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Search results

1000 results found for “deaminase”

Name

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  • View Data Sheet

    Name :

    Chitinase Protein

    Description:

    Chitinase Clostridium Paraputrificum Recombinant

    Product # :

    ENZ-031

    Price :

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    Description

    Chitinase Clostridium Paraputrificum Recombinant fused with a His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 582 amino acids and having a molecular mass of 64.2kDa. The Chitinase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Chitinase lyophilized from a 0.2µm filtered concentrated solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chitinase is a digestive enzyme which breaks down glycosidic bonds in chitin. Due to chitin being a component of the cell walls of fungi and exoskeletal elements of some animals (including worms and arthropods), chitinases are usually found in organisms that either need to remake their own chitin or to dissolve and digest the chitin of fungi or animals. Chitinivorous organisms include many bacteria genuses such as Aeromonas, Bacillus, Vibrio, among others, which may be pathogenic or detritivorous. Chitinase expression is mediated by the NPR1 gene and the salicylic acid pathway, both of which are involved in resisting fungal and insect attack. Human chitinases appear in gastric juices. They are likely to be digestive chitinases, for catabolic activity. Chitinase activity is identified systemically in humans, in the blood, and possibly cartilage. Chitinase has been related to allergies, asthma in particular has been linked to enhanced chitinase expression levels, also dust mites and mold spores which are both chitin covered.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MRGSGSHHHH HHMYYGDWSI WGGQGNFYPK DIPADKLTHL NFAFMDFNSS GELIYCDKDA AIGHPLGNLG VTYGDVNGGI LNAFQVLKSE NPNLKIGVSL GGWSKSGDFS TIAATPSIRA KFVENVMKFI KYTNMDFVDI DWEYPGDYRE PDKTDNINDE GTPNASAGDK ENYILLLQDL KEALNKQGKE LGKVYELSVA LPAGVSKIEK GIDVDKLFNI VDFANIMTYD MAGAWSTTSG HQTALYTNPN APEEYKGLSV DESVKYYISQ GAEREKIVVG AAYYTRGWEQ VSDKGTDPNN PGLFGEAAVV NKDADLSPTP GALNEAPMKN GEGGRAGGVW GYNALDKLKS KYTGLKEYWD DSAKAPYLYN SETGAFFTYD NIRSIQEKAK YVKENNLGGI IGWMASQDAT TNSTKRDELT TATKESLFGK EDLPKYEIKY TENDITCTVT PVKQSWGSGG VLKMSITNNE KLDESGEVLS TVETSAKTVK NMKVYIKTDG IAITGSQYPA GPVTKEGDYY VIDFGKISDG KLMKAGITFT FDLNLDKAIE DTNNIISIEV SQRMYQTSPE FNRQTIWENT NS.

    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.

    Chitinase
  • View Data Sheet

    Name :

    GLUD1 Human

    Description:

    Glutamate Dehydrogenase 1 Human Recombinant

    Glutamate Dehydrogenase 1, GLUD, GDH 1, EC 1.4.1.3, GDH, GDH1, Glutamate Dehydrogenase (NAD(P)+), Glutamate Dehydrogenase 1 Mitochondrial, EC 1.4.1, GLUD1.

    Product # :

    ENZ-792

    Price :

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    Description

    GLUD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 528 amino acids (54-558) and having a molecular mass of 58.4kDa.GLUD1 is fused to a 23 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The GLUD1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamate dehydrogenase 1, mitochondrial precursor (GLUD1) is a member of the Glu/Leu/Phe/Val dehydrogenases family. GLUD1 is a mitochondrial glutamate dehydrogenase, which converts L-glutamate into alpha-ketoglutarate. GLUD1 has a pivotal role in nitrogen metabolism in plants and animals. GLUD1 is observed in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate. The GLUD1 enzyme has a vital role in regulating amino acid induced insulin secretion. GLUD1 gene mutations cause hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 enzyme is allosterically activated by ADP and inhibited by GTP and ATP.

    • Synonyms

      Glutamate Dehydrogenase 1, GLUD, GDH 1, EC 1.4.1.3, GDH, GDH1, Glutamate Dehydrogenase (NAD(P)+), Glutamate Dehydrogenase 1 Mitochondrial, EC 1.4.1, GLUD1.

