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Search results

1000 results found for “creatine kinases”

Name

Description

Product #

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  • 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

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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 :

    ErbB4 Human

    Description:

    Tyrosine Kinase ErbB-4 Human Recombinant

    Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 4.

    Product # :

    PKA-128

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    Description

    ErbB4 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 863 amino acids (26-649 a.a) and having a molecular mass of 96.6 kDa.ErbB4 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The ErbB4 solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Measured by its binding ability in a functional ELISA with Human NRG1(CAT# cyt-1186). The ED50 range ≤ 0.2 ug/ml.

    More Info

    • Introduction

      Tyrosine Kinase ErbB-4 (ErbB4) is a receptor tyrosine kinase that is a member of the epidermal growth factor receptor family whose members play a role as receptors for the EGF family of growth factors. ErbB4is a single-pass type I transmembrane protein with multiple furin-like cysteine rich domains,PDZ domain binding motif, a tyrosine kinase domain and a phosphotidylinositol-3 kinase binding site. ErbB4binds its ligands with low affinity and is expressed in normal skeletal muscle, heart, pituitary, brain and some breast carcinomas. Monomeric ErbB4 takes part in neuronal development and development of the heart and cancer.

    • Synonyms

      Receptor tyrosine-protein kinase erbB-4, Proto-oncogene-like protein c-ErbB-4, Tyrosine kinase-type cell surface receptor HER4, p180erbB4, 4ICD, E4ICD, s80HER4, ERBB4, HER4, receptor tyrosine-protein kinase erbB-4 isoform JM-a/CVT-1, receptor tyrosine-protein kinase erbB-4, tyrosine kinase-type cell surface receptor HER4, avian erythroblastic leukemia viral (v-erb-b2) oncogene homolog 4, proto-oncogene-like protein c-ErbB-4, ALS19, v-erb-a erythroblastic leukemia viral oncogene homolog 4, v-erb-b2 avian erythroblastic leukemia viral oncogene homolog 4, human epidermal growth factor receptor 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

      QSVCAGTENK LSSLSDLEQQ YRALRKYYEN CEVVMGNLEI TSIEHNRDLS FLRSVREVTG YVLVALNQFR YLPLENLRII RGTKLYEDRY ALAIFLNYRK DGNFGLQELG LKNLTEILNG GVYVDQNKFL CYADTIHWQD IVRNPWPSNL TLVSTNGSSG CGRCHKSCTG RCWGPTENHC QTLTRTVCAE QCDGRCYGPY VSDCCHRECA GGCSGPKDTD CFACMNFNDS GACVTQCPQT FVYNPTTFQL EHNFNAKYTY GAFCVKKCPH NFVVDSSSCV RACPSSKMEV EENGIKMCKP CTDICPKACD GIGTGSLMSA QTVDSSNIDK FINCTKINGN LIFLVTGIHG DPYNAIEAID PEKLNVFRTV REITGFLNIQ SWPPNMTDFS VFSNLVTIGG RVLYSGLSLL ILKQQGITSL QFQSLKEISA GNIYITDNSN LCYYHTINWT TLFSTINQRI VIRDNRKAEN CTAEGMVCNH LCSSDGCWGP GPDQCLSCRR FSRGRICIES CNLYDGEFRE FENGSICVEC DPQCEKMEDG LLTCHGPGPD NCTKCSHFKD GPNCVEKCPD GLQGANSFIF KYADPDRECH PCHPNCTQGC NGPTSHDCIY YPWTGHSTLP QHARLEPKSC DKTHTCPPCP APELLGGPSV FLFPPKPKDT LMISRTPEVT CVVVDVSHED PEVKFNWYVD GVEVHNAKTK PREEQYNSTY RVVSVLTVLH QDWLNGKEYK CKVSNKALPA PIEKTISKAK GQPREPQVYT LPPSRDELTK NQVSLTCLVK GFYPSDIAVE WESNGQPENN YKTTPPVLDS DGSFFLYSKL TVDKSRWQQG NVFSCSVMHE ALHNHYTQKS LSLSPGKHHH HHH

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

    Erbb4 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

    Price :

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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.

    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.

    Ldhb Mouse
  • View Data Sheet

    Name :

    ECH1 Human

    Description:

    Enoyl CoA Hydratase 1, Peroxisomal Human Recombinant

    peroxisomal, enoyl Coenzyme A hydratase 1.

