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Search results

1000 results found for “enolase”

Name

Description

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  • View Data Sheet

    Name :

    TPST2 Human

    Description:

    Tyrosylprotein Sulfotransferase 2 Human Recombinant

    Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.

    Product # :

    ENZ-707

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    Description

    TPST2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 375 amino acids (26-377) and having a molecular mass of 41kDa.TPST2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TPST2 solution (0.5mg/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

      Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.

    • Synonyms

      Protein-tyrosine sulfotransferase 2, EC 2.8.2.20, Tyrosylprotein sulfotransferase 2, TPST-2, TPST2, TANGO13B.

    • 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 MGSQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSS.

    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.

    Tpst2 Human
  • View Data Sheet

    Name :

    BLMH Mouse

    Description:

    Bleomycin Hydrolase Mouse Recombinant

    BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    Product # :

    ENZ-1109

    Price :

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    Description

    BLMH Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 478 amino acids (1-455 aa) and having a molecular mass of 54.9 kDa.BLMH is fused to a 23 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BLMH solution (0.25 mg/ml) contains 1mM DTT, 30% Glycerol, 20mM Tris-HCl(pH8.0) and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 1,500 pmole/min/ug. Measured by hydrolysis of 1pmole of Met-AMC to Methionine and AMC per minute at pH7.5 at 37C˚.

    More Info

    • Introduction

      BLMH is affiliate to the papain superfamily of the cysteine protease and the peptidase C1 family. BLMH is a cytoplasmic cysteinepeptidase usually found as a homohexamer. BLMH shields normal and malignant cells from the glycopeptide antitumor drug BLM. BLMH catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxyamide bond of its B-aminoalaninamide moiety and in addition demonstrates general aminopeptidase activity.

    • Synonyms

      BMH, BH, BLM hydrolase, Bleomycin Hydrolase.

    • 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 MGSMNNAGLN SEKVSALIQK LNSDPQFVLA QNVGTTHDLL
      DICLRRATVQ GAQHVFQHVV PQEGKPVTNQ KSSGRCWIFS CLNVMRLPFM KKFNIEEFEF
      SQSYLFFWDK VERCYFFLNA FVDTAQKKEP EDGRLVQYLL MNPTNDGGQW DMLVNIVEKY
      GVVPKKCFPE SHTTEATRRM NDILNHKMRE FCIRLRNLVH SGATKGEISS TQDAMMEEIF
      RVVCICLGNP PETFTWEYRD KDKNYHKIGP ITPLQFYKEH VKPLFNMEDK ICFVNDPRPQ
      HKYNKLYTVD YLSNMVGGRK TLYNNQPIDF LKKMVAASIK DGEAVWFGCD VGKHFNGKLG
      LSDMNVYDHE LVFGVSLKNM NKAERLAFGE SLMTHAMTFT AVSEKDNQEG TFVKWRVENS
      WGEDHGHKGY LCMTDEWFSE YVYEVVVDKK HVPEEVLAVL EQEPIVLPAW DPMGALAE

    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.

    Blmh Mouse
  • View Data Sheet

    Name :

    DHODH Human

    Description:

    Dihydroorotate Dehydrogenase Human Recombinant

    Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.

    Product # :

    ENZ-642

    Price :

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    • purity
    • More Info

    Description

    DHODH Human Recombinant produced in E. coli is a single polypeptide chain containing 390 amino acids (31-395) and having a molecular mass of 42.3 kDa.DHODH is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The DHODH solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Dihydroorotate dehydrogenase quinone (DHODH) is a member of the dihydroorotate dehydrogenase family. DHODH is a mitochondrial protein found on the outer surface of the inner mitochondrial membrane. DHODH catalyzes the 4th enzymatic step, the ubiquinone-mediated oxidation of dihydroorotate to orotate (with quinone as electron acceptor), in de novo pyrimidine biosynthesis. DHODH gene defects cause the postaxial acrofacial dysostosis (POADS), also known as Miller syndrome.

    • Synonyms

      Dihydroorotate dehydrogenase (quinone), Dihydroorotate oxidase, human complement of yeast URA1, DHOdehase, POADS, EC 1.3.5.2, EC 1.3.3.1.

