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Search results

1000 results found for “Epimerase”

Name

Description

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  • View Data Sheet

    Name :

    ENO1 Human

    Description:

    Enolase-1 Human Recombinant

    NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    Product # :

    ENZ-452

    Price :

    Quantity :

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    • description
    • source
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    • More Info

    Description

    The ENO1 Human Recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 47.1kDa and containing 434 amino acids (1-434 a.a.).

    Source

    Escherichia Coli.

    Formulation

    The ENO1 protein solution (1mg/ml) is formulated in 20mM Tris-HCl pH-7.5 1mM MgSO4 and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20,000pmol/min/ug, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    More Info

    • Introduction

      ENO1 is a homodimeric soluble protein that encodes a smaller monomeric structural lens protein, tau-crystallin. ENO1 is a glycolytic enzyme expressed in mainly all tissues. ENO1 isoenzyme full length protein is found in the cytoplasm. The shorter protein is formed from another translation start that is restricted to the nucleus, and binds to a component in the c-myc promoter. ENO1 is involved in anaerobic metabolism under hypoxic conditions and plays a role as a cell surface plasminogen receptor during tissue invasion. Irregular expression of Enolase-1 is linked with tumor progression in several cases of breast and lung cancer. Enolase-1 is as an auto antigen associated with Hashimoto's encephalopathy and severe asthma. ENO1 is the target protein of serum anti-endothelial antibody in Behcet's disease.

    • Synonyms

      NNE, PPH, MPB1, MBP-1, ENO1L1, ENO1, Alpha-Enolase, Enolase-Alpha, 2-phospho-D-glycerate hydro-lyase, Non-neural enolase, Enolase 1, MPB-1, Phosphopyruvate hydratase, C-myc promoter-binding protein, Plasminogen-binding protein, MBPB1.

    • 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

      MSILKIHARE IFDSRGNPTV EVDLFTSKGL FRAAVPSGAS TGIYEALELR DNDKTRYMGK GVSKAVEHIN KTIAPALVSK KLNVTEQEKI DKLMIEMDGT ENKSKFGANA ILGVSLAVCK AGAVEKGVPL YRHIADLAGN SEVILPVPAF NVINGGSHAG NKLAMQEFMI LPVGAANFRE AMRIGAEVYH NLKNVIKEKY GKDATNVGDE GGFAPNILEN KEGLELLKTA IGKAGYTDKV VIGMDVAASE FFRSGKYDLD FKSPDDPSRY ISPDQLADLY KSFIKDYPVV SIEDPFDQDD WGAWQKFTAS AGIQVVGDDL TVTNPKRIAK AVNEKSCNCL LLKVNQIGSV TESLQACKLA QANGWGVMVS HRSGETEDTF IADLVVGLCT GQIKTGAPCR SERLAKYNQL LRIEEELGSK AKFAGRNFRN PLAK.

    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.

    Eno1 Human
  • View Data Sheet

    Name :

    SRM Human

    Description:

    Spermidine Synthase Human Recombinant

    Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    Product # :

    ENZ-027

    Price :

    Quantity :

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    • description
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    Description

    SRM 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 322 amino acids (1-302 a.a.) and having a molecular mass of 36kDa. The SRM is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRM solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SRM is an enzyme which catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The polyamines putrescine, spermine and spermidine are ubiquitous polycationic mediators of cell growth and differentiation. The SRM protein is one of four enzymes in the polyamine-biosynthetic pathway and completes the final step of spermidine biosynthesis.

    • Synonyms

      Spermidine synthase, SPDSY, Putrescine aminopropyltransferase, SRM, SPS1, SRML1, PAPT.

    • 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 MEPGPDGPAA SGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV VQCEIDEDVI QVSKKFLPGM AIGYSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP AESLFKESYY QLMKTALKED GVLCCQGECQ WLHLDLIKEM RQFCQSLFPV VAYAYCTIPT YPSGQIGFML CSKNPSTNFQ EPVQPLTQQQ VAQMQLKYYN SDVHRAAFVL PEFARKALND VS.

    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.

    Srm Human
  • View Data Sheet

    Name :

    REXO2 Human

    Description:

    RNA Exonuclease 2 Human Recombinant

    REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    Product # :

    ENZ-715

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    REXO2 Human Recombinant produced in E. coli is a single polypeptide chain containing 235 amino acids (26-237) and having a molecular mass of 26.8kDa. REXO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The REXO2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      EXO2 is a 3'-to-5' exonuclease specific for small (primarily 5 nucleotides or less in length) single-stranded RNA and DNA oligomers. RNA Exonuclease 2 (REXO2) takes part in DNA repair, replication, and recombination, and in RNA processing and degradation. EXO2 is involved in resistance of human cells to UV-C-induced cell death via its part in the DNA repair process.