    • 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 MGSSEAVADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLR TRESEEQKRN RVRGILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCIAV GESDGSIWNP DGIDPKELED FKLQHGSILG FPKAKPYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFKVY NEAGVTFT.

    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.

    Glud1 Human
  • View Data Sheet

    Name :

    DDT Mouse

    Description:

    D-Dopachrome Tautomerase Mouse Recombinant

    D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    Product # :

    ENZ-1073

    Price :

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    Description

    DDT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-118 a.a) and having a molecular mass of 15.5kDa. DDT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    DDT protein solution (1mg/ml) contains 20mM Tris-Hcl buffer (pH8.0) & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DDT is an enzyme that catayzes the tautomerization of D-dopachrome to give 5,6-dihydroxyindole (DHI). DDT is part of the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. DDT shares a homologous amino acid sequence (33% identical) with MIF and has similar tautomerase activity. DDT functions a proinflammatory cytokine.

    • Synonyms

      D-dopachrome decarboxylase (EC:4.1.1.84), D-dopachrome tautomerase, Ddt.

    • 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 MGSMPFVELE TNLPASRIPA GLENRLCAAT ATILDKPEDR VSVTIRPGMT LLMNKSTEPC AHLLVSSIGV VGTAEQNRTH SASFFKFLTE ELSLDQDRIV IRFFPLEAWQ IGKKGTVMTF 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.

    Ddt Mouse
  • View Data Sheet

    Name :

    NDUFV2 Human

    Description:

    NADH Dehydrogenase Flavoprotein 2 Human Recombinant

    CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    Product # :

    ENZ-743

    Price :

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    Description

    NDUFV2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (33-249 a.a) and having a molecular mass of 26.1kDa.NDUFV2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NDUFV2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NADH Dehydrogenase Flavoprotein 2 (NDUFV2) is a 24 kDa Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which is a part of the minimal assembly required for catalysisthe. NDUFV2 is aslo involved in electron transfer. Mutations in NDUFV2 are implicated in Parkinson's disease, bipolar disorder, schizophrenia, and have been discovered in one case of early onset hypertrophic cardiomyopathy and encephalopathy.

    • Synonyms

      CI-24k, NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial, NADH-ubiquinone oxidoreductase 24 kDa subunit, NDUFV2.

    • 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 MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL.

    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.

    Ndufv2 Human
  • View Data Sheet

    Name :

    LDHB Mouse

    Description:

    Lactate Dehydrogenase B Mouse Recombinant

    L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

    Product # :

    ENZ-1052

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    Description

    LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 150 units/mg, in which one unit will 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5.

    More Info

    • Introduction

      Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
      A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.

    • Synonyms

      L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

    • 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 MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.

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    Ldhb Mouse
  • View Data Sheet

    Name :

    HPGD Human

    Description:

    Hydroxyprostaglandin Dehydrogenase 15-(NAD) Human Recombinant

    GDH1, SDR36C1, 15-PGDH, PGDH, Prostaglandin dehydrogenase 1, hydroxyprostaglandin dehydrogenase 15-(NAD)

    Product # :

    ENZ-564

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    Description

    HPGD Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 286 amino acids (1-266a.a.) and having a molecular mass of 31.1 kDa. HPGD is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HPGD protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 0.1M NaCl,1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      HPGD is the essential enzyme of prostaglandin degradation. 15-PGDH protein strongly decreases the biologic activity of these molecules by catalyzing the oxidation of the 15-hydroxyl group of prostaglandins to a keto group. GDH1 is involved in numerous physiologic and cellular processes, for instance inflammation.

    • Synonyms

      GDH1, SDR36C1, 15-PGDH, PGDH, Prostaglandin dehydrogenase 1, hydroxyprostaglandin dehydrogenase 15-(NAD)

    • 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHVNGKVALV TGAAQGIGRA FAEALLLKGA KVALVDWNLE AGVQCKAALD EQFEPQKTLF IQCDVADQQQ LRDTFRKVVD HFGRLDILVN NAGVNNEKNW EKTLQINLVS VISGTYLGLD YMSKQNGGEG GIIINMSSLA GLMPVAQQPV YCASKHGIVG FTRSAALAAN LMNSGVRLNA ICPGFVNTAI LESIEKEENM GQYIEYKDHI KDMIKYYGIL DPPLIANGLI TLIEDDALNG AIMKITTSKG IHFQDYDTTP FQAKTQ.

