Matrix Metalloproteinase-2 Mouse Recombinant

    72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    Product # :

    ENZ-1117

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    Description

    MMP2 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 644 amino acids (30-662 aa) and having a molecular mass of 72.4kDa.MMP2 is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MMP2 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-2 or gelatinase A, is secreted by fibroblasts, cardiomyocytes, and myofibroblasts. MMP-2 has a broad feild of substrates, that contain elastin, collagen, fibroblast growth factor, endothelin, MMP-9, plasminogen, MMP-13 and TGF-beta, pointing towards bread roles of MMP-2. MMP-2 activity boosts at day four post-MI and attains a maximum by day seven.

    • Synonyms

      72 kDa type IV collagenase, 72 kDa gelatinase, Gelatinase A, Matrix metalloproteinase-2, MMP-2, TBE-1, MMP2, CLG4A, CLG4, MONA, MMP-II.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPEFAPSPI IKFPGDVAPK TDKELAVQYL NTFYGCPKES CNLFVLKDTL KKMQKFFGLP QTGDLDQNTI ETMRKPRCGN PDVANYNFFP RKPKWDKNQI TYRIIGYTPD LDPETVDDAF ARALKVWSDV TPLRFSRIHD GEADIMINFG RWEHGDGYPF DGKDGLLAHA FAPGTGVGGD SHFDDDELWT LGEGQVVRVK YGNADGEYCK FPFLFNGREY SSCTDTGRSD GFLWCSTTYN FEKDGKYGFC PHEALFTMGG NADGQPCKFP FRFQGTSYNS CTTEGRTDGY RWCGTTEDYD RDKKYGFCPE TAMSTVGGNS EGAPCVFPFT FLGNKYESCT SAGRNDGKVW CATTTNYDDD RKWGFCPDQG YSLFLVAAHE FGHAMGLEHS QDPGALMAPI YTYTKNFRLS HDDIKGIQEL YGPSPDADTD TGTGPTPTLG PVTPEICKQD IVFDGIAQIR GEIFFFKDRF IWRTVTPRDK PTGPLLVATF WPELPEKIDA VYEAPQEEKA VFFAGNEYWV YSASTLERGY PKPLTSLGLP PDVQQVDAAF NWSKNKKTYI FAGDKFWRYN EVKKKMDPGF PKLIADSWNA IPDNLDAVVD LQGGGHSYFF KGAYYLKLEN QSLKSVKFGS IKSDWLGCHH HHHH

    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.

    Mmp2 Mouse
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