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Search results

1000 results found for “enterokinase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    KLK3 Human, HEK

    Description:

    Kallikrein-3 Human Recombinant, HEK

    Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1

    Product # :

    ENZ-1149

    Price :

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    Description

    KLK3 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (18-261 a.a) containing a total of 250 amino acids, having a molecular mass of 27.6kDa.KLK3 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells.

    Formulation

    The KLK3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is  > 250pmol/min/ug. Defined by the amount of enzyme that cleaves 1pmole of Succinyl-ArgPro-Tyr-p-Nitroanilide to Succinyl-Arg-Pro-Tyr and p-Nitroanilide per minute at pH 7.5 at 37˚C.

    More Info

    • Introduction

      Kallikrein-3 or KLK3 is a serine proteases subgroup, enzymes can cleave peptide bonds. KLK3 is found in the prostate and may be hold accountable to the regulation of semen liquefaction via seminogelin hydrolysis. The protein is expressed in low concentrations in men with healthy prostates serum. When elevated quantities are found it may show prostate cancer or different prostate disorders such as prostatitis and benign prostatic hyperplasia.

    • Synonyms

      Prostate-specific antigen, PSA, Gamma-seminoprotein, Seminin, Kallikrein-3, P-30 antigen, Semenogelase, KLK3, APS, hK3, KLK2A1

    • 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

      APLILSRIVG GWECEKHSQP WQVLVASRGR AVCGGVLVHP QWVLTAAHCI RNKSVILLGR HSLFHPEDTG QVFQVSHSFP HPLYDMSLLK NRFLRPGDDS SHDLMLLRLS EPAELTDAVK VMDLPTQEPA LGTTCYASGW GSIEPEEFLT PKKLQCVDLH VISNDVCAQV HPQKVTKFML CAGRWTGGKS TCSGDSGGPL VCNGVLQGIT SWGSEPCALP ERPSLYTKVV HYRKWIKDTI VANPHHHHHH

    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.

    Kallikrein 3 Human
  • View Data Sheet

    Name :

    AKR1D1 Human

    Description:

    Aldo-Keto Reductase Family 1 Member D1 Human Recombinant

    3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.

    Product # :

    ENZ-931

    Price :

    Quantity :

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    Description

    AKR1D1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 326 amino acids (1-326 a.a.) and having a molecular mass of 37.3kDa. The AKR1D1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The AKR1D1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aldo-keto reductase family 1 member D1 (AKR1D1) belongs to the AKR superfamily. The AKR family proteins are soluble NADPH oxidoreductases, which have vital roles in the metabolism of drugs, carcinogens and reactive aldehydes. AKR1D1 is also responsible for the catalysis of the 5-beta-reduction of bile acid intermediates and steroid hormones that carry a delta (4)-3-1 structure. AKR1D1 is highly expressed in the liver, colon and testis. Deficiency of the AKR1D1 enzyme may contribute to hepatic dysfunction.

    • Synonyms

      3-oxo-5-beta-steroid 4-dehydrogenase, Aldo-Keto Reductase Family 1, Member D1, SRD5B1, Delta(4)-3-Ketosteroid 5-Beta-Reductase, Delta 4-3-Ketosteroid-5-Beta-Reductase, Delta(4)-3-Oxosteroid 5-Beta-Reductase, CBAS2, Steroid-5-Beta-Reductase, Beta Polypeptide 1 (3-Oxo-5 Beta-Steroid Delta 4-Dehydrogenase Beta 1), Aldo-Keto Reductase Family 1, Member D1 (Delta 4-3-Ketosteroid-5-Beta-Reductase), Aldo-Keto Reductase Family 1 Member D1, 3-Oxo-5-Beta-Steroid 4-Dehydrogenase, EC 1.3.1.3, 3o5bred.