    • 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

      GSSHHHHHH SSGLVPRGSH MGSHMTGDER FYAEHLMPTL QGLLDPESAH RLAVRFTSLG LLPRARFQDS DMLEVRVLGH KFRNPVGIAA GFDKHGEAVD GLYKMGFGFV EIGSVTPKPQ EGNPRPRVFR LPEDQAVINR YGFNSHGLSV VEHRLRARQQ KQAKLTEDGL PLGVNLGKNK TSVDAAEDYA EGVRVLGPLA DYLVVNVSSP NTAGLRSLQG KAELRRLLTK VLQERDGLRR VHRPAVLVKI APDLTSQDKE DIASVVKELG IDGLIVTNTT VSRPAGLQGA LRSETGGLSG KPLRDLSTQT IREMYALTQG RVPIIGVGGV SSGQDALEKI RAGASLVQLY TALTFWGPPV VGKVKRELEA LLKEQGFGGV TDAIGADHRR.

    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.

    Dhodh Human
  • View Data Sheet

    Name :

    MGAT2 Human

    Description:

    Mannoside Acetylglucosaminyltransferase 2 Human Recombinant

    Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    Product # :

    ENZ-781

    Price :

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    Description

    MGAT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (30-447a.a) and having a molecular mass of 50kDa. MGAT2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MGAT2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Mannoside Acetylglucosaminyltransferase 2 (MGAT2) is a golgi enzyme catalyzing an vital step in the conversion of oligomannose to complex N-glycans. MGAT2 enzyme has the characteristic glycosyltransferase domains: a short N-terminal cytoplasmic domain, a hydrophobic non-cleavable signal-anchor domain, and a C-terminal catalytic domain. MGAT2 gene mutations may lead to carbohydrate-deficient glycoprotein syndrome, type II.

    • Synonyms

      Mannosyl (Alpha-1,6-)-Glycoprotein Beta-1,2-N-Acetylglucosaminyltransferase, GlcNAc-T II, Mannoside Acetylglucosaminyltransferase 2, GNT-II, Beta-1,2-N-Acetylglucosaminyltransferase II, N-Glycosyl-Oligosaccharide-Glycoprotein N-Acetylglucosaminyltransferase II, EC 2.4.1.143, CDG2A, CDGS2, GLCNACTI, NT2, Alpha-1,6-Mannosyl-Glycoprotein 2-Beta-N-Acetylglucosaminyltransferase, UDP-N-Acetylglucosamine:Alpha-6-D-Mannoside, Beta-1,2-N-Acetylglucosaminyltransferase II.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MRQRKNEALA PPLLDAEPAR GAGGRGGDHP SVAVGIRRVS NVSAASLVPA VPQPEADNLT LRYRSLVYQL NFDQTLRNVD KAGTWAPREL VLVVQVHNRP EYLRLLLDSL RKAQGIDNVL VIFSHDFWST EINQLIAGVN FCPVLQVFFP FSIQLYPNEF PGSDPRDCPR DLPKNAALKL GCINAEYPDS FGHYREAKFS QTKHHWWWKL HFVWERVKIL RDYAGLILFL EEDHYLAPDF YHVFKKMWKL KQQECPECDV LSLGTYSASR SFYGMADKVD VKTWKSTEHN MGLALTRNAY QKLIECTDTF CTYDDYNWDW TLQYLTVSCL PKFWKVLVPQ IPRIFHAGDC GMHHKKTCRP STQSAQIESL LNNNKQYMFP ETLTISEKFT VVAISPPRKN GGWGDIRDHE LCKSYRRLQ.

    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.

    Mgat2 Human
  • View Data Sheet

    Name :

    NMT1 Human

    Description:

    N-Myristoyltransferase 1 Human Recombinant

    N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 1.

    Product # :

    ENZ-842

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    Description

    NMT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 519 amino acids (1-496 a.a) and having a molecular mass of 59.2kDa.NMT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMT1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4).

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myristate, a rare 14-carbon saturated fatty acid, is co-translationally attached by an amide linkage to the N-terminal glycine residue of cellular & viral proteins with various functions. N-Myristoyltransferase 1, also known as NMT1 catalyzes the transfer of myristate from CoA to proteins. NMT1 seems to be irreversible and is essential for full expression of the biologic activities of several N-myristoylated proteins, as well as the alpha subunit of the signal-transducing guanine nucleotide-binding protein, G protein.

