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Search results

1000 results found for “Asparaginase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    UMPS Human

    Description:

    Uridine Monophosphate Synthetase Human Recombinant

    OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

    Product # :

    ENZ-663

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    Description

    UMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 500 amino acids (1-480 a.a) and having a molecular mass of 54.3kDa.UMPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UMPS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uridine 5'-monophosphate synthase (UMPS), is a bifunctional enzyme that catalyzes the ultimate two steps of the de novo pyrimidine biosynthetic pathway. UMPS in eukaryotes links the orotate phosphoribosyltransferase and the orotidine-5’-monophosphate (OMP) decarboxylase activities into a single protein. The harmony of these 2 enzymes is assumed to be stabilized the catalytic centers as a result of the low molar concentration of the protein in mammalian cells.mutations in this gene are the reason of inherited orotic aciduria disease.

    • Synonyms

      OPRT, Uridine 5'-monophosphate synthase, UMP synthase, Orotate phosphoribosyltransferase , OPRT, OPRTase, Orotidine 5'-phosphate decarboxylase , ODC, OMPdecase.

    • 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 MAVARAALGP LVTGLYDVQA FKFGDFVLKS GLSSPIYIDL RGIVSRPRLL SQVADILFQT AQNAGISFDT VCGVPYTALP LATVICSTNQ IPMLIRRKET KDYGTKRLVE GTINPGETCL IIEDVVTSGS SVLETVEVLQ KEGLKVTDAI VLLDREQGGK DKLQAHGIRL HSVCTLSKML EILEQQKKVD AETVGRVKRF IQENVFVAAN HNGSPLSIKE APKELSFGAR AELPRIHPVA SKLLRLMQKK ETNLCLSADV SLARELLQLA DALGPSICML KTHVDILNDF TLDVMKELIT LAKCHEFLIF EDRKFADIGN TVKKQYEGGI FKIASWADLV NAHVVPGSGV VKGLQEVGLP LHRGCLLIAE MSSTGSLATG DYTRAAVRMA EEHSEFVVGF ISGSRVSMKP EFLHLTPGVQ LEAGGDNLGQ QYNSPQEVIG KRGSDIIIVG RGIISAADRL EAAEMYRKAA WEAYLSRLGV.

    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.

    Umps Human
  • View Data Sheet

    Name :

    CMBL Human

    Description:

    Carboxymethylenebutenolidase Human Recombinant

    Carboxymethylenebutenolidase homolog, CMBL, JS-1.

    Product # :

    ENZ-634

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      Carboxymethylenebutenolidase homolog, CMBL, JS-1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Cmbl Human
  • View Data Sheet

    Name :

    GSTK1 Human

    Description:

    Glutathione S-Transferase Kappa 1 Human Recombinant

    GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    Product # :

    ENZ-476

    Price :

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    • More Info

    Description

    GSTK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (1-226 a.a.) and having a molecular mass of 25.5 kDa. GSTK1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GSTK1 solution containing 20mM Tris pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GSTK1 is involved in cellular detoxification. GSTK1 is localized to the peroxisome and catalyzes the conjugation of the thiol group of glutathione (GSH) to the electrophilic groups of a broad range of hydrophobic substrates, leading to an easier removal of the latter from the cells.

    • Synonyms

      GST13, GST13-13, GSTK1-1, GST class-kappa, EC 2.5.1.18, Glutathione S-transferase kappa 1, Glutathione S-transferase subunit 13, hGSTK1, GSTK1.

    • 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

      MGPLPRTVEL FYDVLSPYSW LGFEILCRYQ NIWNINLQLR PSLITGIMKD SGNKPPGLLP RKGLYMANDL KLLRHHLQIP IHFPKDFLSV MLEKGSLSAM RFLTAVNLEH PEMLEKASRE LWMRVWSRNE DITEPQSILA AAEKAGMSAE QAQGLLEKIA TPKVKNQLKE TTEAACRYGA FGLPITVAHV DGQTHMLFGS DRMELLAHLL GEKWMGPIPP AVNARL.

    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.

    Gstk1 Human
  • 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

    Price :

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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 :

    METTL21A Human

    Description:

    Methyltransferase Like 21A Human Recombinant

    Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.

    Product # :

    ENZ-718

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    Description

    METTL21A Human Recombinant produced in E. coli is a single polypeptide chain containing 149 amino acids (93-218) and having a molecular mass of 17 kDa.METTL21A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The METTL21A solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      METTL21A, which is a part of the methyltransferase superfamily, is a Protein-lysine methyltransferase that in vitro methylates HSPA1, HSPA5 and HSPA8.