    • 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

      MDLSAASHRI PLSDGNSIPI IGLGTYSEPK STPKGACATS VKVAIDTGYR HIDGAYIYQN EHEVGEAIRE KIAEGKVRRE DIFYCGKLWA TNHVPEMVRP TLERTLRVLQ LDYVDLYIIE VPMAFKPGDE IYPRDENGKW LYHKSNLCAT WEAMEACKDA GLVKSLGVSN FNRRQLELIL NKPGLKHKPV SNQVECHPYF TQPKLLKFCQ QHDIVITAYS PLGTSRNPIW VNVSSPPLLK DALLNSLGKR YNKTAAQIVL RFNIQRGVVV IPKSFNLERI KENFQIFDFS LTEEEMKDIE ALNKNVRFVE LLMWRDHPEY PFHDEY.

    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.

    Human Akr1D1
  • View Data Sheet

    Name :

    GOT1 Human, Active

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Human Recombinant, Active

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

    Product # :

    ENZ-1001

    Price :

    Quantity :

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    Description

    GOT1 Human Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-413 a.a.) and having a molecular mass of 48.4 kDa. The GOT1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GOT1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 50 units/mg, and is defined as the amount of enzyme that converts 1umole of a-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.

    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

      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 MAPPSVFAEV PQAQPVLVFK LTADFREDPD PRKVNLGVGA YRTDDCHPWV LPVVKKVEQK IANDNSLNHE YLPILGLAEF RSCASRLALG DDSPALKEKR VGGVQSLGGT GALRIGADFL ARWYNGTNNK NTPVYVSSPT WENHNAVFSA AGFKDIRSYR YWDAEKRGLD LQGFLNDLEN APEFSIVVLH ACAHNPTGID PTPEQWKQIA SVMKHRFLFP FFDSAYQGFA SGNLERDAWA IRYFVSEGFE FFCAQSFSKN FGLYNERVGN LTVVGKEPES ILQVLSQMEK IVRITWSNPP AQGARIVAST LSNPELFEEW TGNVKTMADR ILTMRSELRA RLEALKTPGT WNHITDQIGM FSFTGLNPKQ VEYLVNEKHI YLLPSGRINV SGLTTKNLDY VATSIHEAVT KIQ.

    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 Human Active
  • 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

    Price :

    Quantity :

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    • description
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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.

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

    Got2 Human Active
  • View Data Sheet

    Name :

    MME Human, Active

    Description:

    Membrane Metalloendopeptidase Human Recombinant, Active

    Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.

    Product # :

    ENZ-1116

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    Description

    MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.

    More Info

    • Introduction

      Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.

    • Synonyms

      Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.

    • 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

      ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH

    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.

    Mme Protein
  • View Data Sheet

    Name :

    CKBB Human, Active

    Description:

    Creatine Kinase Brain Human Recombinant, Active

    Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.

    Product # :

    CKI-268

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    Description

    CKBB Human Recombinant produced in Pichia Pastoris is a dimeric glycosylated full length polypeptide chain comprised of 2 identical B subunits and having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and having a Mw of 47kDa The CKBB is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    CKBB Human contains 10Mm Bis-Tris-HCl pH-6.0, 50% glycerol, 0.5mM EDTA and 0.5mM DTT.

    Purity

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

    Biological Activity

    The biological activity of CKBB was measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 854 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 1,171ng/ml.

    More Info

    • Introduction

      Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.

    • Synonyms

      Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.

    • Physical Appearance

      Sterile Filtered colourless liquid formulation.

    • Stability

      CKBB should be stored below -18°C. Please prevent 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.

    Ckbb Human
  • View Data Sheet

    Name :

    GPI Human, Active

    Description:

    Glucose-6-Phosphate Isomerase Human Recombinant, BioActive

    Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.

    Product # :

    ENZ-1148

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    Description

    GPIHuman Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 578 amino acids (1-558) and having a molecular mass of 65.3 kDa.GPI is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GPI solution (1 mg/ml) contains 10% Glycerol, 1mM DTT and 20mM Tris-HCl buffer (pH 8.0).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 400unit/mg.It is defined by the increase of NADPH in absorbance at 340 nm, resulting from the reduction of NADP. 1 unit will convert 1.0 umole of D-Fructose 6-phosphate to D-glucose 6- phosphate per minute at pH 7.4 at 37˚C.