    • Synonyms

      N-Myristoyltransferase 1, NMT, Myristoyl-CoA:Protein N-Myristoyltransferase 1, Type I N-Myristoyltransferase, EC 2.3.1.97, Myristoyl-CoA:Protein,N- Myristoyltransferase, Glycylpeptide N-Tetradecanoyltransferase 1,Peptide N-Myristoyltransferase 1,Alternative, Short Form NMT-S, Short Form NMT-S,Long Form, NMT-L, Alternative, Long Form, NMT-L, NMT 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 MGSMADESET AVKPPAPPLP QMMEGNGNGH EHCSDCENEE DNSYNRGGLS PANDTGAKKK KKKQKKKKEK GSETDSAQDQ PVKMNSLPAE RIQEIQKAIE LFSVGQGPAK TMEEASKRSY QFWDTQPVPK LGEVVNTHGP VEPDKDNIRQ EPYTLPQGFT WDALDLGDRG VLKELYTLLN ENYVEDDDNM FRFDYSPEFL LWALRPPGWL PQWHCGVRVV SSRKLVGFIS AIPANIHIYD TEKKMVEINF LCVHKKLRSK RVAPVLIREI TRRVHLEGIF QAVYTAGVVL PKPVGTCRYW HRSLNPRKLI EVKFSHLSRN MTMQRTMKLY RLPETPKTAG LRPMETKDIP VVHQLLTRYL KQFHLTPVMS QEEVEHWFYP QENIIDTFVV ENANGEVTDF LSFYTLPSTI MNHPTHKSLK AAYSFYNVHT QTPLLDLMSD ALVLAKMKGF DVFNALDLME NKTFLEKLKF GIGDGNLQYY LYNWKCPSMG AEKVGLVLQ.

    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.

    Nmt1 Human
  • View Data Sheet

    Name :

    HPD Human

    Description:

    4-Hydroxyphenylpyruvate Dioxygenase Human Recombinant

    4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.

    Product # :

    ENZ-015

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    Description

    HPD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-393a.a.) and having a molecular mass of 47kDa.HPD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HPD protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 50mM NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      4-Hydroxyphenylpyruvate Dioxygenase Isoform-1 is an Fe-containing enzyme, which catalyzes the second reaction in the catabolism of tyrosine the conversion of 4-hydroxyphenylpyruvate to homogentisate. Present as a homodimer, HPD uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. Flaws in the gene encoding HPD result in tyrosinemia type 3 and hawkinsinuria, two inborn defects of metabolism which are related to a number of symptoms, like mental retardation and seizures and hair and urine abnormalities.

    • Synonyms

      4HPPD, GLOD3, 4-HPPD, PPD, HPPDase, Glyoxalase Domain Containing 3, 4-HydroxyphenylpYruvate Dioxygenase.

    • 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 MTTYSDKGAK PERGRFLHFH SVTFWVGNAK QAASFYCSKM GFEPLAYRGL ETGSREVVSH VIKQGKIVFV LSSALNPWNK EMGDHLVKHG DGVKDIAFEV EDCDYIVQKA RERGAKIMRE PWVEQDKFGK VKFAVLQTYG DTTHTLVEKM NYIGQFLPGY EAPAFMDPLL PKLPKCSLEM IDHIVGNQPD QEMVSASEWY LKNLQFHRFW SVDDTQVHTE YSSLRSIVVA NYEESIKMPI NEPAPGKKKS QIQEYVDYNG GAGVQHIALK TEDIITAIRH LRERGLEFLS VPSTYYKQLR EKLKTAKIKV KENIDALEEL KILVDYDEKG YLLQIFTKPV QDRPTLFLEV IQRHNHQGFG AGNFNSLFKA FEEEQNLRGN LTNMETNGVV PGM

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    Hpd Human
  • View Data Sheet

    Name :

    GMPS Human

    Description:

    GMPS Human Recombinant

    GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.

    Product # :

    ENZ-244

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    Description

    GMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 717 amino acids (1-693) and having a molecular mass of 79.2kDa.GMPS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GMPS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GMP synthase (GMPS) is involved in purine biosynthesis. GMPS, which is a homodimer, catalyzes the last step in the GMP synthesis pathway, specifically the ATP-dependent amination of XMP to GMP. GMPS is comprised of one GMP-binding domain and one glutamine amidotransferase type-1 domain through which it communicates its catalytic activity. GMPS is engaged in the de novo synthesis of nucleotides which are not only vital for DNA and RNA synthesis, but also supply GTP, which is involved in sevral cellular processes important for cell division. GMPS gene chromosomal translocations are linked with acute myeloid leukemias, suggesting a possible role for GMPS in carcinogenesis.