    • Synonyms

      REX2, RNA exonuclease 2 homolog (S. cerevisiae), CGI-114, RFN, SFN, Oligoribonuclease, mitochondrial, RNA exonuclease 2 homolog, Small fragment nuclease,REXO2, SMFN.

    • 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 MGSVREGGAA MAAGESMAQR MVWVDLEMTG LDIEKDQIIE MACLITDSDL NILAEGPNLI IKQPDELLDS MSDWCKEHHG KSGLTKAVKE STITLQQAEY EFLSFVRQQT PPGLCPLAGN SVHEDKKFLD KYMPQFMKHL HYRIIDVSTV KELCRRWYPE EYEFAPKKAA SHRALDDISE SIKELQFYRN NIFKKKIDEK KRKIIENGEN EKTVS.

    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.

    Rexo2 Human
  • View Data Sheet

    Name :

    XYLT2 Human

    Description:

    Xylosyltransferase 2 Human Recombinant

    Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    Product # :

    ENZ-1086

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

    Add To Cart

    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    XYLT2 Human Recombinant is a single, glycosylated polypeptide chain containing 839 amino acids (Gly37-Arg865, luminal domain, isoform 1, natural variant with Thr305) and having a molecular mass of 94.0kDa. XYLT2 is fused to an N-terminal linker (2 extra a.a), C-terminal linker (2 extra a.a) and C-terminal His-tag (6 extra a.a).

    Source

    HEK293 Cells.

    Formulation

    XYLT2 filtered (0.4 µm) and lyophilized in 0.05 M PBS and 0.075 M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      XYLT2 or Xylosyltransferase 2 is an enzyme which is expressed in ubiquitous and is part of the glycosyltransfe-rases family. XYLT2 promotes proteoglycans formation by attaching GAG chains to the substrate protein via transfer of xylose molecule from the donor (nucleoside diphosphate) to the protein’s serine residues. XYLT2 is present in the ER and the cis part of the Golgi, furthermore the protein is released to the extracellular matrix.

    • Synonyms

      Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. XYLT2 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ASGLEEDEAG EKGRQRKPRP LDPGEGSKDT DSSAGRRGST GRRHGRWRGR AESPGVPVAK VVRAVTSRQR ASRRVPPAPP PEAPGRQNLS GAAAGEALVG AAGFPPHGDT GSVEGAPQPT DNGFTPKCEI VGKDALSALA RASTKQCQQE IANVVCLHQA GSLMPKAVPR HCQLTGKMSP GIQWDESQAQ QPMDGPPVRI AYMLVVHGRA IRQLKRLLKA VYHEQHFFYI HVDKRSDYLH REVVELAQGY DNVRVTPWRM VTIWGGASLL TMYLRSMRDL LEVPGWAWDF FINLSATDYP TRTNEELVAF LSKNRDKNFL KSHGRDNSRF IKKQGLDRLF HECDSHMWRL GERQIPAGIV VDGGSDWFVL TRSFVEYVVY TDDPLVAQLR QFYTYTLLPA ESFFHTVLEN SLACETLVDN NLRVTNWNRK LGCKCQYKHI VDWCGCSPND FKPQDFLRLQ QVSRPTFFAR KFESTVNQEV LEILDFHLYG SYPPGTPALK AYWENTYDAA DGPSGLSDVM LTAYTAFARL SLHHAATAAP PMGTPLCRFE PRGLPSSVHL YFYDDHFQGY LVTQAVQPSA QGPAETLEMW LMPQGSLKLL GRSDQASRLQ SLEVGTDWDP KERLFRNFGG LLGPLDEPVA VQRWARGPNL TATVVWIDPT YVVATSYDIT VDTETEVTQY KPPLSRPLRP GPWTVRLLQF WEPLGETRFL VLPLTFNRKL PLRKDDASWL HAGPPHNEYM EQSFQGLSSI LNLPQPELAE EAAQRHTQLT GPALEAWTDR ELSSFWSVAG LCAIGPSPCP SLEPCRLTSW SSLSPDPKSE LGPVKADGRL RKLHHHHHH.