    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.

    Hpgd Human
  • View Data Sheet

    Name :

    OGG1 Human

    Description:

    8-Oxoguanine DNA Glycosylase Human Recombinant

    HMMH, HOGG1, MUTM, OGH1, AP lyase.

    Product # :

    ENZ-253

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    Description

    OGG1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 368 amino acids (1-345 a.a.) and having a molecular mass of 41.2 kDa. The OGG1 is fused to 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing PBS (pH-7.4) and 40% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      OGG1 is a DNA glycosylase enzyme which takes part in base excision repair. OGG1 protein is the main enzyme accountable for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which arises as a result of exposure to reactive oxygen species (ROS). OGG1 shows beta lyase activity that nicks DNA 3'' to the lesion.

    • Synonyms

      HMMH, HOGG1, MUTM, OGH1, AP lyase.

    • Physical Appearance

      Sterile filtered colourless 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 TGSMPARALL PRRMGHRTLA STPALWASIP CPRSELRLDL VLPSGQSFRW REQSPAHWSG VLADQVWTLT QTEEQLHCTV YRGDKSQASR PTPDELEAVR KYFQLDVTLA QLYHHWGSVD SHFQEVAQKF QGVRLLRQDP IECLFSFICS SNNNIARITG MVERLCQAFG PRLIQLDDVT YHGFPSLQAL AGPEVEAHLR KLGLGYRARY VSASARAILE EQGGLAWLQQ LRESSYEEAH KALCILPGVG TKVADCICLM ALDKPQAVPV DVHMWHIAQRDYSWHPTTSQ AKGPSPQTNK ELGNFFRSLW GPYAGWAQAV LFSADLRQCR HAQEPPAKRRKGSKGPEG.

    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.

    Ogg1 Human
  • View Data Sheet

    Name :

    HSD17B10 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 10 Human Recombinant

    17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.

    Product # :

    PRO-823

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    Description

    HSD17B10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 271 amino acids (12-261 a.a.) and having a molecular mass of 28.1 kDa. HSD17B10 protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    HSD17B10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      HSD17B10 functions in mitochondrial tRNA maturation. HSD17B10 is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5''-ends. HSD17B10 interacts with intracellular amyloid-beta, and contributes to the neuronal dysfunction associated with Alzheimer disease.

    • Synonyms

      17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.

    • 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 MVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV IRLDGAIRMQ P.

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    Hsd17B10 Human
  • View Data Sheet

    Name :

    IVD Human

    Description:

    Isovaleryl Coenzyme A Dehydrogenase Human Recombinant

    FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.

    Product # :

    ENZ-490

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    Description

    IVD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 415 amino acids (33-426 a.a.) and having a molecular mass of 45.3 kDa. The IVD is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      IVD is a mitochondrial matrix enzyme that is part of the cyl-CoA dehydrogenase family which catalyzes the third step in leucine catabolism. The genetic deficiency of IVD leads to a buildup of isovaleric acid, which is toxic to the central nervous system and results in isovaleric acidemia. IVD is a homotetrameric flavoenzyme which catalyzes the conversion of isovaleryl-CoA to 3-methylcrotonyl-CoA.

    • Synonyms

      FLJ12715, isovaleryl-CoA dehydrogenase mitochondrial, FLJ34849, EC 1.3.99.10, IVD, ACAD2.