    • Synonyms

      GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMALCNG DSKLENAGGD LKDGHHHYEG AVVILDAGAQ YGKVIDRRVR ELFVQSEIFP LETPAFAIKE QGFRAIIISG GPNSVYAEDA PWFDPAIFTI GKPVLGICYG MQMMNKVFGG TVHKKSVRED GVFNISVDNT CSLFRGLQKE EVVLLTHGDS
      VDKVADGFKV VARSGNIVAG IANESKKLYG AQFHPEVGLT ENGKVILKNF LYDIAGCSGT FTVQNRELEC IREIKERVGT SKVLVLLSGG VDSTVCTALL NRALNQEQVI AVHIDNGFMR KRESQSVEEA LKKLGIQVKV INAAHSFYNG TTTLPISDED RTPRKRISKT LNMTTSPEEK
      RKIIGDTFVK IANEVIGEMN LKPEEVFLAQ GTLRPDLIES ASLVASGKAE LIKTHHNDTE LIRKLREEGK VIEPLKDFHK DEVRILGREL GLPEELVSRH PFPGPGLAIR VICAEEPYIC KDFPETNNIL KIVADFSASV KKPHTLLQRV KACTTEEDQE KLMQITSLHS LNAFLLPIKT
      VGVQGDCRSY SYVCGISSKD EPDWESLIFL ARLIPRMCHN VNRVVYIFGP PVKEPPTDVT PTFLTTGVLS TLRQADFEAH NILRESGYAG KISQMPVILT PLHFDRDPLQ KQPSCQRSVV IRTFITSDFM TGIPATPGNE IPVEVVLKMV TEIKKIPGIS RIMYDLTSKP PGTTEWE.

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    Gmps Human
  • View Data Sheet

    Name :

    CTSZ Human, Sf9

    Description:

    Cathepsin-Z Human Recombinant, Sf9

    Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    Product # :

    ENZ-1097

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    Description

    CTSZ produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 288 amino acids (24-303.a.) and having a molecular mass of 32.5kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CTSZ is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    CTSZ protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The specific activity is determent as the ability of 1 unit to convert 1.0 pmole of Mca-PLGL-Dpa-AR-NH2 to MCA- Pro-Leu-OH per minute at pH 3.5 at 25C and is > 1,400 pmol/min/ug.

    More Info

    • Introduction

      Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and a member of the peptidase C1 family. CTSZ, which is known also as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and as other members of this family, takes part in tumorigenesis.

    • Synonyms

      Cathepsin Z, Cathepsin X, Cysteine-Type Carboxypeptidase, Lysosomal Carboxypeptidase B, Carboxypeptidase LB, Cathepsin B2, Cathepsin IV, Cathepsin Z1, Cathepsin P, Cathepsin Y, EC 3.4.18.1, Preprocathepsin P, CTSX.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      GLYFRRGQTC YRPLRGDGLA PLGRSTYPRP HEYLSPADLP KSWDWRNVDG VNYASITRNQ
      HIPQYCGSCW AHASTSAMAD RINIKRKGAW PSTLLSVQNV IDCGNAGSCE GGNDLSVWDY
      AHQHGIPDET CNNYQAKDQE CDKFNQCGTC NEFKECHAIR NYTLWRVGDY GSLSGREKMM
      AEIYANGPIS CGIMATERLA NYTGGIYAEY QDTTYINHVV SVAGWGISDG TEYWIVRNSW
      GEPWGERGWL RIVTSTYKDG KGARYNLAIE EHCTFGDPIV LEHHHHHH

    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.

    Cathepsin Z Protein
  • View Data Sheet

    Name :

    GFPT1 Human

    Description:

    Glutamine--Fructose-6-Phosphate Transaminase 1 Human Recombinant

    Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 1.

    Product # :

    ENZ-818

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    Description

    GFPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (332-699 a.a) and having a molecular mass of 43.7kDa.GFPT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GFPT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Glutamine--Fructose-6-Phosphate Transaminase 1 (GFPT1) participates in the hexosamine pathway and controls the glucose fluidity into the hexosamine pathway. GFPT1 regulates the availability of precursors for N- and O-linked glycosylation of proteins. GFPT1 controls the circadian expression of clock genes ARNTL/BMAL1 and CRY1.

    • Synonyms

      Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 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 MGSQQIMKGN FSSFMQKEIF EQPESVVNTM RGRVNFDDYT VNLGGLKDHI KEIQRCRRLI LIACGTSYHA GVATRQVLEE LTELPVMVEL ASDFLDRNTP VFRDDVCFFL SQSGETADTL MGLRYCKERG ALTVGITNTV GSSISRETDC GVHINAGPEI GVASTKAYTS QFVSLVMFAL MMCDDRISMQ ERRKEIMLGL KRLPDLIKEV LSMDDEIQKL ATELYHQKSV LIMGRGYHYA TCLEGALKIK EITYMHSEGI LAGELKHGPL ALVDKLMPVI MIIMRDHTYA KCQNALQQVV ARQGRPVVIC DKEDTETIKN TKRTIKVPHS VDCLQGILSV IPLQLLAFHL AVLRGYDVDF PRNLAKSVTV E.