    More Info

    • Introduction

      GPI or Glucose-6-phosphate isomerase, is a protein, part of the multifunctional phosphoglucose isomerase family, which its members take part in energy pathways. GPI is a dimeric enzyme that enhances the isomerization of glucose-6-phosphate and fructose-6- phosphate (both reversible). In mammals, GPI acts as an angiogenic factor & tumor-secreted cytokine. The enzyme also acts as a neurotrophic factor for spinal & sensory neurons.

    • Synonyms

      Glucose-6-phosphate isomerase, Autocrine motility factor, Neuroleukin, Phosphoglucose isomerase, Phosphohexose isomerase, Sperm antigen 36, GPI, AMF, GNPI, NLK, PGI, PHI, SA36, SA-36.

    • 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 MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ

    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.

    Gpi Enzyme
  • View Data Sheet

    Name :

    GPT Human

    Description:

    Glutamic-Pyruvate Transaminase Human Recombinant

    Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    Product # :

    ENZ-192

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    Description

    GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.

    • Synonyms

      Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.

    • 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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS

    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.

    Gpt Human
  • View Data Sheet

    Name :

    Y.Enterocolitica (O:9) YopB

    Description:

    Yersinia Enterocolitica (O:9) YopB Recombinant

    Protein YopD, pYV0054.

    Product # :

    PRO-2575

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    Description

    Recombinant Yersinia Enterocolitica (O:9) YopB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain having a calculated molecular mass of 43kDa. Y.Enterocolitica (O:9) YopB is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Y.Enterocolitica (O:9) YopB is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Gastroenteritis which has been identified as caused by Yersinia Enterocolitica has been discovered by virulent isolates of the bacteria. During infection, pores are being formed in the presence of adapter protein Yersiniosis. YopB's Interaction with the target membrane to form pores enables the entrance of YopE effectors to the cytoplasmic space of the host’s cell.

    • Synonyms

      Protein YopD, pYV0054.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Activity

      1. Binds IgG- and IgM-type human antibodies.2. Immunodot test with positive/negative samples.

    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.

    Yopb Protein
  • View Data Sheet

    Name :

    TRXR E.Coli

    Description:

    Thioredoxin Reductase E.Coli Recombinant

    TRXB, TRXR, Thioredoxin Reductase.

    Product # :

    ENZ-507

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    Description

    TRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    TRXR E.Coli solution containing 20mM Tris HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 4-5 units/ml, and was measured in a coupled assay with DTNB and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.

    More Info

    • Introduction

      TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.

    • Synonyms

      TRXB, TRXR, Thioredoxin Reductase.

    • 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

      MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.

    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.

    Trxr Ecoli
  • View Data Sheet

    Name :

    Aminopeptidase

    Description:

    Aminopeptidase Aeromonas Recombinant

    Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    Product # :

    ENZ-275

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    Description

    The 29 kDa Aeromonas Aminopeptidase is produced by genetic engineering and can be used for physical & structural investigations, sequence and amino-terminal determinations. This exopeptidase recognizes a specific stop sign at –X- Pro and requires a free a-amino group in the L-configuration. It is therefore suitable for the removal of the redundant N-terminal methionine often added to engineered recombinant proteins.

    Source

    Aeromonas Proteolytica.

    Formulation

    Buffered solution containing 10mM Tris-HCl, 100mM NaCl and 5µM ZnSO4, pH 8.0.

    Purity

    Greater than 95.0% as determined by SEC-HPLC.

    Biological Activity

    Recombinant Aeromonas Aminopeptidase was found to have an activity of 108 Units/mg protein.

    More Info

    • Synonyms

      Bacterial leucyl aminopeptidase, EC 3.4.11.10.

    • Physical Appearance

      Sterile filtered liquid formulation.