    • 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 MHSLLPVDDA INGLSEEQRQ LRQTMAKFLQ EHLAPKAQEI DRSNEFKNLR EFWKQLGNLG VLGITAPVQY GGSGLGYLEH VLVMEEISRA SGAVGLSYGA HSNLCINQLV RNGNEAQKEK YLPKLISGEY IGALAMSEPN AGSDVVSMKL KAEKKGNHYI LNGNKFWITN GPDADVLIVY AKTDLAAVPA SRGITAFIVE KGMPGFSTSK KLDKLGMRGS NTCELIFEDC KIPAANILGH ENKGVYVLMS GLDLERLVLA GGPLGLMQAV LDHTIPYLHV REAFGQKIGH FQLMQGKMAD MYTRLMACRQ YVYNVAKACD EGHCTAKDCA GVILYSAECA TQVALDGIQC FGGNGYINDF PMGRFLRDAK LYEIGAGTSE VRRLVIGRAF NADFH.

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    Ivd Human
  • View Data Sheet

    Name :

    MDH1 Human

    Description:

    Malate Dehydrogenase 1 Human Recombinant

    MDH-s, MDHA, MOR2.

    Product # :

    ENZ-256

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    Description

    MDH1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-334 a.a.) and having a molecular mass of 37.4 kDa. The MDH1 is fused to an 8 amino acid His tag at C-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The MDH1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 250 units/mg, and is defined as the amount of enzyme that cleaves 1umole of oxalacetate and beta-NADH to L-malate and beta-NAD per minute at pH8.0 at 25°C.

    More Info

    • Introduction

      MDH1 catalyzes the reversible oxidation of malate to oxaloacetate, using the NAD/NADH cofactor system in the citric acid cycle. MDH1 is abundantly found in the cytoplasm and is involved in the malate-aspartate shuttle that functions in the metabolic coordination between cytosol and mitochondria. MDH1 regulates p53-dependent cell-cycle arrest and apoptosis in response to glucose deprivation.

    • Synonyms

      MDH-s, MDHA, MOR2.

    • 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). Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MSEPIRVLVT GAAGQIAYSL LYSIGNGSVF GKDQPIILVL LDITPMMGVL DGVLMELQDC ALPLLKDVIA TDKEDVAFKD LDVAILVGSM PRREGMERKD LLKANVKIFK SQGAALDKYA KKSVKVIVVG NPANTNCLTA SKSAPSIPKE NFSCLTRLDH NRAKAQIALK LGVTANDVKN VIIWGNHSST QYPDVNHAKV KLQGKEVGVY EALKDDSWLK GEFVTTVQQR GAAVIKARKL SSAMSAAKAI CDHVRDIWFG TPEGEFVSMG VISDGNSYGV PDDLLYSFPV VIKNKTWKFV EGLPINDFSR EKMDLTAKEL TEEKESAFEF LSSALEHHHH HH.

    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.

    Mdh1 Human
  • View Data Sheet

    Name :

    RNLS Human

    Description:

    Renalase Human Recombinant

    Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.

    Product # :

    ENZ-653

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    Description

    RNLS Human Recombinant produced in E. coli is a single polypeptide chain containing 349 amino acids (18-342) and having a molecular mass of 38.8 kDa.RNLS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RNLS solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Renalase (RNLS) is a flavin adenine dinucleotide-dependent amine oxidase which is secreted into the blood from the kidney. RNLS acts as a hormone which metabolizes circulating catecholamines that have an active role in the sympathetic and parasympathetic nervous systems. High catecholamine concentration activates plasma RNLS and promotes its secretion and synthesis.

    • Synonyms

      Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMALLRRQ TSGPLYLAVW DKAEDSGGRM TTACSPHNPQ CTADLGAQYI TCTPHYAKKH QRFYDELLAY GVLRPLSSPI EGMVMKEGDC NFVAPQGISS IIKHYLKESG AEVYFRHRVT QINLRDDKWE VSKQTGSPEQ FDLIVLTMPV PEILQLQGDI TTLISECQRQ QLEAVSYSSR YALGLFYEAG TKIDVPWAGQ YITSNPCIRF VSIDNKKRNI ESSEIGPSLV IHTTVPFGVT YLEHSIEDVQ ELVFQQLENI LPGLPQPIAT KCQKWRHSQV TNAAANCPGQ MTLHHKPFLA CGGDGFTQSN FDGCITSALC VLEALKNYI

    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.

    Rnls Human
  • View Data Sheet

    Name :

    GATM Human

    Description:

    Glycine Amidinotransferase Human Recombinant

    Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    Product # :

    ENZ-583

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    Description

    GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GATM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.