    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.

    Xylt2 Human
  • View Data Sheet

    Name :

    UBE2L3 Human His

    Description:

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant, His Tag

    Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    Product # :

    ENZ-344

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    Description

    Ubiquitin-Conjugating Enzyme E2L 3 Human Recombinant produced in E.coli is an 18.9 kDa protein containing 162 amino acids.The UBE2L3 protein contains 6xHis tag and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.

    Purity

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

    More Info

    • Introduction

      Human Ubquitin Conjugating Enzyme 7 (UbcH7) is a class I enzyme which functions in the stress response and the control of transcription factors. The enzyme is ubiquitously expressed with high levels of expression seen in adult muscle. UbcH7 mediates the selective degradation of short-lived and abnormal proteins and is highly homologous to UbcH5. It has been demonstrated to participate in the ubiquitinylation of p53, c-Fos and NF-?B. UbcH7 is one of two E2s (UbcH5 being the other) with which HECT domain proteins interact with UbcH7 being able to efficiently substitute for UbcH5 in E6-AP-dependent ubiquitinylation.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 L3, EC 6.3.2.19, Ubiquitin-protein ligase L3,Ubiquitin carrier protein L3, UbcH7, E2-F1, L-UBC, UbcM4.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Lyophilized UBE2L3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2L3 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized UBE2L3 in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHHHHHHAMAASRRLMKELEEIRKCGMKNFRNIQVDEANLLTWQGLIVP
      DNPPYDKGAFRIEINFPAEYPFKPPKITFKTKIYHPNIDEKGQVCLPVISAEN
      WKPATKTDQVIQSLIALVNDPQPEHPLRADLAEEYSKDRKKFCKNAEEFT
      KKYGEKRPVD.

    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.

    Ube2L3 Human His
  • View Data Sheet

    Name :

    ARG1 Human, Active

    Description:

    Arginase-1, Active Human Recombinant

    Arginase-1 liver, Arginase-1, liver, Arginase-1, liver A I, Al, ARG 1, ARG1, Arginase 1, Arginase liver, Arginase type I, Arginase1, Liver type arginase, Type I arginase.

    Product # :

    ENZ-1120

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    Description

    ARG1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids ( 1-322aa ) and having a molecular mass of 35.8 kDa. ARG1 is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARG1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) containing 20% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of arginine to urea per minute at pH 10.5 at 37C.

    More Info

    • Introduction

      Arginase-1 is part of the urea cycle, it catalyzes the hydrolysis of arginine to ornithine and urea. There are two isoforms of mammalian arginase which differ in their tissue location, subcellular localization, immunologic crossreactivity & physiologic role. Arginase-1is a cytosolic enzyme and expressed primarily in the liver tissue. Inherited deficiency in this enzyme may lead toargininemia, which is an autosomal recessive disease in which hyperammonemia is detected.

    • Synonyms

      Arginase-1 liver, Arginase-1, liver, Arginase-1, liver A I, Al, ARG 1, ARG1, Arginase 1, Arginase liver, Arginase type I, Arginase1, Liver type arginase, Type I arginase.

    • 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

      MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT LACFGLAREG NHKPIDYLNP PKLEHHHHHH.

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    Arginase 1
  • View Data Sheet

    Name :

    MSRB3 Human

    Description:

    Methionine Sulfoxide Reductase B3 Human Recombinant

    Methionine-R-sulfoxide reductase B3, MSRB3, DFNB74, FLJ36866, DKFZp686C1178.

    Product # :

    ENZ-093

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    Description

    MSRB3 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (21-185 a.a.) and having a molecular mass of 19kDa. The MSRB3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MSRB3 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionine sulfoxide reductase B3 (MSRB3) is a member of the methionine sulfoxide reductases (MSR) family proteins. MSRB3 catalyzes the reduction of methionine sulfoxide to methionine. The MSRB3 enzyme acts as a monomer and requires zinc as a cofactor. MSRs are thought to defend against reactive oxygen species-induced oxidative damage in various organs, including the most environmentally exposed organ, the human skin. MSRB3 has a vital role in cold tolerance by eliminating MetO and ROS which accumulate at the ER during cold acclimation.

    • Synonyms

      Methionine-R-sulfoxide reductase B3, MSRB3, DFNB74, FLJ36866, DKFZp686C1178.