    • Stability

      Two years when stored at -20°C, 2 weeks at 4°C.

    • Unit Definition

      One unit of aminopeptidase activity is defined as the amount of enzyme that releases 1 μmole p-nitroaniline at 25°C in 1 minute.

    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.

    Aminopeptidase
  • View Data Sheet

    Name :

    IDE Human

    Description:

    Insulin-Degrading Enzyme Human Recombinant

    Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.

    Product # :

    ENZ-813

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    Description

    IDE Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Leu1019) containing 1026 amino acids including a 7 aa His tag at C-terminus. The total calculated molecular mass is 119kDa.

    Source

    Escherichia Coli.

    Formulation

    IDE filtered (0.4µm) in 20mM Tris buffer, 50mM NaCl, pH 8.0 and 10% (w/v) glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Insulin-Degrading Enzyme (IDE) is a zinc metallopeptidase which degrades intracellular insulin, and thus terminates insulins activity, as well as playing a part in intercellular peptide signaling by degrading various peptides such as amylin, bradykinin, and kallidin. The preferential affinity of the IDE enzyme for insulin results in insulin-mediated inhibition of the degradation of additional peptides such as beta-amyloid. Deficiencies in IDE protein's function are linked with Alzheimer's disease and type 2 diabetes mellitus nevertheless mutations in the IDE gene have not been demonstrated to be causative for these diseases. Insulin-Degrading Enzyme localizes mainly to the cytoplasm however in some cell types it localizes to the extracellular space, cell membrane, peroxisome, and mitochondrion. In addition, IDE degrades amyloid formed by APP and IAPP. Furthermore, IDE plays a part in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.

    • Synonyms

      Insulin-Degrading Enzyme, Abeta-Degrading Protease, Insulin Protease, EC 3.4.24.56, Insulinase, INSULYSIN, Insulysin, EC 3.4.24, IDE.

    • 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

      MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAAL DVHIGSLSDP PNIAGLSHFC EHMLFLGTKK YPKENEYSQF LSEHAGSSNA FTSGEHTNYY FDVSHEHLEG ALDRFAQFFL CPLFDESCKD REVNAVDSEH EKNVMNDAWR LFQLEKATGN PKHPFSKFGT GNKYTLETRP NQEGIDVRQE LLKFHSAYYS SNLMAVCVLG RESLDDLTNL VVKLFSEVEN KNVPLPEFPE HPFQEEHLKQ LYKIVPIKDI RNLYVTFPIP DLQKYYKSNP GHYLGHLIGH EGPGSLLSEL KSKGWVNTLV GGQKEGARGF MFFIINVDLT EEGLLHVEDI ILHMFQYIQK LRAEGPQEWV FQECKDLNAV AFRFKDKERP RGYTSKIAGI LHYYPLEEVL TAEYLLEEFR PDLIEMVLDK LRPENVRVAI VSKSFEGKTD RTEEWYGTQY KQEAIPDEVI KKWQNADLNG KFKLPTKNEF IPTNFEILPL EKEATPYPAL IKDTAMSKLW FKQDDKFFLP KACLNFEFFS PFAYVDPLHC NMAYLYLELL KDSLNEYAYA AELAGLSYDL QNTIYGMYLS VKGYNDKQPI LLKKIIEKMA TFEIDEKRFE IIKEAYMRSL NNFRAEQPHQ HAMYYLRLLM TEVAWTKDEL KEALDDVTLP RLKAFIPQLL SRLHIEALLH GNITKQAALG IMQMVEDTLI EHAHTKPLLP SQLVRYREVQ LPDRGWFVYQ QRNEVHNNCG IEIYYQTDMQ STSENMFLEL FCQIISEPCF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQALA IRRLDKPKKL SAECAKYWGE IISQQYNFDR DNTEVAYLKT LTKEDIIKFY KEMLAVDAPR RHKVSVHVLA REMDSCPVVG EFPCQNDINL SQAPALPQPE VIQNMTEFKR GLPLFPLVKP HINFMAAKL E HHHHHH.