    Product # :

    ENZ-562

    Price :

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    Description

    ECH1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (34-328a.a.) and having a molecular mass of 34.4kDa.ECH1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ECH1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 1mM DTT, 50mM NaCl, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ECH1 is a member of the hydratase/isomerase superfamily. ECH1 demonstrates high sequence similarity to enoyl-coenzyme A (CoA) hydratases of more than a few species, mostly within a conserved domain characteristic of these proteins. ECH1 contains a C-terminal peroxisomal targeting sequence, localizes to both the peroxisome and the mitochondria. peroxisomal takes part in the auxiliary step of the fatty acid beta-oxidation pathway specifically functioning to catalyze the isomerization of 3-trans, 5-cis-dienoyl-CoA to 2-trans, 4-transdienoyl-CoA.

    • Synonyms

      peroxisomal, enoyl Coenzyme A hydratase 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MTGSSAQEAA SGVALGEAPD HSYESLRVTS AQKHVLHVQL NRPNKRNAMN KVFWREMVEC FNKISRDADC RAVVISGAGK MFTAGIDLMD MASDILQPKG DDVARISWYL RDIITRYQET FNVIERCPKP VIAAVHGGCI GGGVDLVTAC DIRYCAQDAF FQVKEVDVGL AADVGTLQRL PKVIGNQSLV NELAFTARKM MADEALGSGL VSRVFPDKEV MLDAALALAA EISSKSPVAV QSTKVNLLYS RDHSVAESLN YVASWNMSML QTQDLVKSVQ ATTENKELKT VTFSKL.

    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.

    Ech1 Human
  • View Data Sheet

    Name :

    RNASE2 Human

    Description:

    Ribonuclease 2 Human Recombinant

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

    Product # :

    ENZ-1175

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    Description

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

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Rnase2 Human
  • View Data Sheet

    Name :

    GLB1 E.Coli

    Description:

    Galactosidase-Beta 1 E.coli Recombinant

    lacZ, beta-gal, β-gal.

    Product # :

    ENZ-041

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    Description

    The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.

    Source

    Escherichia Coli.

    Formulation

    Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol

    Purity

    Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.

    More Info

    • Introduction

      Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.

    • Synonyms

      lacZ, beta-gal, β-gal.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Protein should be stored for Short Term at 4°C and for long term at -20°C.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Glb1 Ecoli Recombinant
  • 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.

    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.

    Ca12 Human
  • View Data Sheet

    Name :

    GLUL Human, His Active

    Description:

    Glutamine Synthetase Human Recombinant, His Active

    GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

    Product # :

    ENZ-984

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    Description

    GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLUL Human solution containing 20mM Tris-HCl pH-8, 5mM DTT, 0.2M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,800 pmol/min/ug, and is defined as the amount of enzyme that convert 1.0 pmole of L-glutamate to L-glutamine per miunte at pH 7.5 at 37C in coupled system with PK/LDH.

    More Info

    • Introduction

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

    • Synonyms

      GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.

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

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

    Glul Human His Active
  • View Data Sheet

    Name :

    GPT2 Mouse

    Description:

    Glutamic-Pyruvate Transaminase 2 Mouse Recombinant

    ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.

    Product # :

    ENZ-1096

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    Description

    GPT2 Mouse Recombinant produced in E. coli is a single polypeptide chain containing 522 amino acids (1-522) and having a molecular mass of 60.1 kDa. Mouse GPT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The GPT2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 20% glycerol, and 2mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Biological Activity

    Greater than 50units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH7.5 at 37℃.

    More Info

    • Introduction

      Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.

    • Synonyms

      ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 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 MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ.

    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.

    Gpt2 Mouse
  • View Data Sheet

    Name :

    NQO1 Human

    Description:

    NAD(P)H Dehydrogenase Quinone 1 Human Recombinant

    NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    Product # :

    ENZ-448

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    Description

    NQO1 Human Recombinant fused with a 20 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids (1-274 a.a.) and having a molecular mass of 33kDa.The NQO1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The NQO1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.

    • Synonyms

      NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.

    • 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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK.

    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.

    Nqo1 Human
  • View Data Sheet

    Name :

    GLYAT Human

    Description:

    Glycine-N-Acyltransferase Human Recombinant

    Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.

    Product # :

    ENZ-148

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    Description

    GLYAT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-296) and having a molecular mass of 36.0 kDa.The GLYAT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GLYAT protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.