    • 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

      MCGLPSGSCR DKKNCKVVFS QQELRKRLTP LQYHVTQEKG TESAFEGEYT HHKDPGIYKC VVCGTPLFKS ETKFDSGSGW PSFHDVINSE AITFTDDFSY GMHRVETSCS QCGAHLGHIF DDGPRPTGKR YCINSAALSF TPADSSGTAE GGSGVASPAQ ADKAELLEHH HHHH.

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    Msrb3 Human
  • View Data Sheet

    Name :

    NAT6 Human

    Description:

    N-Acetyltransferase 6 Human Recombinant

    Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

    Product # :

    ENZ-410

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    Description

    Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.

    • Synonyms

      Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.

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    Nat6 Human
  • View Data Sheet

    Name :

    ACO1 Human

    Description:

    Aconitase-1 Human Recombinant

    Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.

    Product # :

    ENZ-056

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    Description

    ACO1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 912 amino acids (1-889a.a.) and having a molecular mass of 100.8kDa.ACO1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACO1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    2mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ACO1 has a part in an iron sensor. ACO1 catalyzes the stereo-specific isomerization of citrate to isocitrate via cis-aconitate in the tricarboxylic acid cycle, a non-redox-active process.

    • Synonyms

      Onitase 1 Soluble, IRP1, IREB1, IREBP, Citrate hydro-lyase, Iron regulatory protein 1, Ferritin repressor protein, Iron-responsive element-binding protein 1, ACONS, Aconitate Hydratase, EC 4.2.1.3, Aconitase.

    • 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 MGSMSNPFAH LAEPLDPVQP GKKFFNLNKL EDSRYGRLPF SIRVLLEAAI RNCDEFLVKK QDIENILHWN VTQHKNIEVP FKPARVILQD FTGVPAVVDF AAMRDAVKKL GGDPEKINPV CPADLVIDHS IQVDFNRRAD SLQKNQDLEF ERNRERFEFL KWGSQAFHNM RIIPPGSGII HQVNLEYLAR VVFDQDGYYY PDSLVGTDSH TTMIDGLGIL GWGVGGIEAE AVMLGQPISM VLPQVIGYRL MGKPHPLVTS TDIVLTITKH LRQVGVVGKF VEFFGPGVAQ LSIADRATIA NMCPEYGATA AFFPVDEVSI TYLVQTGRDE EKLKYIKKYL QAVGMFRDFN DPSQDPDFTQ VVELDLKTVV PCCSGPKRPQ DKVAVSDMKK DFESCLGAKQ GFKGFQVAPE HHNDHKTFIY DNTEFTLAHG SVVIAAITSC TNTSNPSVML GAGLLAKKAV DAGLNVMPYI KTSLSPGSGV VTYYLQESGV MPYLSQLGFD VVGYGCMTCI GNSGPLPEPV VEAITQGDLV AVGVLSGNRN FEGRVHPNTR ANYLASPPLV IAYAIAGTIR IDFEKEPLGV NAKGQQVFLK DIWPTRDEIQ AVERQYVIPG MFKEVYQKIE TVNESWNALA TPSDKLFFWN SKSTYIKSPP FFENLTLDLQ PPKSIVDAYV LLNLGDSVTT DHISPAGNIA RNSPAARYLT NRGLTPREFN SYGSRRGNDA VMARGTFANI RLLNRFLNKQ APQTIHLPSG EILDVFDAAE RYQQAGLPLI VLAGKEYGAG SSRDWAAKGP FLLGIKAVLA ESYERIHRSN LVGMGVIPLE YLPGENADAL GLTGQERYTI IIPENLKPQM KVQVKLDTGK TFQAVMRFDT DVELTYFLNG GILNYMIRKM AK

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    Aco1 Human
  • View Data Sheet

    Name :

    ADK Mouse

    Description:

    Adenosine Kinase Mouse Recombinant

    AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    Product # :

    PKA-105

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    Description

    ADK produced in E.Coli is a single, non-glycosylated polypeptide chain containing 384 amino acids (1-361a.a.) and having a molecular mass of 42.5kDa.ADK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ADK protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-HCl buffer (pH8.0), 1mM EDTA & 50mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 pmol/min/ug and is defined as the amount of enzyme that convert 1.0 pmole of adenosine to AMP per minute at pH 7.5 at 37C in a couple system with PK and LDH. 