    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
  • View Data Sheet

    Name :

    Welqut Protease

    Description:

    Welqut Protease Staphylococcus aureus Recombinant

    Product # :

    ENZ-1113

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Unit Definition

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

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

    Welqut Protease
  • View Data Sheet

    Name :

    TSEN15 Human

    Description:

    tRNA Splicing Endonuclease 15 Human Recombinant

    tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.

    Product # :

    PRO-144

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    Description

    TSEN15 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids (1-171 a.a.) and having a molecular mass of 20.9kDa. The TSEN15 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TSEN15 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      tRNA-splicing endonuclease subunit Sen15 (TSEN15) is a member of the SEN15 family. tRNA splicing is an essential process required for cell growth and division. TSEN15 is a subunit of the tRNA splicing endonuclease. TSEN15 cleaves pre-tRNA at the 5' and 3' splice sites to release the intron.

    • Synonyms

      tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.

    • 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 MEERGDSEPT PGCSGLGPDG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM ELDIGDATHV YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE GLQTVVPTPI TASLSHNRIR EILKASRKLQ GDPDLPMSFT LAIVESDSTI VYYKLTDGFM LPDPQNISLR R.

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    Tsen15 Human
  • View Data Sheet

    Name :

    CSNK2A2 Human

    Description:

    Casein Kinase 2, Alpha 2 Prime Human Recombinant

    Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.

    Product # :

    PKA-042

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    Description

    CSNK2A2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 374 amino acids (1-350 a.a) and having a molecular mass of 43.7kDa. CSNK2A2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    CSNK2A2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Casein kinase 2 subunit alpha (CSNK2A2) controls numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. CSNK2A2 protein functions as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response.

    • Synonyms

      Casein Kinase 2, Alpha Prime Polypeptide, CK II Alpha, EC 2.7.11.1, CK2A2, EC 2.7.11, CSNK2A1, Casein kinase II subunit alpha'.

    • 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 MGSHMPGPAA GSRARVYAEV NSLRSREYWD YEAHVPSWGN QDDYQLVRKL GRGKYSEVFE AINITNNERV VVKILKPVKK KKIKREVKIL ENLRGGTNII KLIDTVKDPV SKTPALVFEY INNTDFKQLY QILTDFDIRF YMYELLKALD YCHSKGIMHR DVKPHNVMID HQQKKLRLID WGLAEFYHPA QEYNVRVASR YFKGPELLVD YQMYDYSLDM WSLGCMLASM IFRREPFFHG QDNYDQLVRI AKVLGTEELY GYLKKYHIDL DPHFNDILGQ HSRKRWENFI HSENRHLVSP EALDLLDKLL RYDHQQRLTA KEAMEHPYFY PVVKEQSQPC ADNAVLSSGL TAAR.

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    Csnk2A2 Human
  • View Data Sheet

    Name :

    HYKK Human

    Description:

    Hydroxylysine Kinase Human Recombinant

    Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 1.

    Product # :

    PKA-064

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    Description

    HYKK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 396 amino acids (1-373a.a) and having a molecular mass of 44.3kDa.HYKK is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    HYKK solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 40% glycerol, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hydroxylysine Kinase, also known as HYKK, is a Protein Coding gene. HYKK which is a part of the aminoglycoside phosphotransferase family catalyzes the GTPdependent phosphorylation of 5-hydroxy-L-lysine.