    • Synonyms

      Glycine-N-acyltransferase, ACGNAT, GAT, CAT, AAc, HRP-1(CLP), Acyl-CoA: glycine amino acid N-acyltransferase, EC 2.3.1.13.

    • Physical Appearance

      GLYAT is supplied as a 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 MMLPLQGAQM LQMLEKSLRK SLPASLKVYG TVFHINHGNP FNLKAVVDKW PDFNTVVVCP QEQDMTDDLD HYTNTYQIYS KDPQNCQEFL GSPELINWKQ HLQIQSSQPS LNEAIQNLAA IKSFKVKQTQ RILYMAAETA KELTPFLLKS KILSPSGGKP KAINQEMFKL SSMDVTHAHL VNKFWHFGGN ERSQRFIERC IQTFPTCCLL GPEGTPVCWD LMDQTGEMRM AGTLPEYRLH GLVTYVIYSH AQKLGKLGFP VYSHVDYSNE AMQKMSYTLQ HVPIPRSWNQ WNCVPL.

    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.

    Glyat Human
  • View Data Sheet

    Name :

    HaeIII

    Description:

    HaeIII Recombinant

    site-specific DNA-methyltransferase, HaeIVRM.

    Product # :

    ENZ-1203

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    Description

    HaeIII is a prokaryotic DNA that protects organisms from an unknown DNA. HaeIII’s recognition site is the GGCC nucleotide sequence which means it cleaves DNA at the site 5′-GG/CC-3.

    Source

    E. coli that carries the HaeIII gene from Haemophilus aegypticus

    Purity

    Great than 95 % as estimated by SDS-PAGE analyses.

    More Info

    • Synonyms

      site-specific DNA-methyltransferase, HaeIVRM.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Background

      HaeIII cleaves the DNA at the positions where the GGCC sequence is found. The cleavage happens between the 2nd and the third nucleotides -G and C. The resulting DNA fragments are known as restriction fragments. HaeIII cuts both strands of DNA in the same location, creating restriction fragments with blunt ends.

    • Storage Buffer

      10mM Tris-HCl (pH 7.4), 1 mM DTT, 50% (v/v) glycerol, 0.1mM EDTA, 50 mM KCl and 200µg/ml BSA.

    • Unit Definition

      1 unit is defined as the amount of HaeIII required to digest 1 µg of lambda DNA in 1 hour at 37°C in 50 µL of recommended reaction buffer.

    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.

    Haeiii Enzyme
  • View Data Sheet

    Name :

    ELANE Mouse

    Description:

    Elastase-2 Mouse Recombinant

    Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    Product # :

    ENZ-1105

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    Description

    ELANE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (27-265a.a.) fused to a 6 aa His Tag at C-terminus containing 245 amino acids and having a molecular mass of 26.8kDa.ELANE shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    ELANE protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 30% Glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elastase-2 (ELANE) is a serine protease that belongs to the chymotrypsin family. ELANE breaks down elastin, an elastic fiber together with collagen and controls the mechanical properties of connective tissue. The neutrophil form breaks down the Outer membrane protein A (OmpA) of E. coli and other Gram-negative bacteria. ELANEis inhibited by the acute-phase protein alpha 1-antitrypsin (A1AT), which binds almost irreversibly to the active site of elastase and trypsin.A1AT is usually secreted by the liver cells into the serum. A1AD leads to uninhibited destruction of elastic fiber by elastase.

    • Synonyms

      Elane, Ela2, F430011M15Rik, NE, Neutrophil elastase, Elastase-2, Leukocyte elastase.

    • 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

      SEIVGGRPAR PHAWPFMASL QRRGGHFCGA TLIARNFVMS AAHCVNGLNF RSVQVVLGAH
      DLRRQERTRQ TFSVQRIFEN GFDPSQLLND IVIIQLNGSA TINANVQVAQ LPAQGQGVGD
      RTPCLAMGWG RLGTNRPSPS VLQELNVTVV TNMCRRRVNV CTLVPRRQAG ICFGDSGGPL
      VCNNLVQGID SFIRGGCGSG LYPDAFAPVA EFADWINSII RSHNDHLLTH PKDREGRTNH HHHHH

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    Elastase 2 Mouse
  • View Data Sheet

    Name :

    PPP1CC Human, Active

    Description:

    Protein Phosphatase 1, Catalytic Subunit Gamma Human Recombinant, Active

    Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.