    More Info

    • Introduction

      Adenosine Kinase is an abundant enzyme in mammalian tissues which catalyzes the transfer of the gamma-phosphate from ATP to adenosine, thus is as a regulator of concentrations of both extracellular adenosine and intracellular adenine nucleotides. Adenosine has extensive effects on the cardiovascular, nervous, respiratory, and immune systems and inhibitors of the enzyme take a crucial pharmacological part in growing intravascular adenosine concentrations and acting as anti-inflammatory agents.

    • Synonyms

      AK, ADK, Adenosine Kinase, Adenosine 5-Phosphotransferase.

    • 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 MGSMAAADEP KPKKLKVEAP QALSENVLFG MGNPLLDISA VVDKDFLDKY SLKPNDQILA EDKHKELFDE LVKKFKVEYH AGGSTQNSMK VAQWLIQEPH KAATFFGCIG IDKFGEILKR KAADAHVDAH YYEQNEQPTG TCAACITGGN RSLVANLAAA NCYKKEKHLD LERNWVLVEK ARVYYIAGFF LTVSPESVLK VARYAAENNR VFTLNLSAPF ISQFFKEALM DVMPYVDILF GNETEAATFA REQGFETKDI KEIAKKAQAL PKVNSKRQRT VIFTQGRDDT IVAAENDVTA FPVLDQNQEE IIDTNGAGDA FVGGFLSQLV SDKPLTECIR AGHYAASVII RRTGCTFPEK PDFH.

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    Adenosine Kinase Mouse
  • View Data Sheet

    Name :

    CA12 Human

    Description:

    Carbonic Anhydrase XII Human Recombinant

    Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    Product # :

    ENZ-886

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    Description

    CA12 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 283 amino acids (25-301a.a.) and having a molecular mass of 31.94kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).CA12 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CA12 protein solution (0.5mg/ml) containing Phosphate Buffer Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 300 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.

    More Info

    • Introduction

      Carbonic anhydrase 12 (CA12) is an enzyme that belongs to the Carbonic anhydrases (CAs) family. This is a large family of zinc metalloenzymes which catalyze the reversible hydration of carbon dioxide. They are involved in various biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva, and gastric acid. CA12 is a type I membrane protein which is highly expressed in normal tissues, such as the kidney, colon and pancreas, and is overexpressed in 10% of clear cell renal carcinomas.

    • Synonyms

      Carbonic anhydrase 12, Carbonate dehydratase XII, Carbonic anhydrase XII, CA-XII, Tumor antigen HOM-RCC-3.1.3, CA12, Carbonic Anhydrase XII, Carbonic anhydrase 12 isoform 1, CAXII, HsT18816.

    • 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

      APVNGSKWTY FGPDGENSWS KKYPSCGGLL QSPIDLHSDI LQYDASLTPL EFQGYNLSAN KQFLLTNNGH SVKLNLPSDM HIQGLQSRYS ATQLHLHWGN PNDPHGSEHT VSGQHFAAEL HIVHYNSDLY PDASTASNKS EGLAVLAVLI EMGSFNPSYD KIFSHLQHVK YKGQEAFVPG FNIEELLPER TAEYYRYRGS LTTPPCNPTV LWTVFRNPVQ ISQEQLLALE TALYCTHMDD PSPREMINNF RQVQKFDERL VYTSFSQVQV CTAAGLSHHH HHH.

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    Ca12 Human
  • View Data Sheet

    Name :

    ECHS1 Human, Active

    Description:

    Enoyl CoA Hydratase, Short chain, 1, Mitochondrial, Human Recombinant, Active

    Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .

    Product # :

    ENZ-1046

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    Description

    ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a) and having a molecular mass of 30.6kDa. ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ECHS1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% Glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 umole of crotonoyl-CoA to hydroxybutyryl-CoA per minute per minute at pH 7.5 at 25°C.

    More Info

    • Introduction

      ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.

    • Synonyms

      Enoyl-CoA Hydratase, Short Chain1, Enoyl Coenzyme A Hydratase, Short Chain, 1, Mitochondrial, Enoyl-CoA Hydratase, Short Chain, 1, Mitochondrial, Short Chain Enoyl-CoA Hydratase, EC 4.2.1.17, SCEH, Enoyl-CoA Hydratase, Mitochondrial, Short-Chain Enoyl-CoA Hydratase, Enoyl-CoA Hydratase 1, EC 4.2.1, ECHS1D, ECHS1 .

    • 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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.

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    Echs1 Human Active
  • View Data Sheet

    Name :

    ACKA E.Coli

    Description:

    Acetate Kinase E.Coli Recombinant

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

    Product # :

    PKA-063

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Acka Ecoli
  • View Data Sheet

    Name :

    glpE E.Coli

    Description:

    Thiosulfate sulfurtransferase E.Coli Recombinant

    ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.