    • Synonyms

      Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.

    • 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 MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
      RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
      ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.

    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.

    Gatm Human
  • View Data Sheet

    Name :

    GOT2 Human, Active

    Description:

    Glutamic-Oxaloacetic Transaminase 2 Human Recombinant, Active

    EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    Product # :

    ENZ-998

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    Description

    GOT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 60 units/mg, and is defined as the amount of enzyme that convert 1umole of α-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

    More Info

    • Introduction

      GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.

    • Synonyms

      EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.

    • 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 MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.

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    Got2 Human Active
  • View Data Sheet

    Name :

    GOT1 Mouse

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

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

    Product # :

    ENZ-872

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Got1 Mouse
  • View Data Sheet

    Name :

    MAT2A Human

    Description:

    Methionine Adenosyltransferase II Alpha Human Recombinant

    MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.

    Product # :

    ENZ-320

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    Description

    MAT2A Human Recombinant fused with His tag (20 a.a.) at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 45.8 kDa.The MAT2A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAT2A solution (1mg/ml) contains 20mM Tris pH-8 & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.

    • Synonyms

      MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY.

    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.

    Mat2A Human
  • View Data Sheet

    Name :

    ADH1C Human

    Description:

    Alcohol Dehydrogenase 1C Human Recombinant

    Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.

    Product # :

    ENZ-622

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    Description

    ADH1C Human Recombinant produced in E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4 kDa.ADH1C is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ADH1C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.

    • Synonyms

      Alcohol dehydrogenase 1C (class I) gamma polypeptide, Alcohol dehydrogenase subunit gamma, alcohol dehydrogenase 3 (class I) gamma polypeptide, ADH gamma subunit, aldehyde reductase, ADH3, EC 1.1.1.1, EC 1.1.1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMSTAGK VIKCKAAVLW ELKKPFSIEE VEVAPPKAHE VRIKMVAAGI CRSDEHVVSG NLVTPLPVIL GHEAAGIVES VGEGVTTVKP GDKVIPLFTP QCGKCRICKN PESNYCLKND LGNPRGTLQD GTRRFTCSGK PIHHFVGVST FSQYTVVDEN AVAKIDAASP LEKVCLIGCG FSTGYGSAVK VAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIAVDIN KDKFAKAKEL GATECINPQD YKKPIQEVLK EMTDGGVDFS FEVIGRLDTM MASLLCCHEA CGTSVIVGVP PDSQNLSINP MLLLTGRTWK GAIFGGFKSK ESVPKLVADF MAKKFSLDAL ITNILPFEKI NEGFDLLRSG KSIRTVLTF.

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    Adh1C Human
  • View Data Sheet

    Name :

    DERA

    Description:

    Deoxyribose-Phosphate Aldolase E.Coli Recombinant

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

    Product # :

    ENZ-127

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Dera Ecoli 259 Aa
  • View Data Sheet

    Name :

    IDE Human, Active

    Description:

    Insulin-Degrading Enzyme Human Recombinant

    Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1. 

    Product # :

    ENZ-1192

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    Description

    IDE Human, Active Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (42-1019 a.a) containing a total of 984 amino acids, having a molecular mass of 114 kDa. IDE is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The IDE solution (0.5mg/ml) contains 10% Glycerol, 100mM NaCl, 0.05% Brij35 and 20mM Tris-HCl buffer (pH 7.5).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is greater than 3,000 pmol/min/ug in which 1 unit will convert 1.0 pmole of Mca-RPPGFSAFK(Dnp)-OH to MCA-Pro-Leu-OH per minute at pH 7.5 at 25°C.

    More Info

    • Synonyms

      Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulysin, EC 3.4.24.56, Insulinase, Insulin Protease, INSULYSIN, EC 3.4.24, IDE, insulin-degrading enzyme isoform 1.