    • Synonyms

      Hydroxylysine kinase, AGPHD1, 5-hydroxy-L-lysine kinase, HYKK, Aminoglycoside phosphotransferase domain-containing protein 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 MGSMSSGNYQ QSEALSKPTF SEEQASALVE SVFGLKVSKV RPLPSYDDQN FHVYVSKTKD GPTEYVLKIS NTKASKNPDL IEVQNHIIMF LKAAGFPTAS VCHTKGDNTA SLVSVDSGSE IKSYLVRLLT YLPGRPIAEL PVSPQLLYEI GKLAAKLDKT LQRFHHPKLS SLHRENFIWN LKNVPLLEKY LYALGQNRNR EIVEHVIHLF KEEVMTKLSH FRECINHGDL NDHNILIESS KSASGNAEYQ VSGILDFGDM SYGYYVFEVA ITIMYMMIES KSPIQVGGHV LAGFESITPL TAVEKGALFL LVCSRFCQSL VMAAYSCQLY PENKDYLMVT AKTGWKHLQQ MFDMGQKAVE EIWFETAKSY ESGISM.

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    Hykk Human
  • View Data Sheet

    Name :

    melA E. coli

    Description:

    Alpha-Galactosidase E.coli Recombinant

    Mel-7, Alpha-galactosidase, b4119, JW4080.

    Product # :

    ENZ-609

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    Description

    melA E. coli Recombinant produced in E. coli is a single polypeptide chain containing 474 amino acids (1-451) and having a molecular mass of 53.0kDa.melA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      melA is a member of the glycosyl hydrolase 4 family. melA catalyze the hydrolysis of saccharides containing o-1,6,-galactoside bonds. melA catalyze the same reaction in E.coli, human and yeast but is found in different cellular sections: The E.coli melA is a cytoplasmic protein and the human and yeast melA are secretory proteins. Thus, even though the active enzyme from all three species has almost an equal molecular weight, structural resemblances, as well as dissimilarities, are probable.

    • Synonyms

      Mel-7, Alpha-galactosidase, b4119, JW4080.

    • 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 MGSMMSAPKI TFIGAGSTIF VKNILGDVFH REALKTAHIA LMDIDPTRLE ESHIVVRKLM DSAGASGKIT CHTQQKEALE DADFVVVAFQ IGGYEPCTVT DFEVCKRHGL EQTIADTLGP GGIMRALRTI PHLWQICEDM TEVCPDATML NYVNPMAMNT WAMYARYPHI KQVGLCHSVQ GTAEELARDL NIDPATLRYR CAGINHMAFY LELERKTADG SYVNLYPELL AAYEAGQAPK PNIHGNTRCQ NIVRYEMFKK LGYFVTESSE HFAEYTPWFI KPGREDLIER YKVPLDEYPK RCVEQLANWH KELEEYKKAS RIDIKPSREY ASTIMNAIWT GEPSVIYGNV RNDGLIDNLP QGCCVEVACL VDANGIQPTK VGTLPSHLAA LMQTNINVQT LLTEAILTEN RDRVYHAAMM DPHTAAVLGI DEIYALVDDL IAAHGDWLPG WLHR.

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    melA E. coli
  • View Data Sheet

    Name :

    GUK1 Human, Active

    Description:

    Guanylate Kinase 1 Human Recombinant, Active

    GMK, GMP kinase.

    Product # :

    PKA-309

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    Description

    GUK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (1-197 a.a.)and having a total molecular mass of 23.9 kDa. GUK1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GUK1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 100 units/mg and is defined as the amount of enzyme that convert 1.0 umole of GMP and ATP to GDP and ADP per minute at pH 7.5 at 37C in coupled system with PK/LDH.

    More Info

    • Introduction

      GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.

    • Synonyms

      GMK, GMP kinase.

    • Physical Appearance

      Sterile Filtered colorless clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA.

    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.

    Guk1 Human Active
  • View Data Sheet

    Name :

    ENTPD3 Human

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant

    Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    Product # :

    ENZ-844

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    Description

    ENTPD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (44-485 a.a) and having a molecular mass of 52kDa. ENTPD3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ENTPD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.

    • Synonyms

      Ectonucleoside Triphosphate Diphosphohydrolase 3, CD39L3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, HB6, NTPDase-3.

    • 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 MGSQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPP.