    Product # :

    ENZ-714

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    Description

    glpE Recombinant produced in E. coli is a single polypeptide chain containing 131 amino acids (1-108) and having a molecular mass of 14.5kDa. glpE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The glpE solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.

    • Synonyms

      ECK3411, JW3388, b3425, Thiosulfate sulfurtransferase GlpE.

    • 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 MGSMDQFECI NVADAHQKLQ EKEAVLVDIR DPQSFAMGHA VQAFHLTNDT LGAFMRDNDF DTPVMVMCYH GNSSKGAAQY LLQQGYDVVY SIDGGFEAWQ RQFPAEVAYG A.

    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.

    Glpe Ecoli
  • View Data Sheet

    Name :

    Phosphotransacetylase

    Description:

    Phosphotransacetylase Bacillus S. Recombinant

    Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.

    Product # :

    ENZ-1205

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    Description

    Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
    Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.

    More Info

    • Introduction

      Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
      and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

    • Synonyms

      Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE

    • Unit Definition

      1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate

    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.

    Phosphotransacetylase
  • View Data Sheet

    Name :

    GLSA1 E.Coli

    Description:

    Glutaminase 1 E.Coli Recombinant

    Glutaminase 1, ybaS.

    Product # :

    ENZ-133

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    Description

    GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa. The GLSA1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GLSA1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

    • Synonyms

      Glutaminase 1, ybaS.

    • 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 MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG

    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.

    Glsa1 Ecoli
  • View Data Sheet

    Name :

    ALDH2 Mouse

    Description:

    Aldehyde Dehydrogenase 2 Mouse Recombinant

    Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.

    Product # :

    ENZ-879

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    Description

    ALDH2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (20-519 a.a) and having a molecular mass of 56.8kDa. ALDH2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ALDH2 protein e solution (0.5mg/ml) containing Phosphate buffered salin(pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ALDH2 is part of the aldehyde dehydrogenase family of proteins which catalyze the chemical transformation from acetaldehyde to acetic acid. ALDH2 is the second enzyme of the major oxidative pathway of alcohol metabolism. ALDH2 has 2 major liver isoforms: cytosolic and mitochondrial, which differ by their electrophoretic mobilities, kinetic properties, and subcellular localizations. Nearly all Caucasians have 2 major isozymes, whereas roughly 50% of Orientals have only the cytosolic isozyme, omitting the mitochondrial isozyme. The extremely higher rate of acute alcohol intoxication with Orientals compared to Caucasians is due to the fact of the absence of mitochondrial isozyme. ALDH2 has a low Km for acetaldehydes, and is localized in mitochondrial matrix.

    • Synonyms

      Aldehyde dehydrogenase, mitochondrial, AHD-M1, ALDH class 2, ALDH-E2, ALDHI.

    • 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 MGSSAAATSA VPAPNHQPEV FCNQIFINNE WHDAVSRKTF PTVNPSTGEV ICQVAEGNKE DVDKAVKAAR AAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHE PVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGST EVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDS RTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGL AAAVFTKDLD KANYLSQALQ AGTVWINCYD VFGAQSPFGG YKMSGSGREL GEYGLQAYTE VKTVTVKVPQ KNS.

    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.

    Aldh2 Mouse
  • View Data Sheet

    Name :

    CA8 Human

    Description:

    Carbonic Anhydrase 8 Human Recombinant

    Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.

    Product # :

    ENZ-235

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    Description

    CA8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-290) and having a molecular mass of 35.5kDa.CA8 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CA8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CA8 was first called CA-related protein since there is a sequence similarity to other identified carbonic anhydrase genes. Still, this protein has no carbonic anhydrase activity - the reversible hydration of carbon dioxide. CA8 still holds a carbonic anhydrase designation due to obvious sequence similarity to other members of the carbonic anhydrase gene family. Mutations in CA8 result in cerebellar ataxia mental retardation and dysequilibrium syndrome type 3 (CMARQ3).

    • Synonyms

      Carbonic anhydrase VIII, CALS, CARP, CA-VIII, CAMRQ3, CA-related protein, carbonate dehydratase, carbonic anhydrase-like sequence, carbonic anhydrase-related protein.