    Product # :

    ENZ-1042

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    Description

    PPP1CC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323a.a.) and having a molecular mass of 39.1kDa.PPP1CC is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PPP1CC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 2mM DTT and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 700 units/mg, and is defined as the amount of enzyme that hydrolyzes 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      PPP1CC is vital for cell division and takes part in the regulation of protein synthesis, muscle contractility and glycogen metabolism. Additionally, PPP1CC has a role in long-term synaptic plasticity and regulation of ionic conductance, and has a significant role in dephosphorylating substrates such as the postsynaptic density-associated Ca2+/calmodulin dependent protein kinase II.

    • Synonyms

      Protein phosphatase 1 catalytic subunit gamma isozyme/isoform, Protein phosphatase 1C catalytic subunit, serine/threonine phosphatase 1 gamma, serine/threonine-protein phosphatase PP1-gamma catalytic subunit, PP1gamma, PPP1G, EC 3.1.3.16.

    • 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 MADLDKLNID SIIQRLLEVR GSKPGKNVQL QENEIRGLCL KSREIFLSQP ILLELEAPLK ICGDIHGQYY DLLRLFEYGG FPPESNYLFL GDYVDRGKQS LETICLLLAY KIKYPENFFL LRGNHECASI NRIYGFYDEC KRRYNIKLWK TFTDCFNCLP IAAIVDEKIF CCHGGLSPDL QSMEQIRRIM RPTDVPDQGL LCDLLWSDPD KDVLGWGEND RGVSFTFGAE VVAKFLHKHD LDLICRAHQV VEDGYEFFAK RQLVTLFSAP NYCGEFDNAG AMMSVDETLM CSFQILKPAE KKKPNATRPV TPPRGMITKQ AKK.

    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.

    Ppp1Cc Human Active
  • View Data Sheet

    Name :

    KRT18 Human, His

    Description:

    Cytokeratin 18 Human Recombinant , His Tag

    Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 protein.

    Product # :

    PRO-484

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    Description

    KRT18 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a calculated molecular mass of 52.42kDa.The KRT18 is fused to a His Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT18 protein solution (0.8mg/ml) contains 20mM Tris pH 8, 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KRT18 encodes the type I intermediate filament chain keratin 18. Keratin 18, together with its filament partner keratin 8, are perhaps the most commonly found members of the intermediate filament gene family. They are expressed in single layer epithelial tissues of the body. Mutations in this gene have been linked to cryptogenic cirrhosis. Two transcript variants encoding the same protein have been found for this gene.

    • Synonyms

      Keratin type I cytoskeletal 18, Cytokeratin-18, CK-18, Keratin-18, K18, KRT18,CYK18,Cell proliferation-inducing gene 46 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. Please avoid freeze thaw cycles.

    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.

    Krt18 Human His
  • View Data Sheet

    Name :

    DARS Human

    Description:

    Aspartyl-tRNA Synthetase Human Recombinant

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

    Product # :

    ENZ-591

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    Description

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

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Dars Human
  • View Data Sheet

    Name :

    DNase Human

    Description:

    Deoxyribonuclease I Human Recombinant

    EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.

    Product # :

    ENZ-319

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    Description

    Deoxyribonuclease I Human Recombinant produced in CHO is a glycosylated, polypeptide chain containing 260 amino acids and having a total molecular mass of 37,000 Dalton with a molecular formula of C1321H1999N339O396S9. DNase is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    Each mg contains 150 µg calcium chloride dehydrate and 8.77 mg NaCl.

    More Info

    • Introduction

      Deoxyribonuclease I Human Recombinant (rhDNase), an enzyme which selectively cleaves DNA. Recombinant Human Dnase is an endonuclease enzyme which splits phosphodiester linkages within polynucleotides, acting primarely on single stranded DNA (ssDNA), double stranded DNA (ddDNA) and chromatin. Dnase is activated by bivalent metals such as Mg+2 and Ca+2 .
      Dnase enzymes are common reagents used in biochemical methods requiring diestion of DNA and recovery of RNA, or where DNA is to be removed without affecting structural proteins or enzymes. Dnase enzymes are also used in tissue culture to digest DNA from damaged cells, resulting in reduced viscosity, and for removal of membrane-bound DNA fragments.