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    Entpd3 Human
  • View Data Sheet

    Name :

    ARG1 Human

    Description:

    Arginase-1 Human Recombinant

    EC 3.5.3.1, Arginase 1, Type I Arginase, Liver-Type Arginase.

    Product # :

    ENZ-517

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    Description

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

    Source

    Escherichia Coli.

    Formulation

    ARG1 Human protein solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARG1 catalyzes the hydrolysis of arginine to ornithine and urea. 2 isoforms of mammalian arginase exist which vary in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic role. ARG1 is a cytosolic enzyme and expressed widely in the liver as part of the urea cycle. Inherited deficiency of this ARG1 causes argininemia, which is an autosomal recessive disorder characterized by hyperammonemia.

    • Synonyms

      EC 3.5.3.1, Arginase 1, Type I Arginase, Liver-Type Arginase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Arg1 Human
  • View Data Sheet

    Name :

    KLK1 Human, HEK

    Description:

    Kallikrein-1 Human Recombinant, HEK

    KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.

    Product # :

    ENZ-293

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    Description

    KLK1 Human Recombinant produced in HEK293 cells is a single, glycosylated, polypeptide chain containing 244 amino acids ( Pro19-Ser262 ).KLK-1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 cells

    Formulation

    Provided as a solution in 20mM TrisHCl, 150mM NaCl, 2mM CaCl2, pH- 8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Kallikreins are serine protease enzymes having various physiological functions.
      Kallikreins are implicated in carcinogenesis and have potenital as novel cancer disease biomarkers. KLK1 is one of the fifteen kallikrein subfamily members located in a cluster on chromosome 19. KLK1 is functionally conserved in its ability to release the vasoactive peptide, Lys-bradykinin, from low molecular weight kininogen.
      Human Kallikrein-1, also called as Kallidinogenase, Kininogenase or Kininogenin, is an active protein enzyme present in saliva, pancreatic juices, and urine that catalyzes the proteolysis of bradykininogen to bradykinin.
      Kallikrein-1, which derived from human or porcine, have been used as drugs for a long time, they are mainly used in the treatment f light to medium hypertension and occlusion of cerebral and surrounding blood vessels.
      KLK1 demonstrates both trypsin- and chymotrypsin-like selectivities with Tyr/Arg preferred at site P1, Ser/Arg strongly preferred at P1', and Phe/Leu at P2.
      rs5517 in the KLK1 gene is considerably connected with hypertension in a Chinese Han population. KLK1 is expressed de novo in endothelial cells and mediates relaxation of human umbilical veins. The K allele of KLK1 promoter and TT genotype of TGF-beta1 are a genetic KLK1 -130 GN and -128 G-C, and the defenselessness factor contributing to progressive renal descent in Taiwanese primary vesicoureteric reflux children.
      Induction of KLK1 in carotid arteriosclerosis doesn’t lead to kallikrein-kinins pathway activation. Transgenic rats expressing KLK1 have impaired renal response to acute volume expansion Endothelial cells synthesize and release active form of KLK1on the surface which is important function in maintenance of circulation homeostasis.
      KLK1 participates in epidermal desquamation through cleavage of desmoglein 1 and regulation by lympho-epithelial Kazal-type-related inhibitor (LEKTI).

    • Synonyms

      KLK1, KLK-1, HK1, HK-1, KLKR, KLK6, Tissue Kallikrein, hKLK1, EC 3.4.21.35, Kidney/pancreas/salivary gland kallikrein, Kallikrein-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store KLK1 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.

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    Klk 1 Human
  • View Data Sheet

    Name :

    ARG2 Human

    Description:

    Arginase Type II Human Recombinant

    Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.

    Product # :

    ENZ-526

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    Description

    ARG2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (23-354 a.a.) and having a molecular mass of 38.3 kDa. The ARG2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARG2 Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARG2 participates in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, ARG2 takes part in both male and female sexual arousal and therefore a potential target for the treatment of male and female sexual arousal disorders.

    • Synonyms

      Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.