    • 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 MGSHMADLSF IEDTVAFPEK EEDEEEEEEG VEWGYEEGVE WGLVFPDANG EYQSPINLNS REARYDPSLL DVRLSPNYVV CRDCEVTNDG HTIQVILKSK SVLSGGPLPQ GHEFELYEVR FHWGRENQRG SEHTVNFKAF PMELHLIHWN STLFGSIDEA VGKPHGIAII ALFVQIGKEH VGLKAVTEIL QDIQYKGKSK TIPCFNPNTL LPDPLLRDYW VYEGSLTIPP CSEGVTWILF RYPLTISQLQ IEEFRRLRTH VKGAELVEGC DGILGDNFRP TQPLSDRVIR AAFQ

    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.

    Ca8 Human
  • View Data Sheet

    Name :

    TPX E.coli

    Description:

    Thiol Peroxidase E.Coli Recombinant

    Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.

    Product # :

    ENZ-135

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    Description

    TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Recombinant TPX solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Lipid hydroperoxide peroxidase (TPX) belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. TPX has an imperative role in thioredoxin peroxidase activity.

    • Synonyms

      Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.

    • Physical Appearance

      Sterile filtered liquid formulation 1 mg/ml.

    • Stability

      TPX E.Coli 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 MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA.

    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.

    Tpx Ecoli
  • View Data Sheet

    Name :

    STK17A Human

    Description:

    Serine/Threonine Kinase 17A Human Recombinant

    DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    Product # :

    PKA-314

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    Description

    STK17A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (64-321 a.a) and having a molecular mass of 31.9kDa.STK17A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STK17A protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STK17A belongs to the DAP kinase-associated apoptosis-inducing protein kinase family and encodes an autophosphorylated nuclear protein with a protein kinase domain. STK17A acts as a positive regulator of apoptosis. STK17A is greatly expressed in the placenta with lower levels in the heart, lung, skeletal muscle, kidney and pancreas.

    • Synonyms

      DRAK1, Serine/threonine-protein kinase 17A, DAP kinase-related apoptosis-inducing protein kinase 1, STK17A.

    • 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 MGSGRELGRG KFAVVRKCIK KDSGKEFAAK FMRKRRKGQD CRMEIIHEIA VLELAQDNPW VINLHEVYET ASEMILVLEY AAGGEIFDQC VADREEAFKE KDVQRLMRQI LEGVHFLHTR DVVHLDLKPQ NILLTSESPL GDIKIVDFGL SRILKNSEEL REIMGTPEYV APEILSYDPI SMATDMWSIG VLTYVMLTGI SPFLGNDKQE TFLNISQMNL SYSEEEFDVL SESAVDFIRT LLVKKPEDRA TAEECLKHPW 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.

    Stk17A Human
  • View Data Sheet

    Name :

    PIN1 Mouse

    Description:

    Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    Product # :

    ENZ-1045

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    Description

    PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PIN1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,200 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin.

    More Info

    • Introduction

      Pin 1 is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and essential for cell cycle regulation Pin1 is nuclear PPIase containing a WW protein interaction domain, and is structurally and functionally related to Ess1/Ptf1, an essential protein in budding yeast. PPIase activity is necessary for Ess1/Pin1 function in yeast. Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting with NIMA and attenuating its mitosis-promoting activity. Substrates of Pin1 include the mitotic regulators (Cdc25 phosphatase and NIMA, PLK I, Wee, and Myt1 kinases), several transcription factors like b-Catenin, c-Jun, and the tumor suppressor protein p53, and some specific proteins like the RNA Pol II, the cytoskeleton protein tau, and the G1/S protein Cyclin D1.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (EC:5.2.1.8), Peptidyl-prolyl cis-trans isomerase Pin1, PPIase Pin1, Pin1, PIN1.

    • 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 MGSMADEEKL PPGWEKRMSR SSGRVYYFNH ITNASQWERP SGGSTVGGSS KNGQGEPAKV RCSHLLVKHS QSRRPSSWRQ EKITRSKEEA LELINGYIQK IKSGEEDFES LASQFSDCSS AKARGDLGPF SRGQMQKPFE DASFALRTGE MSGPVFTDSG IHIILRTE.

    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.

    Pin1 Mouse
  • View Data Sheet

    Name :

    Urokinase Human

    Description:

    Urokinase Human

    Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.

    Product # :

    ENZ-264

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    • More Info

    Description

    Urokinase is a two-chain glycoprotein containing 411 amino acids with 12 disulfide bonds. Its molecular weight is 54,000 Dalton.