    • Synonyms

      Protein N-lysine methyltransferase METTL21A, HSPA lysine methyltransferase, HSPA-KMT, Hepatocellular carcinoma-associated antigen 557b, Methyltransferase-like protein 21A, METTL21A, FAM119A, HCA557B, Methyltransferase Like 21A.

    • 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 MGSTDRKVAL EFLKSNVQAN LPPHIQTKTV VKELTWGQNL GSFSPGEFDL ILGADIIYLE ETFTDLLQTL EHLCSNHSVI LLACRIRYER DNNFLAMLER QFTVRKVHYD PEKDVHIYEA QKRNQKEDL.

    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.

    Mettl21A Human
  • View Data Sheet

    Name :

    ACY1 Mouse

    Description:

    AminoAcylase-1 Mouse Recombinant

    Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

    Product # :

    ENZ-905

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    Description

    ACY1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-408 a.a) and having a molecular mass of 48.4kDa. ACY1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACY1 protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Acy1 or Aminoacylase1 is a cytosolic, homodimeric, zinc-binding enzyme which catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been suggested to operate in the catabolism and salvage of acylated amino acids. ACY1 is localized in chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been observed to be reduced or undetectable in SCLC cell lines and tumors.

    • Synonyms

      Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, Aminoacylase 1, Acy1.

    • 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 MGSEFMTTKD PESEHPSVTL FRQYLRICTV QPNPDYGGAI TFLEERARQL GLSCQKIEVV PGFVITVLTW PGTNPSLPSI LLNSHTDVVP VFKEHWHHDP FEAFKDSEGY IYARGSQDMK SVSIQYLEAV RRLKSEGHRF PRTIHMTFVP DEEVGGHKGM ELFVKRPEFQ ALRAGFALDE GLANPTDAFT VFYSERSPWW VRVTSTGKPG HASRFIEDTA AEKLHKVISS ILAFREKERQ RLQANPHLKE GAVTSVNLTK LEGGVAYNVV PATMSASFDF RVAPDVDMKA FEKQLQRWCQ EAGEGVTFEF AQKFTEPRMT PTDDSDPWWA AFSGACKAMN LTLEPEIFPA ATDSRYIRAV GIPALGFSPM NRTPVLLHDH NERLHEDIFL RGVDIYTGLL SALASVPTLP GES.

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    Acy1 Mouse
  • View Data Sheet

    Name :

    CASP3 Human, Sf9

    Description:

    Caspase 3 Apoptosis-Related Cysteine Peptidase Human Recombinant, Sf9

    CASP3, CPP32, CPP32B, SCA-1, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1.

    Product # :

    ENZ-1106

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    Description

    CASP3 Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (29-277 a.a.) and having a molecular mass of 29.4kDa (Migrates at 13.5-18kDa on SDS-PAGE under reducing conditions). CASP3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CASP3 protein solution (0.5mg/ml) containing 20mM HEPES buffer (pH 7.5), 0.1M NaCl, 1mM EDTA, 20% Glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is  greater than 5,000 pmol/min/ug. One unit will liberate 1 pmoles of Ac-DEVD-AFC to Ac-DEVD and AFC per minute at pH7.5 at 25C.

    More Info

    • Introduction

      Caspase 3 Apoptosis-Related Cysteine Peptidase (CASP3) belongs to the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a key role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to generate 2 subunits, large and small, that dimerize to create the active enzyme. CASP3 protein cleaves and activates caspases 6, 7 and 9, and the protein itself is processed by caspases 8, 9 and 10. CASP3 is the leading caspase involved in the cleavage of amyloid-beta 4A precursor protein, which is linked with neuronal death in Alzheimer's disease. In addition, CASP3 is involved in the cleavage of huntingtin. CASP3 also cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. CASP3 initiates cell adhesion in sympathetic neurons through RET cleavage.