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    Gfpt1 Human
  • View Data Sheet

    Name :

    BCAT2 Human

    Description:

    Branched Chain Amino-Acid Transaminase 2 Human Recombinant

    Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.

    Product # :

    ENZ-606

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    Description

    BCAT2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (28-392) and having a molecular mass of 43.9kDa.BCAT2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCAT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 7.5), 10% glycerol, 0.2M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Branched Chain Amino-Acid Transaminase 2 (BCAT2) is a member of the class-IV pyridoxal-phosphate-dependent aminotransferase family. BCAT2 is a branched chain aminotransferase found in mitochondria. BCAT2 forms a dimer which catalyzes the first step in the production of the branched chain amino acids leucine, isoleucine, and valine. In addition, BCAT2 may actn as a transporter of branched chain alpha-keto acids.

    • Synonyms

      Branched-chain-amino-acid aminotransferase mitochondrial, BCAT(m), Placental protein 18, PP18, BCAT2, BCATM, BCT2, ECA40, BCAM.

    • 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 MGSHMASSSF KAADLQLEMT QKPHKKPGPG EPLVFGKTFT DHMLMVEWND KGWGQPRIQP FQNLTLHPAS SSLHYSLQLF EGMKAFKGKD QQVRLFRPWL NMDRMLRSAM RLCLPSFDKL ELLECIRRLI EVDKDWVPDA AGTSLYVRPV LIGNEPSLGV SQPTRALLFV ILCPVGAYFP GGSVTPVSLL ADPAFIRAWV GGVGNYKLGG NYGPTVLVQQ EALKRGCEQV LWLYGPDHQL TEVGTMNIFV YWTHEDGVLE LVTPPLNGVI LPGVVRQSLL DMAQTWGEFR VVERTITMKQ LLRALEEGRV REVFGSGTAC QVCPVHRILY KDRNLHIPTM ENGPELILRF QKELKEIQYG IRAHEWMFPV.

    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.

    Bcat2 Human
  • View Data Sheet

    Name :

    MAT2A Human

    Description:

    Methionine Adenosyltransferase II Alpha Human Recombinant

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

    Product # :

    ENZ-320

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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    Mat2A Human
  • View Data Sheet

    Name :

    GCK Human, Active

    Description:

    Hexokinase-4 Human Recombinant, Active

    Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.

    Product # :

    PKA-116

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    Description

    GCK Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.3kDa. GCK is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GCK protein solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2,000 pmol/min/ug. One unit will convert 1 pmoles of D-Glucose to D-Glucose-6-phosphate per minute at pH8.0 at 37C.

    More Info

    • Introduction

      GCK is an enzyme that expedite the formation of glucose-6-phosphate for glucose by phosphorylation. Humans and other vertebrates have GCK in the cells of the pancreas and liver. In both organs, the enzyme has an important role in carbohydrate metabolism regulation by sensing sugar levels and acting according to the change in glucose levels, that can rise after a meal or fall during fasting. Mutations in the gene that codes for this enzyme can cause hypoglycemia or diabetes.

      .

    • Synonyms

      Glucokinase, Glucokinase (Hexokinase 4), Hexokinase Type IV, HK IV, HK4, Maturity Onset Diabetes of The Young 2, ATP:D-Hexose 6-Phosphotransferase, Hexokinase D, Pancreatic Isozyme, Hexokinase-4, Hexokinase-D, Hexokinase 4.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLDDRARMEA AKKEKVEQIL AEFQLQEEDL KKVMRRMQKE MDRGLRLETH EEASVKMLPT YVRSTPEGSE VGDFLSLDLG GTNFRVMLVK VGEGEEGQWS VKTKHQMYSI PEDAMTGTAE MLFDYISECI SDFLDKHQMK HKKLPLGFTF SFPVRHEDID KGILLNWTKG FKASGAEGNN VVGLLRDAIK RRGDFEMDVV AMVNDTVATM ISCYYEDHQC EVGMIVGTGC NACYMEEMQN VELVEGDEGR MCVNTEWGAF GDSGELDEFL LEYDRLVDES SANPGQQLYE KLIGGKYMGE LVRLVLLRLV DENLLFHGEA SEQLRTRGAF ETRFVSQVES DTGDRKQIYN ILSTLGLRPS TTDCDIVRRA CESVSTRAAH MCSAGLAGVI NRMRESRSED VMRITVGVDG SVYKLHPSFK ERFHASVRRL TPSCEITFIE SEEGSGRGAA LVSAVACKKA CMLGQ.

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    Hexokinase 4
  • View Data Sheet

    Name :

    TYMP Human

    Description:

    Thymidine Phosphorylase Human Recombinant

    Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.