    • Physical Appearance

      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

      MNNPAIKRIG NHITKSPEDK REYRGLELAN GIKVLLISDP TTDKSSAALD VHIGSLSDPP NIAGLSHFCE HMLFLGTKKY PKENEYSQFL SEHAGSSNAF TSGEHTNYYF DVSHEHLEGA LDRFAQFFLC PLFDESCKDR EVNAVDSEHE KNVMNDAWRL FQLEKATGNP KHPFSKFGTG NKYTLETRPN QEGIDVRQEL LKFHSAYYSS NLMAVCVLGR ESLDDLTNLV VKLFSEVENK NVPLPEFPEH PFQEEHLKQL YKIVPIKDIR NLYVTFPIPD LQKYYKSNPG HYLGHLIGHE GPGSLLSELK SKGWVNTLVG GQKEGARGFM FFIINVDLTE EGLLHVEDII LHMFQYIQKL RAEGPQEWVF QECKDLNAVA FRFKDKERPR GYTSKIAGIL HYYPLEEVLT AEYLLEEFRP DLIEMVLDKL RPENVRVAIV SKSFEGKTDR TEEWYGTQYK QEAIPDEVIK KWQNADLNGK FKLPTKNEFI PTNFEILPLE KEATPYPALI KDTAMSKLWF KQDDKFFLPK ACLNFEFFSP FAYVDPLHCN MAYLYLELLK DSLNEYAYAA ELAGLSYDLQ NTIYGMYLSV KGYNDKQPIL LKKIIEKMAT FEIDEKRFEI IKEAYMRSLN NFRAEQPHQH AMYYLRLLMT EVAWTKDELK EALDDVTLPR LKAFIPQLLS RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS
      QLVRYREVQL PDRGWFVYQQ RNEVHNNCGI EIYYQTDMQS TSENMFLELF CQIISEPCFN TLRTKEQLGY IVFSGPRRAN GIQGLRFIIQ SEKPPHYLES RVEAFLITME KSIEDMTEEA FQKHIQALAI RRLDKPKKLS AECAKYWGEI ISQQYNFDRD NTEVAYLKTL TKEDIIKFYK EMLAVDAPRR HKVSVHVLAR EMDSCPVVGE FPCQNDINLS QAPALPQPEV IQNMTEFKRG LPLFPLVKPH INFMAAKLHH HHHH.

    • Background

      Insulin-degrading enzyme (IDE) is a crucial protease that plays a significant role in maintaining glucose homeostasis by degrading insulin and other bioactive peptides. Dysregulation of IDE has been implicated in various metabolic disorders, particularly type 2 diabetes mellitus. IDE is also associated with the clearance of amyloid-beta peptides in the brain, making it relevant to Alzheimer's disease pathology. Studying the recombinant form of IDE is fundamental to understanding its functional mechanisms and exploring potential avenues for therapeutic interventions.

      The primary goal of this research is to express and purify recombinant IDE using diverse expression systems. Recombinant DNA techniques will be employed to construct expression vectors containing the IDE gene, followed by expression in bacterial, yeast, or mammalian cell-based systems. The recombinant IDE will be purified using affinity chromatography or other appropriate methods, facilitating subsequent biochemical and biophysical characterization.

      The second objective is to investigate the substrate specificity and catalytic activity of the purified IDE. In vitro enzymatic assays will be conducted to analyse the ability of the recombinant IDE to degrade insulin and other potential substrates. The effects of various factors, such as pH, temperature, and potential modulators, on IDE activity will be evaluated. Additionally, the interactions between IDE and its substrates will be explored using binding assays.

      The third objective is to elucidate the three-dimensional structure of the IDE recombinant using techniques like X-ray crystallography or nuclear magnetic resonance (NMR) spectroscopy. Structural insights into the active site and binding pockets of IDE will provide valuable information for understanding its substrate recognition and catalytic mechanisms. This knowledge could be instrumental in designing targeted therapeutic compounds.

      By characterizing the IDE recombinant, this research aims to contribute to our understanding of its role in insulin metabolism, glucose regulation, and potential therapeutic applications. The findings from this study may have implications for the development of novel treatments for diabetes and other related disorders.

    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.