    • Synonyms

      CASP3, CPP32, CPP32B, SCA-1, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 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

      MSGISLDNSY KMDYPEMGLC IIINNKNFHK STGMTSRSGT DVDAANLRET FRNLKYEVRN
      KNDLTREEIV ELMRDVSKED HSKRSSFVCV LLSHGEEGII FGTNGPVDLK KITNFFRGDR
      CRSLTGKPKL FIIQACRGTE LDCGIETDSG VDDDMACHKI PVEADFLYAY STAPGYYSWR
      NSKDGSWFIQ SLCAMLKQYA DKLEFMHILT RVNRKVATEF ESFSFDATFH AKKQIPCIVS MLTKELYFYH HHHHHH

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    Caspase 3 Protein
  • View Data Sheet

    Name :

    CA1 E.Coli

    Description:

    Carbonic Anhydrase-1 E.Coli Recombinant

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

    Product # :

    ENZ-1138

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Ca1 Protein
  • View Data Sheet

    Name :

    MMP1 Human, sf9

    Description:

    Matrix Metalloproteinase-1 Human Recombinant, sf9

    Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1.

    Product # :

    ENZ-989

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    Description

    MMP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 460 amino acids (18-469a.a) and having a molecular mass of 53.1kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). MMP1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MMP1 protein solution (0.25mg/ml) containing 20mM MES buffer (pH 5.5), 10mM CaCl2, 100 mM NaCl, 0.05% Brij35 and 30% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) 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

      Matrix Metallopeptidase 1, Interstitial Collagenase, Fibroblast Collagenase, EC 3.4.24.7, CLG, Matrix Metalloproteinase 1 (Interstitial Collagenase), Matrix Metallopeptidase 1 (Interstitial Collagenase), Matrix Metalloproteinase 1, Matrix Metalloproteinase-1, Matrix Metalloprotease 1, EC 3.4.24, MMP-1, CLGN, Fibroblast collagenase, 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

      HSFPATLETQ EQDVDLVQKY LEKYYNLKND GRQVEKRRNS GPVVEKLKQM QEFFGLKVTG KPDAETLKVM KQPRCGVPDV AQFVLTEGNP RWEQTHLTYR IENYTPDLPR ADVDHAIEKA FQLWSNVTPL TFTKVSEGQA DIMISFVRGD HRDNSPFDGP GGNLAHAFQP GPGIGGDAHF DEDERWTNNF REYNLHRVAA HELGHSLGLS HSTDIGALMY PSYTFSGDVQ LAQDDIDGIQ AIYGRSQNPV QPIGPQTPKA CDSKLTFDAI TTIRGEVMFF KDRFYMRTNP FYPEVELNFI SVFWPQLPNG LEAAYEFADR DEVRFFKGNK YWAVQGQNVL HGYPKDIYSS FGFPRTVKHI DAALSEENTG KTYFFVANKY WRYDEYKRSM DPGYPKMIAH DFPGIGHKVD AVFMKDGFFY FFHGTRQYKF DPKTKRILTL QKANSWFNCR KNLEHHHHHH.

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    Mmp1 Human Sf9
  • View Data Sheet

    Name :

    RPIA Human

    Description:

    Ribose 5-Phosphate Isomerase A Human Recombinant

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

    Product # :

    ENZ-228

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Rpia Human
  • View Data Sheet

    Name :

    ACKA E.Coli

    Description:

    Acetate Kinase E.Coli Recombinant

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

    Product # :

    PKA-063

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Acka Ecoli
  • View Data Sheet

    Name :

    GDA Human, His

    Description:

    Guanine Deaminase Human Recombinant, His Tag

    CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    Product # :

    ENZ-682

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    Description

    GDA Human Recombinant produced in E. coli is a single polypeptide chain containing 477 amino acids (1-454) and having a molecular mass of 53kDa. GDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      GDA is a member of the ATZ/TRZ family and is in charge for the hydrolytic deamination of guanine. GDA takes part in microtubule assembly. Multiple transcript variants encoding different isoforms have been found for GDA.

    • Synonyms

      CYPIN, GUANASE, NEDASIN, Guanine aminase, Guanine aminohydrolase, GAH, p51-nedasin.

    • 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 MGSMCAAQMP PLAHIFRGTF VHSTWTCPME VLRDHLLGVS DSGKIVFLEE ASQQEKLAKE WCFKPCEIRE LSHHEFFMPG LVDTHIHASQ YSFAGSSIDL PLLEWLTKYT FPAEHRFQNI DFAEEVYTRV VRRTLKNGTT TACYFATIHT DSSLLLADIT DKFGQRAFVG KVCMDLNDTF PEYKETTEES IKETERFVSE MLQKNYSRVK PIVTPRFSLS CSETLMGELG NIAKTRDLHI QSHISENRDE VEAVKNLYPS YKNYTSVYDK NNLLTNKTVM AHGCYLSAEE LNVFHERGAS IAHCPNSNLS LSSGFLNVLE VLKHEVKIGL GTDVAGGYSY SMLDAIRRAV MVSNILLINK VNEKSLTLKE VFRLATLGGS QALGLDGEIG NFEVGKEFDA ILINPKASDS PIDLFYGDFF GDISEAVIQK FLYLGDDRNI EEVYVGGKQV VPFSSSV.