    Product # :

    ENZ-005

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    Description

    TYMP Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 493 amino acids (11-482 a.a.) and having a molecular mass of 51.3kDa. The TYMP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thymidine phosphorylase precursor (TYMP) is a platelet-derived endothelial cell growth factor that catalyzes the formation of thymine and 2-deoxy-D-ribose-1-phosphate from thymidine and orthophosphate. TYMP is an angiogenic inducer that potently stimulates the growth of endothelial cells and induces chemotaxis. TYMP has a highly restricted target cell specificity acting only on endothelial cells. An increased expression of TYMP is found in a broad array of different solid tumors and inflammatory diseases and is frequently associated with poor prognosis. Mutations in the TYMP gene are linked to mitochondrial neurogastrointestinal encephalomyopathy.

    • Synonyms

      Thymidine phosphorylase, Gliostatin, Platelet-derived endothelial cell growth factor, PD-ECGF, TdRPase, TYMP, ECGF1, TP, MNGIE, MEDPS1, MTDPS1, PDECGF, hPD-ECGF.

    • 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 MAPPAPGDFS GEGSQGLPDP SPEPKQLPEL IRMKRDGGRL SEADIRGFVA AVVNGSAQGA QIGAMLMAIR LRGMDLEETS VLTQALAQSG QQLEWPEAWR QQLVDKHSTG GVGDKVSLVL APALAACGCK VPMISGRGLG HTGGTLDKLE SIPGFNVIQS PEQMQVLLDQ AGCCIVGQSE QLVPADGILY AARDVTATVD SLPLITASIL SKKLVEGLSA LVVDVKFGGA AVFPNQEQAR ELAKTLVGVG ASLGLRVAAA LTAMDKPLGR CVGHALEVEE ALLCMDGAGP PDLRDLVTTL GGALLWLSGH AGTQAQGAAR VAAALDDGSA LGRFERMLAA QGVDPGLARA LCSGSPAERR QLLPRAREQE ELLAPADGTV ELVRALPLAL VLHELGAGRS RAGEPLRLGV GAELLVDVGQ RLRRGTPWLR VHRDGPALSG PQSRALQEAL VLSDRAPFAA PSPFAELVLP PQQ.

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    Tymp Human
  • 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 :

    ACP5 Human

    Description:

    Acid Phosphatase-5 Human Recombinant

    Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, Human Purple Acid Phosphatase, EC 3.1.3.2, TrATPase, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase 5a, Tartrate-Resistant Acid Phosphatase 5b, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TRACP5a, TRACP5b, TR-AP, HPAP, TRAP, ACP5.

    Product # :

    ENZ-1025

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    Description

    ACP5 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 304 amino acids (22-325 a.a.) and having a molecular mass of 34.3kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).ACP5 is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACP5 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >10,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmoles of p-nitrophenyl phosphate (pNPP) per minute at pH 5.0 at 37°C.

    More Info

    • Introduction

      Tartrate-resistant acid phosphatase type 5 (ACP5) is involved in osteopontin and bone sialoprotein dephosphorylation. ACP5 is an iron containing glycoprotein which catalyzes the conversion of orthophosphoric monoester to alcohol and orthophosphate. ACP5 expression seems to increase in some pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias. ACP5 is the most basic of the acid phosphatases and is the only form not inhibited by L(+)-tartrate.

    • Synonyms

      Acid Phosphatase 5, Tartrate Resistant, Tartrate-Resistant Acid ATPase, Human Purple Acid Phosphatase, EC 3.1.3.2, TrATPase, Tartrate-Resistant Acid Phosphatase Type 5, Tartrate-Resistant Acid Phosphatase 5a, Tartrate-Resistant Acid Phosphatase 5b, Tartrate-Resistant Acid Phosphatase, Type 5 Acid Phosphatase, TRACP5a, TRACP5b, TR-AP, HPAP, TRAP, ACP5.

    • 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

      ATPALRFVAV GDWGGVPNAP FHTAREMANA KEIARTVQIL GADFILSLGD NFYFTGVQDI NDKRFQETFE DVFSDRSLRK VPWYVLAGNH DHLGNVSAQI AYSKISKRWN FPSPFYRLHF KIPQTNVSVA IFMLDTVTLC GNSDDFLSQQ PERPRDVKLA RTQLSWLKKQ LAAAREDYVL VAGHYPVWSI AEHGPTHCLV KQLRPLLATY GVTAYLCGHD HNLQYLQDEN GVGYVLSGAG NFMDPSKRHQ RKVPNGYLRF HYGTEDSLGG FAYVEISSKE MTVTYIEASG KSLFKTRLPR RARP.