    Ide Human Active
  • View Data Sheet

    Name :

    GOT2 Mouse, Active

    Description:

    Glutamic-Oxaloacetic Transaminase 2, Active Mouse Recombinant

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

    Product # :

    ENZ-1111

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    Description

    GOT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (30-430 aa) and having a molecular mass of 46.8kDa.GOT2 is fused to a 21 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT2 solution (0.5 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH7.4)

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 20 units/mg. Measured by the amount of enzyme that converts 1umole of alpha-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C˚.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Got 2 Mouse
  • View Data Sheet

    Name :

    HSD17B8 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 8 Human Recombinant

    E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.

    Product # :

    ENZ-108

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    Description

    HSD17B8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 281 amino acids (1-261 a.a.) and having a molecular mass of 29.1kDa.HSD17B8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HSD17B8 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 150mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      E2 17-beta-dehydrogenase 8 (HSD17B8) is a member of the short-chain dehydrogenases/reductases (SDR) family. In mice, the HSD17B8 protein is a 17-beta-hydroxysteroid dehydrogenase which can regulate the concentration of biologically active estrogens and androgens. HSD17B8 is preferentially an oxidative enzyme and inactivates E2, testosterone, and DHT. However, the HSD17B8 enzyme has some reductive activity and can synthesize E2 from E1. HSD17B8 may have a role in biosynthesis of fatty acids in mitochondria.

    • Synonyms

      E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.

    • 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 MASQLQNRLR SALALVTGAG SGIGRAVSVR LAGEGATVAA CDLDRAAAQE TVRLLGGPGS KEGPPRGNHA AFQADVSEAR AARCLLEQVQ ACFSRPPSVV VSCAGITQDE FLLHMSEDDW DKVIAVNLKG TFLVTQAAAQ ALVSNGCRGS IINISSIVGK VGNVGQTNYA ASKAGVIGLT QTAARELGRH GIRCNSVLPG FIATPMTQKV PQKVVDKITE MIPMGHLGDP EDVADVVAFL ASEDSGYITG TSVEVTGGLF M.

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    Hsd17B8 Human
  • View Data Sheet

    Name :

    IDH1 Human

    Description:

    Isocitrate Dehydrogenase-1 Human Recombinant

    Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    Product # :

    ENZ-193

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    Description

    IDH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 434 amino acids (1-414) and having a molecular mass of 48.8 kDa.IDH1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The IDH1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,
    1mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The Specific activity is > 0.7 units/ml. One unit will convert 1.0 umole of isocitrate to alpha-ketoglutarate per minute at pH7.5 at 25C.

    More Info

    • Introduction

      Isocitrate Dehydrogenase is an enzyme of the oxidoreductase class that catalyzes the conversion of isocitrate and NAD+ to yield 2-ketoglutarate, carbon dioxide, and NADH. It occurs in cell mitochondria. The enzyme requires Mg2+, Mn2+; it is activated by ADP, citrate, and Ca2+, and inhibited by NADH, NADPH, and ATP. The reaction is the key rate-limiting step of the citric acid (tricarboxylic) cycle.

    • Synonyms

      Isocitrate dehydrogenase [NADP] cytoplasmic, EC 1.1.1.42, Cytosolic NADP-isocitrate dehydrogenase, Oxalosuccinate decarboxylase, IDH, NADP(+)-specific ICDH, IDP, PICD.

    • 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 MSKKISGGSV VEMQGDEMTR IIWELIKEKL IFPYVELDLH SYDLGIENRD ATNDQVTKDA AEAIKKHNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL VSGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPSD GTQKVTYLVH NFEEGGGVAM GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKQYKSQFE AQKIWYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLVCPDG KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWTRGL AHRAKLDNNK ELAFFANALE EVSIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKIKLA QAKL

    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.

    Idh1 Human
  • View Data Sheet

    Name :

    NMNAT1 Human, Active

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant , Active

    NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    Product # :

    ENZ-1002

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    Description

    NMNAT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (1-279 a.a.) and having a molecular mass of 36 kDa. The NMNAT1 is fused to a 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NMNAT1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl, 1mM DTT and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 7,000 pmol/min/ug, and was obtained by measuring the beta-NAD from nicotinamide mononucleotide and ATP per minute at pH 8.0 at 37C.