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    Gda Human
  • View Data Sheet

    Name :

    PNPO Human

    Description:

    Pyridoxamine 5'-Phosphate Oxidase Human Recombinant

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

    Product # :

    ENZ-030

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Pnpo Human
  • View Data Sheet

    Name :

    HPRT1 Human

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase Human Recombinant

    Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    Product # :

    ENZ-524

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    Description

    HPRT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 26.7 kDa. The HPRT1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPRT1 Human solution containing 20mM Tris HCl pH-8, & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine-Guanine Phosphoribosyltransferase , EC 2.4.2.8, HGPRT, HGPRTase, HPRT, HPRT1.

    • 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 MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKV ASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA.

    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.

    Hprt1 Human
  • View Data Sheet

    Name :

    PCYT2 Human

    Description:

    Phosphate Cytidylyltransferase 2 Human Recombinant

    MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.

    Product # :

    ENZ-221

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    Description

    PCYT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-389) and having a molecular mass of 45.9kDa.PCYT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCYT2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCYT2 is a member of the cytidylyltransferase family. PCYT2 is an enzyme which catalyzes the formation of CDP-MEA from CTP and phospho MEA in the Kennedy pathway of phospholipid synthesis. PCYT2 has the strongest expression in the liver, heart, and skeletal muscle.

    • Synonyms

      MEA-phosphate cytidylyltransferase, CTP:phospho MEA cytidylyltransferase, Phosphoryl MEA transferase, PCYT2, ET.

    • 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 MIRNGRGAAG GAEQPGPGGR RAVRVWCDGC YDMVHYGHSN QLRQARAMGD YLIVGVHTDE EIAKHKGPPV FTQEERYKMV QAIKWVDEVV PAAPYVTTLE TLDKYNCDFC VHGNDITLTV DGRDTYEEVK QAGRYRECKR TQGVSTTDLV GRMLLVTKAH HSSQEMSSEY REYADSFGKC PGGRNPWTGV SQFLQTSQKI IQFASGKEPQ PGETVIYVAG AFDLFHIGHV DFLEKVHRLA ERPYIIAGLH FDQEVNHYKG KNYPIMNLHE RTLSVLACRY VSEVVIGAPY AVTAELLSHF KVDLVCHGKT EIIPDRDGSD PYQEPKRRGI FRQIDSGSNL TTDLIVQRII TNRLEYEARN QKKEAKELAF LEAARQQAAQ PLGERDGDF.

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    Pcyt2 Human
  • View Data Sheet

    Name :

    PRCP Human

    Description:

    Prolylcarboxypeptidase Human Recombinant

    Angiotensinase-C, PRCP, Proline Carboxypeptidase.

    Product # :

    ENZ-1178

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    Description

    PRCP Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (22-496 a.a) containing a total of 481 amino acids, having a molecular mass of 54.3 kDa. PRCP is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The PRCP solution (0.25mg/ml) contains 30% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 3,000 pmol/min/μg, and is defined as the amount of enzyme that converts 1pmole of Z-ProAla-OH/min. at pH-4 at 25˚C.

    More Info

    • Introduction

      PRCP is a plasma protein which takes part in the cleavage of C-terminal amino acids linked to proline in proteinfor example angiotensin-2 & 3 at acidic pHenvironment rather than at neutral pHwhich exhibit less activity. This cleavage is important since Angiotensin-2 takes part in regulation of blood pressure & electrolyte balance which is essential to hypertension.

    • Synonyms

      Angiotensinase-C, PRCP, Proline Carboxypeptidase.