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    Human Acp5
  • View Data Sheet

    Name :

    lldD E. coli

    Description:

    L-Lactate Dehydrogenase E.Coli Recombinant

    L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.

    Product # :

    ENZ-618

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    Description

    lldD E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3kDa.lldD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).

    • Synonyms

      L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.

    • 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 MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA.

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    Lldd E Coli
  • View Data Sheet

    Name :

    CS Human

    Description:

    Citrate Synthase Human Recombinant

    Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, mitochondrial.

    Product # :

    ENZ-824

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    Description

    CS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (28-466 a.a) and having a molecular mass of 51.4kDa. CS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Citrate synthase also known as CS is a Krebs tricarboxylic acid cycle enzyme which catalyzes the synthesis of citrate from oxaloacetate and acetyl coenzyme A. CS is present in almost all cells capable of oxidative metabolism. CS is nuclear encoded and transported into the mitochondrial matrix, where the mature form is found. The diseases related to CS are: critical illness polyneuropathy and mitochondrial cardiomyopathy.

    • Synonyms

      Citrate Synthase, EC 2.3.3.1, Citrate (Si)-Synthase, EC 2.3.3, Citrate synthase, 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 MGSASSTNLK DILADLIPKE QARIKTFRQQ HGKTVVGQIT VDMMYGGMRG MKGLVYETSV LDPDEGIRFR GFSIPECQKL LPKAKGGEEP LPEGLFWLLV TGHIPTEEQV SWLSKEWAKR AALPSHVVTM LDNFPTNLHP MSQLSAAVTA LNSESNFARA YAQGISRTKY WELIYEDSMD LIAKLPCVAA KIYRNLYREG SGIGAIDSNL DWSHNFTNML GYTDHQFTEL TRLYLTIHSD HEGGNVSAHT SHLVGSALSD PYLSFAAAMN GLAGPLHGLA NQEVLVWLTQ LQKEVGKDVS DEKLRDYIWN TLNSGRVVPG YGHAVLRKTD PRYTCQREFA LKHLPNDPMF KLVAQLYKIV PNVLLEQGKA KNPWPNVDAH SGVLLQYYGM TEMNYYTVLF GVSRALGVLA QLIWSRALGF PLERPKSMST EGLMKFVDSK SG.

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    Cs Human
  • View Data Sheet

    Name :

    GOT1 Human

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Human Recombinant

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

    Product # :

    ENZ-528

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    Description

    GOT1 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 acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GOT1 Human solution containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

      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.

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    Got1 Human
  • View Data Sheet

    Name :

    ODC1 Human

    Description:

    Ornithine Decarboxylase 1 Human Recombinant

    ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    Product # :

    ENZ-181

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    Description

    ODC1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 484 amino acids (1-461) and having a molecular mass of 53.5 kDa.ODC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The ODC1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ornithine decarboxylase is the preliminary and rate-limiting enzyme in the biosynthetic pathway of polyamines and it takes part in the alteration of ornithine to putrescine. ODC1 is a key member of various biological processes, such as cell growth, transformation, differentiation and apoptosis. Overexpression of the ODC1 gene has a vital part in cell proliferation and the progress of cancer.

    • Synonyms

      ODC, Ornithine decarboxylase 1, EC 4.1.1.17.

    • 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 MGSMNNFGNE EFDCHFLDEG FTAKDILDQK INEVSSSDDK DAFYVADLGD ILKKHLRWLK ALPRVTPFYA VKCNDSKAIV KTLAATGTGF DCASKTEIQL VQSLGVPPER IIYANPCKQV SQIKYAANNG VQMMTFDSEV ELMKVARAHP KAKLVLRIAT DDSKAVCRLS VKFGATLRTS RLLLERAKEL NIDVVGVSFH VGSGCTDPET FVQAISDARC VFDMGAEVGF SMYLLDIGGG FPGSEDVKLK FEEITGVINP ALDKYFPSDS GVRIIAEPGR YYVASAFTLA VNIIAKKIVL KEQTGSDDED ESSEQTFMYY VNDGVYGSFN CILYDHAHVK PLLQKRPKPD EKYYSSSIWG PTCDGLDRIV ERCDLPEMHV GDWMLFENMG AYTVAAASTF NGFQRPTIYY VMSGPAWQLM QQFQNPDFPP EVEEQDASTL PVSCAWESGM KRHRAACASA SINV

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    Odc1 Human
  • View Data Sheet

    Name :

    L-Asparaginase

    Description:

    L-Asparaginase

    Product # :

    ENZ-287

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    Description

    L-asparaginase was purified from E.coli ASI.357.

    Source

    Escherichia Coli.