    • Synonyms

      EC 3.1.21.1, Deoxyribonuclease I, DNase I, DNL1, DRNI, FLJ38093, DNASE1.

    • Physical Appearance

      Sterile liquid colorless solution at a concentration of 1mg/ml.

    • Stability

      2 years when stored at 4°C, three weeks at 15°C, pH-6.3.

    • Unit Definition

      Dnase is generally assayed according to the photometric method developed by Kunitz. One Dnase unit results in an increase in absorbance at 260nm of 0.001/minute at 25°C when acting upon highly polymerized solution of DNA at pH-5. Also 0.005 Kunitz unit digests 1µgof lambda phage DNA in 10 minutes at 37°C in50mM Tris, 1mMMg++, pH 7.8 in a 50ul reaction.

    • Specific Activity

      1000IU/1mg.

    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.

    Dnase I Human
  • View Data Sheet

    Name :

    KLRK1 Human

    Description:

    Killer Cell lectin-Like Receptor Subfamily K, Member 1 Human Recombinant

    CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    Product # :

    PRO-1290

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    Description

    KLRK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 168 amino acids (73-216 a.a.) and having a molecular mass of 19.2kDa. KLRK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    KLRK1 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Killer Cell lectin-Like Receptor Subfamily K, Member 1 (KLRK1) is an activating receptor which has recently generated considerable interest. The most fascinating of these, are a couple of closely related proteins known as MICA and MICB. These are cell-surface molecules distantly related to MHC class I proteins, and their genes have elements of heat shock promoters. Thus, MICA and MICB are expressed in the course of cell stress and are up-regulated in tumor cells and during viral infections. This receptor-ligand combination has a crucial role in the immune response to various pathologies.

    • Synonyms

      CD314, D12S2489E, KLR, NKG2-D, NKG2D, Killer cell lectin-like receptor subfamily K member 1, NK cell receptor D, NKG2-D-activating NK receptor, CD314.

    • 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 MGSMIWSAVF LNSLFNQEVQ IPLTESYCGP CPKNWICYKN NCYQFFDESK NWYESQASCM SQNASLLKVY SKEDQDLLKL VKSYHWMGLV HIPTNGSWQW EDGSILSPNL LTIIEMQKGD CALYASSFKG YIENCSTPNT YICMQRTV.

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    Klrk1 Human
  • View Data Sheet

    Name :

    KRT16 Human

    Description:

    Cytokeratin 16 Human Recombinant

    Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    Product # :

    PRO-1899

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    Description

    KRT16 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 496 amino acids (1-473) and having a molecular mass of 53.7 kDa.KRT16 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The KRT16 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokeratin 16, also known as KRT16, is a member of the keratin gene family. KRT16 which acts as a regulator of innate immunity in response to skin barrier breach is required for some inflammatory checkpoint for the skin barrier maintenance. KRT16 is coexpressed with keratin 14 in a few epithelial tissues as esophagus, tongue, and hair follicles.

    • Synonyms

      Keratin, type I cytoskeletal 16, Cytokeratin 16, KRT16, Cytokeratin-16, CK-16, Keratin-16, K16, KRT16A, FNEPPK, K1CP, NEPPK.

    • 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 MGSMTTCSRQ FTSSSSMKGS CGIGGGIGGG SSRISSVLAG GSCRAPSTYG GGLSVSSRFS SGGACGLGGG YGGGFSSSSS FGSGFGGGYG GGLGAGFGGG LGAGFGGGFA GGDGLLVGSE KVTMQNLNDR LASYLDKVRA LEEANADLEV KIRDWYQRQR PSEIKDYSPY FKTIEDLRNK IIAATIENAQ PILQIDNARL AADDFRTKYE HELALRQTVE ADVNGLRRVL DELTLARTDL EMQIEGLKEE LAYLRKNHEE EMLALRGQTG GDVNVEMDAA PGVDLSRILN EMRDQYEQMA EKNRRDAETW FLSKTEELNK EVASNSELVQ SSRSEVTELR RVLQGLEIEL QSQLSMKASL ENSLEETKGR YCMQLSQIQG LIGSVEEQLA QLRCEMEQQS QEYQILLDVK TRLEQEIATY RRLLEGEDAH LSSQQASGQS YSSREVFTSS SSSSSRQTRP ILKEQSSSSF SQGQSS.