    • 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

      LRPALRALGS LHLPTNPTSL PAVAKNYSVL YFQQKVDHFG FNTVKTFNQR YLVADKYWKK NGGSILFYTG NEGDIIWFCN NTGFMWDVAE ELKAMLVFAE HRYYGESLPF GDNSFKDSRH LNFLTSEQAL ADFAELIKHL KRTIPGAENQ PVIAIGGSYG GMLAAWFRMK YPHMVVGALA ASAPIWQFED LVPCGVFMKI VTTDFRKSGP HCSESIHRSW DAINRLSNTG SGLQWLTGALHLCSPLTSQD IQHLKDWISE TWVNLAMVDY PYASNFLQPL PAWPIKVVCQ YLKNPNVSDS LLLQNIFQAL NVYYNYSGQV KCLNISETAT SSLGTLGWSY QACTEVVMPF CTNGVDDMFE PHSWNLKELS DDCFQQWGVR PRPSWITTMY GGKNISSHTN IVFSNGELDP WSGGGVTKDI TDTLVAVTIS EGAHHLDLRT KNALDPMSVL LARSLEVRHM KNWIRDFYDS AGKQ HHHHHH

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    Prcp Human
  • View Data Sheet

    Name :

    ACP1 Human

    Description:

    Acid Phosphatase-1 Human Recombinant

    HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.

    Product # :

    ENZ-408

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    Description

    Recombinant Human ACP1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 178 amino acids (1-158 a.a.) and having a molecular mass of 20.1 kDa. ACP1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACP1 protein solution contains 20mM MES, pH-6, 0.1mM PMSF, 2mM EDTA and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACP1 is part of the phosphotyrosine protein. ACP1 functions as an acid phosphatase and a protein tyrosine phosphatase (PTPase) existing in all human tissues, including adipocytes. ACP1 enzyme hydrolyzes protein tyrosine phosphate to protein tyrosine and orthophosphate, and also orthophosphoric monoesters to alcohol and orthophosphate. ACP1 is present in adipocytes, thus playing a specific role in the regulation of adipose tissue. High levels of the ACP1 negatively regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. High significant differences in birth weight-placental weight relationships were observed among acid phosphatase locus 1 phenotypes.

    • Synonyms

      HAAP, MGC3499, MGC111030, ACP1, Low molecular weight phosphotyrosine protein phosphatase, LMW-PTPase, LMW-PTP, Low molecular weight cytosolic acid phosphatase, Red cell acid phosphatase 1, Adipocyte acid phosphatase.

    • 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 MAEQATKSVL FVCLGNICRS PIAEAVFRKL VTDQNISENW VIDSGAVSDW NVGRSPDPRA VSCLRNHGIHTAHKARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKTC KAKIELLGSY DPQKQLIIED PYYGNDSDFE TVYQQCVRCC RAFLEKAH.

    • Unit Definition

      One unit is defined as the amount of enzyme that will hydrolyze 1nmole of p-nitrophenyl phosphate per minute at 37°C in MES pH5.0 using 10mM of substrate.

    • Specific Activity

      > 15,000 Units per 1mg protein.

    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.

    Acp1 Human
  • View Data Sheet

    Name :

    NUDT10 Human

    Description:

    Nudix Type Motif 10 Human Recombinant

    Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.

    Product # :

    ENZ-126

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    Description

    NUDT10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-164 a.a.) and having a molecular mass of 19.5kDa.NUDT10 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NUDT10 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.

    • Synonyms

      Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      NUDT10 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDPLEHHHH HH.

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    Nudt10 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 :

    UNG

    Description:

    Uracil DNA Glycosilase

    Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.

    Product # :

    ENZ-352

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    Description

    E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).

    Source

    Escherichia Coli strain that carries the UNG gene from E.coli.

    Formulation

    UNG solution in 10mM Tris-HCl (pH-7.4 at 25°C), 50mM KCl, 1mM DTT, 0.1mM EDTA, 0.1 mg/ml BSA and 50% glycerol.

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    • Synonyms

      Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Uracil DNA Glycosilase although stable at 15°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.

    • Reaction Conditions

      1X UNG Reaction Buffer, incubate at 37°C.UNG is active over a broad pH rabge with an optimum at pH-8.0, doesn't require divalent cation, and is inhibited by high ionic strength (>200mM). The abasic sites formed in DNA by UNG may be cleaved by heat, alkali-treatment or endonucleases that cleave specifically at abasic sites.

    • Inactivation

      Inactivated by heating at 95°C for 10min. Enzyme activity is partially restored at temperatures lower than 55°C.

    • Unit Definition

      1 Unit of the enzyme catalyzes the release of 1 nanomole of uracil-containing DNA template in 60 min at 37°C.

    • Specific Activity

      The Specific Activity was found to be 5U/µl.