    Source

    Human urine.

    Formulation

    The Urokinase was lyophilized from a concentrated (1mg/ml) solution containing phosphate buffer.

    Purity

    Greater than 90.0%.

    More Info

    • Introduction

      Urokinase (UK) is a serine protease, which is one of biological plasminogen activators.
      It is involved in a number of biological functions including fibrinolysis, embryogenesis, cell migration, tissue remodeling, ovulation, and wound healing.
      It can be obtained from human urine or kidney cell culture.

    • Synonyms

      Urokinase, Abbokinase, Urokinase-type Plasminogen Activator,uPA, EC 3.4.21.73, UK.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Contaminants

      Free of: Hepatitis B surface antigen, Hepatitis C antibody and HIV I and II.

    • Specific Activity

      187,973IU/mg.

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

    Urokinase Human
  • View Data Sheet

    Name :

    NUDT14 Human

    Description:

    Nudix Type Motif 14 Human Recombinant

    UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.

    Product # :

    ENZ-691

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    Description

    NUDT14 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222) and having a molecular mass of 26.5kDa. NUDT14 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT14 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Uridine diphosphate glucose pyrophosphatase (NUDT14), is a part of the nudix hydrolase family. NUDT14 is a cytoplasmic protein which contains one nudix hydrolase domain and acts as the sugar donor in numerous glycosylation reactions, including those involved in the production of glycogen. NUDT14 hydrolyzes ADP-ribose into ribose 5-phosphate and AMP, and UDP-glucose to glucose 1-phosphate and UMP. NUDT14 is a homodimer which binds magnesium as a cofactor and is encoded by a gene located on human chromosome 14.

    • Synonyms

      UGPP, UGPPase, Uridine diphosphate glucose pyrophosphatase, UDPG pyrophosphatase, Nucleoside diphosphate-linked moiety X motif 14, Nudix motif 14, NUDT14.

    • 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 MGSMERIEGA SVGRCAASPY LRPLTLHYRQ NGAQKSWDFM KTHDSVTVLL FNSSRRSLVL VKQFRPAVYA GEVERRFPGS LAAVDQDGPR ELQPALPGSA GVTVELCAGL VDQPGLSLEE VACKEAWEEC GYHLAPSDLR RVATYWSGVG LTGSRQTMFY TEVTDAQRSG PGGGLVEEGE LIEVVHLPLE GAQAFADDPD IPKTLGVIFG VSWFLSQVAP NLDLQ.

    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.

    Nudt14 Human
  • View Data Sheet

    Name :

    NUDT2 Human

    Description:

    Nudix Type Motif 2 Human Recombinant

    nudix (nucleoside diphosphate linked moiety X)-type motif 2, APAH1, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, Diadenosine tetraphosphatase, Nucleoside diphosphate-linked moiety X motif 2, Ap4Aase, EC 3.6.1.17, MGC10404, Ap4A hydrolase 1, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase.

    Product # :

    ENZ-063

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NUDT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147a.a.) and having a molecular mass of 19.0kDa.NUDT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NUDT2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      NUDT2 belongs to the MutT family of nucleotide pyrophosphatases, a subset of the larger NUDIX hydrolase family. NUDT2 conserves homeostasis by using water to cleave the metabolite NUDT symmetrically back into its original ATP and AMP molecules. In addition, NUDT2 is active towards other adenosine and diadenosine polyphosphates with four or more phosphate groups, however, not towards diadenosine triphosphate. NUDT2 has a role in heat shock and metabolic stress by regulating intracellular dinucleoside polyphosphate concentrations.

    • Synonyms

      nudix (nucleoside diphosphate linked moiety X)-type motif 2, APAH1, Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase, Diadenosine tetraphosphatase, Nucleoside diphosphate-linked moiety X motif 2, Ap4Aase, EC 3.6.1.17, MGC10404, Ap4A hydrolase 1, bis(5'-nucleosyl)-tetraphosphatase (asymmetrical), diadenosine 5',5''-P1,P4-tetraphosphate pyrophosphohydrolase.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MALRACGLII FRRCLIPKVD NNAIEFLLLQ ASDGIHHWTP PKGHVEPGED DLETALRETQ EEAGIEAGQL TIIEGFKREL NYVARNKPKT VIYWLAEVKD YDVEIRLSHE HQAYRWLGLE EACQLAQFKE MKAALQEGHQ FLCSIEA

    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.

    Nudt2 Human
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