    • 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 MVHSVAVIGA PFSQGQKRKG VEHGPAAIRE AGLMKRLSSL GCHLKDFGDL SFTPVPKDDL YNNLIVNPRS VGLANQELAE VVSRAVSDGY SCVTLGGDHS LAIGTISGHA RHCPDLCVVW VDAHADINTP LTTSSGNLHG QPVSFLLREL QDKVPQLPGF SWIKPCISSA SIVYIGLRDV DPPEHFILKN YDIQYFSMRD IDRLGIQKVM ERTFDLLIGK RQRPIHLSFD IDAFDPTLAP ATFTPVVGGL TYREGMYIAE EIHNTGLLSA LDLVEVNPQL ATSEEEAKTT ANLAVDVIAS SFGQTREGGH IVYDQLPTPS SPDESENQAR VRI.

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    Arg2 Human
  • View Data Sheet

    Name :

    MSRB E.Coli

    Description:

    Methionine Sulfoxide Reductase B E.Coli Recombinant

    Peptide methionine sulfoxide reductase MsrB, Peptide-methionine (R)-S-oxide reductase, msrB, yeaA, b1778, JW1767.

    Product # :

    ENZ-124

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    Description

    MSRB produced in E.Coli is a single, non-glycosylated polypeptide chain containing 157 amino acids (1-137 a.a.) and having a molecular mass of 17.6kDa.MSRB is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Methionine sulfoxide reductase B (MsrB) from Escherichia coli is a member of the msrB Met sulfoxide reductase family. The E.coli msrB carries out the reduction of methionine-R-sulfoxide to methionine. msrB possess a metal binding site composed of 2 CXXC motifs. The bound metal (zinc or iron) may stabilize the conformation of the enzymes.

    • Synonyms

      Peptide methionine sulfoxide reductase MsrB, Peptide-methionine (R)-S-oxide reductase, msrB, yeaA, b1778, JW1767.

    • 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 MANKPSAEEL KKNLSEMQFY VTQNHGTEPP FTGRLLHNKR DGVYHCLICD APLFHSQTKY DSGCGWPSFY EPVSEESIRY IKDLSHGMQR IEIRCGNCDA HLGHVFPDGP QPTGERYCVN SASLRFTDGE NGEEING.

    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.

    Msrb Ecoli
  • View Data Sheet

    Name :

    MECR Human

    Description:

    Mitochondrial Trans-2-Enoyl-CoA Reductase Human Recombinant

    NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.

    Product # :

    ENZ-533

    Price :

    Quantity :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    MECR Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 341 amino acids (54-373 a.a.) and having a molecular mass of 49.8 kDa. The MECR is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MECR Human solution containing 20mM Trsi pH-8, 0.2M NaCl, 5mM DTT & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MECR catalyzes the reduction of trans-2-enoyl-CoA to acyl-CoA with chain length from C6 to C16 in an NADPH dependent manner with preference to medium chain length substrate. MECR protein takes part in the mitochondrial synthesis of fatty acids.

    • Synonyms

      NRBF1, CGI-63, FASN2B, EC 1.3.1.38, MECR, Mitochondrial Trans-2-Enoyl-CoA Reductase.

    • 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 MPAKVVELKN LELAAVRGSD VRVKMLAAPI NPSDINMIQG NYGLLPELPA VGGNEGVAQV VAVGSNVTGL KPGDWVIPAN AGLGTWRTEA VFSEEALIQV PSDIPLQSAA TLGVNPCTAY RMLMDFEQLQ PGDSVIQNAS NSGVGQAVIQ IAAALGLRTI NVVRDRPDIQ KLSDRLKSLG AEHVITEEEL RRPEMKNFFK DMPQPRLALN CVGGKSSTEL LRQLARGGTM VTYGGMAKQP VVASVSLLIF KDLKLRGFWL SQWKKDHSPD QFKELILTLC DLIRRGQLTA PACSQVPLQD YQSALEASMK PFISSKQILT M.

    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.

    Mecr Human
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