    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.

    Uracil Dna Glycosylase 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 :

    HPRT1 Human, Active

    Description:

    Hypoxanthine-Guanine Phosphoribosyltransferase, Human Recombinant, Active

    Hypoxanthine Phosphoribosyltransferase 1, EC 2.4.2.8, HGPRTase, HGPRT, HPRT , Hypoxanthine-Guanine Phosphoribosyltransferase 1, Hypoxanthine-Guanine Phosphoribosyltransferase, Testicular Tissue Protein Li 89, Lesch-Nyhan Syndrome, HPRT1.

    Product # :

    ENZ-1006

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    Description

    HPRT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 238 amino acids (1-218 a.a) and having a molecular mass of 26.7kDa. HPRT1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HPRT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 15 units/mg and is defined as the amount of enzyme that catalyze the formation of 1 umole of guanosine 5’-monophosphate (GMP) per minute from guanine and phosphoribosyl pyrophosphate at pH 7.5 at 37C.

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    • Introduction

      HPRT1 has a main part in the generation of purine nucleotides through the purine salvage pathway. HPRT1 primarily functions to salvage purines from degraded DNA to renewed purine synthesis. Therefore, it performs as a catalyst in the reaction between guanine and phosphoribosyl pyrophosphate to form GMP.

    • Synonyms

      Hypoxanthine Phosphoribosyltransferase 1, EC 2.4.2.8, HGPRTase, HGPRT, HPRT , Hypoxanthine-Guanine Phosphoribosyltransferase 1, Hypoxanthine-Guanine Phosphoribosyltransferase, Testicular Tissue Protein Li 89, Lesch-Nyhan Syndrome, HPRT1.

    • 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 MATRSPGVVI SDDEPGYDLD LFCIPNHYAE DLERVFIPHG LIMDRTERLA RDVMKEMGGH HIVALCVLKG GYKFFADLLD YIKALNRNSD RSIPMTVDFI RLKSYCNDQS TGDIKVIGGD DLSTLTGKNV LIVEDIIDTG KTMQTLLSLV RQYNPKMVKVASLLVKRTPR SVGYKPDFVG FEIPDKFVVG YALDYNEYFR DLNHVCVISE TGKAKYKA

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    Hprt1 Human Active
  • View Data Sheet

    Name :

    OTC Human

    Description:

    Ornithine Carbamoyltransferase Human Recombinant

    Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    Product # :

    ENZ-596

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    Description

    OTC Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (33-354) and having a molecular mass of 38.9kDa.OTC is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The OTC solution (0.5mg/ml) contains 20mM MES buffer (pH 6.0), 100mM Nacl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      OTC is a member of the ATCase/OTCase family. OTC has a key part in the urea cycle, catalyzing the second step in this pathway: the transformation of L-orthinine and carbamoyl phosphate to L-citrulline. In humans, the urea cycle is a vital pathway to detoxification of ammonia. Alterations in the gene encoding OTC are linked to the X-linked disorder OTCD (ornithine carbamoyltransferase deficiency). OTCD disorder of the urea cycle is characterized by hyperammonemia.

    • Synonyms

      Ornithine carbamoyltransferase mitochondrial, Ornithine transcarbamylase, OTCase, OCTD, EC 2.1.3.3.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSHMNKVQL KGRDLLTLKN FTGEEIKYML WLSADLKFRI KQKGEYLPLL QGKSLGMIFE KRSTRTRLST ETGFALLGGH PCFLTTQDIH LGVNESLTDT ARVLSSMADA VLARVYKQSD LDTLAKEASI PIINGLSDLY HPIQILADYL TLQEHYSSLK GLTLSWIGDG NNILHSIMMS AAKFGMHLQA ATPKGYEPDA SVTKLAEQYA KENGTKLLLT NDPLEAAHGG NVLITDTWIS MGQEEEKKKR LQAFQGYQVT MKTAKVAASD WTFLHCLPRK PEEVDDEVFY SPRSLVFPEA ENRKWTIMAV MVSLLTDYSP QLQKPKF.

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    Otc Human
  • View Data Sheet

    Name :

    CHST10 Human

    Description:

    Carbohydrate Sulfotransferase 10 Human Recombinant

    Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    Product # :

    ENZ-894

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    Description

    CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.

    • Synonyms

      Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.

    • 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 MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.

    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.

    Chst10 Human
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