    More Info

    • Introduction

      NMNAT1 enzyme is vital for NAD biosynthesis, catalyzing the condensation of nicotinamide mononucleotide (NMN) or nicotinic acid mononucleotide (NaMN) with the AMP moiety of ATP to form NAD or NaAD. NMNAT1 is widely expressed with high levels in skeletal muscle, heart, liver and kidney. This protein appears to have the ability to protect against axonal degeneration following mechanical or toxic insults.

    • Synonyms

      NMNAT, NMNAT1, PNAT1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase 1, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, EC=2.7.7.1, EC=2.7.7.18.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMENS EKTEVVLLAC GSFNPITNMH LRLFELAKDY MNGTGRYTVV KGIISPVGDA YKKKGLIPAY HRVIMAELAT KNSKWVEVDT WESLQKEWKE TLKVLRHHQE KLEASDCDHQ QNSPTLERPG RKRKWTETQD SSQKKSLEPK TKAVPKVKLL CGADLLESFA VPNLWKSEDI TQIVANYGLI CVTRAGNDAQ KFIYESDVLW KHRSNIHVVN EWIANDISST KIRRALRRGQSIRYLVPDLV QEYIEKHNLY SSESEDRNAG VILAPLQRNT AEAKT.

    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.

    Nmnat1 Human Active
  • View Data Sheet

    Name :

    ALDH2 Mouse, Active

    Description:

    Aldehyde Dehydrogenase 2 Mouse Recombinant, Active

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

    Product # :

    ENZ-1093

    Price :

    Quantity :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

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

    Source

    Escherichia Coli.

    Formulation

    ALDH2 Mouse protein (0.5mg/ml) is formulated in Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 180 pmol/min/ug, and was obtained by measuring the increase of NADH in absorbance at 340 nm resulting from the reduction of NAD at pH 8.0 at 25C.

    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 DVDKAVKAARAAFQLGSPWR RMDASDRGRL LYRLADLIER DRTYLAALET LDNGKPYVIS YLVDLDMVLK CLRYYAGWAD KYHGKTIPID GDFFSYTRHEPVGVCGQIIP WNFPLLMQAW KLGPALATGN VVVMKVAEQT PLTALYVANL IKEAGFPPGV VNIVPGFGPT AGAAIASHEG VDKVAFTGSTEVGHLIQVAA GSSNLKRVTL ELGGKSPNII MSDADMDWAV EQAHFALFFN QGQCCCAGSR TFVQENVYDE FVERSVARAK SRVVGNPFDSRTEQGPQVDE TQFKKILGYI KSGQQEGAKL LCGGGAAADR GYFIQPTVFG DVKDGMTIAK EEIFGPVMQI LKFKTIEEVV GRANDSKYGLAAAVFTKDLD 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 Murine
  • View Data Sheet

    Name :

    RNASE7 Human

    Description:

    Ribonuclease 7 Human Recombinant

    Ribonuclease, RNase A Family, 7, Skin-Derived Antimicrobial Protein 2, RNase 7, SAP-2, EC 3.1.27.5, EC 3.1.27., EC 3.1.27, Ribonuclease 7.

    Product # :

    ENZ-704

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    RNASE7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (29-156 a.a) and having a molecular mass of 16.9kDa. RNASE7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNASE7 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ribonuclease 7 (RNASE7) is one of the final RNase A superfamily ribonucleases. RNASE7 was isolated from skin-derived stratum corneum. RNASE7 protein demonstrated potent ribonuclease activity and hence may contribute to the well-known ribonuclease activity of human skin. RNASE7 has revealed a broad spectrum antimicrobial activity against many pathogenic microorganisms and extraordinarily potent activity.

    • Synonyms

      Ribonuclease, RNase A Family, 7, Skin-Derived Antimicrobial Protein 2, RNase 7, SAP-2, EC 3.1.27.5, EC 3.1.27., EC 3.1.27, Ribonuclease 7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKPKGMTS SQWFKIQHMQ PSPQACNSAM KNINKHTKRC KDLNTFLHEP FSSVAATCQT PKIACKNGDK NCHQSHGPVS LTMCKLTSGK YPNCRYKEKR QNKSYVVACK PPQKKDSQQF HLVPVHLDRV 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.

    Rnase7 Human
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