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    Krt16 Human
  • View Data Sheet

    Name :

    Troponin-C2 Human

    Description:

    Troponin-C2 Human Recombinant

    Troponin C, skeletal muscle, TNNC2.

    Product # :

    PRO-2572

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    Description

    Troponin-C2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 160 amino acids having a molecular mass of 18.1kDa. The Recombinant Human Troponin-C2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein (1mg/ml) contains 20 mM Tris-HCl buffer (pH 7.5), 1mM DTT, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Troponin-C2 (Troponin C, skeletal muscle) is the central regulatory antigen of striated muscle contraction, and modulates the Ca2+-activation characteristics of muscle fibers. Troponin-C2 has three subunits, Troponin I(Tn-1), Troponin T(Tn-T) and Troponin C(Tn-C). Tn-I subunit inhibits actomyosin ATPase and Tn-T subunit binds tropomyosin and Tn-C, while Tn-C subunit binds calcium and overcomes the inhibitory action of the troponin complex on actin filaments. Mutations in all components of this complex have been linked with skeletal muscle disease.

    • Synonyms

      Troponin C, skeletal muscle, TNNC2.

    • 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

      MTDQQAEARS YLSEEMIAEF KAAFDMFDAD GGGDISVKEL GTVMRMLGQT PTKEELDAII EEVDEDGSGT IDFEEFLVMM VRQMKEDAKG KSEEELAECF RIFDRNADGY IDPEELAEIF RASGEHVTDE EIESLMKDGD KNNDGRIDFD EFLKMMEGVQ.

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    Troponin C2
  • View Data Sheet

    Name :

    PSPH Human

    Description:

    Phosphoserine Phosphatase Human Recombinant

    Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.

    Product # :

    PKA-224

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    Description

    Phosphoserine Phosphatase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids and having a molecular mass of 25 kDa. PSP was overexpressed in E. coli and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Hepes pH 7.5, 1mM DTT &100mM KCl2.

    Purity

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

    More Info

    • Introduction

      Human Phosphoserine phosphatase (hPSP) is an important enzyme in the phosphorylated pathway of serine biosynthesis, which contributes a major portion of the endogenous L-serine. Similar to known L-3-phosphoserine phosphatases, it catalyzed the Mg2+-dependent hydrolysis of L-phosphoserine and an exchange reaction between L-serine and L-phosphoserine. Recently, its complex structures reveal that the open-closed environmental change of the active site, generated -helical bundle domain, is important to substrate by local rearrangement of the recognition and hydrolysis.

    • Synonyms

      Phosphoserine phosphatase, EC 3.1.3.3, PSP, O-phosphoserine phosphohydrolase, PSPase, L-3-phosphoserine phosphatase, PSPH.

    • 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

      MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE.

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    Psph Human
  • View Data Sheet

    Name :

    ACYP1 Human

    Description:

    Acylphosphatase 1 Human Recombinant

    Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1, ACYP1, ACYPE.

    Product # :

    ENZ-078

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    Description

    ACYP1 Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-99 a.a.) and having a molecular mass of 13.6kDa. The ACYP1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ACYP1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Erythrocyte acylphosphatase (ACYP1) is a cytosolic enzyme which catalyzes the hydrolysis of the carboxyl-phosphate bond of acylphosphates. There are two acylphophatase isoenzymes: ACYP1 and ACYP2. These isoenzymes share 60% homology and have the same substrate specificity, even though ACYP1 has a higher catalytic activity than ACYP2.

    • Synonyms

      Acylphosphatase-1, Acylphosphatase, erythrocyte isozyme, Acylphosphatase, organ-common type isozyme, Acylphosphate phosphohydrolase 1, ACYP1, ACYPE.

    • 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 MGSMAEGNTL ISVDYEIFGK VQGVFFRKHT QAEGKKLGLV GWVQNTDRGT VQGQLQGPIS KVRHMQEWLE TRGSPKSHID KANFNNEKVI LKLDYSDFQI VK.

    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.

    Acyp1 Human
  • View Data Sheet

    Name :

    Rhodanese Human

    Description:

    Thiosulfate Sulfurtransferase Human Recombinant

    EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    Product # :

    ENZ-459

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    Description

    Recombinant Human Rhodanese produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 35.6 kDa. Rhodanese is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The Rhodanese protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.

    • Synonyms

      EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.

    • 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 MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA.

    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.

    Rhodanese 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.

    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.

    Echs1 Human Active
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