    Formulation

    The enzyme was lyophilized with no additives.

    Purity

    Greater than 96.0% as determined by SDS-PAGE.

    Biological Activity

    One IU of L- Asparaginase is defined as that amount of enzyme required to generate 1 µmol of ammonia per minute at pH 7.3 and 37°C.

    More Info

    • Introduction

      L-Asparaginase is an enzyme that depletes L-Asparagine "an important nutrient for cancer cells" resulting in cancer/tumor cell starvation. L-asparaginase is an anti-tumor agent derived from E.coli.,which can inhibit the growth of malignant cells. It is used mainly for the induction of remission in acute lymphoblastic leukaemia. Because of the lymph node origin of malignant B cells in Multiple Myeloma, L-Asparagine is an essential amino acid for their cell metabolism, and, consequently, L-Asparaginase may be of value in managing the disease.
      The rationale behind asparaginase is that it takes advantage of the fact that ALL cellsare unable to synthesize the non-essential amino acidasparaginewhereas normal cells are able to make their own asparagine. These leukemic cells depend on circulating asparagine. Asparaginase however catalyzes the conversion of L-asparagine to aspartic acidand ammonia. This deprives the leukemic cell of circulating asparagine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized L-Asparaginase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution L-Asparaginase should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized L-Asparaginase in 18M-cm H2O at 1mg/ml.

    • Background

      L-Asparaginase Enzyme: Unraveling Its Therapeutic Potential in Cancer Treatment

      Abstract: L-Asparaginase is an enzyme that plays a crucial role in cancer therapy by depleting the levels of asparagine in the blood, thereby inhibiting the growth of cancer cells.

      This research paper provides a comprehensive analysis of L-Asparaginase, including its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications.

      The paper explores the significance of L-Asparaginase as a key enzyme in cancer treatment and highlights its potential for improving patient outcomes.

      1. Introduction L-Asparaginase is an enzyme widely used in cancer therapy, particularly in the treatment of acute lymphoblastic leukemia (ALL). This section introduces L-Asparaginase and its role in cancer treatment, emphasizing its importance in medical research and clinical practice.
      2. Biochemical Properties of L-Asparaginase L-Asparaginase belongs to the class of enzymes known as hydrolases and catalyzes the hydrolysis of asparagine to aspartic acid and ammonia. This section discusses the biochemical properties of L-Asparaginase, including its structure, catalytic mechanism, and factors influencing its activity and stability.
      3. Mechanisms of Action L-Asparaginase exerts its anti-cancer effects by depleting circulating asparagine, an essential amino acid for cancer cell survival. This section delves into the mechanisms of action of L-Asparaginase, including its ability to selectively target cancer cells and induce metabolic stress, leading to cell death. The impact of asparagine deprivation on cancer cell metabolism and survival is also explored.
      4. Therapeutic Applications of L-Asparaginase L-Asparaginase has demonstrated therapeutic efficacy in the treatment of various malignancies, including ALL and certain solid tumors. This section provides an overview of the therapeutic applications of L-Asparaginase, highlighting its use as a first-line treatment in ALL and its potential in other cancer types. The challenges and limitations associated with L-Asparaginase therapy are also discussed.
      5. Clinical Implications and Future Perspectives L-Asparaginase therapy has shown promising results in improving patient outcomes, but it is not without side effects and challenges. This section discusses the clinical implications of L-Asparaginase treatment, including its impact on patient survival, toxicity profile, and the development of resistance. Additionally, the future prospects of L-Asparaginase therapy, such as the development of novel formulations and combination strategies, are explored.
      6. Conclusion L-Asparaginase is a vital enzyme in cancer treatment, particularly in the management of ALL. This research paper has provided a comprehensive analysis of L-Asparaginase, highlighting its biochemical properties, mechanisms of action, therapeutic applications, and clinical implications. Further research on L-Asparaginase and its optimization in cancer therapy will enhance our understanding and pave the way for improved treatments.

    • Unit Definition

      One unit of enzyme catalyzes hydrolyzation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.

    • Specific Activity

      250IU/mg.

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    L Asparaginase
  • View Data Sheet

    Name :

    DECR1 Human

    Description:

    2,4-Dienoyl CoA Reductase 1 Human Recombinant

    2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.

    Product # :

    ENZ-102

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    Description

    DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa. The DECR1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DECR1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.

    • Synonyms

      2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.

    • 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 MNTEALQSKF FSPLQKAMLP PNSFQGKVAF ITGGGTGLGK GMTTLLSSLG AQCVIASRKM DVLKATAEQI SSQTGNKVHA IQCDVRDPDM VQNTVSELIK VAGHPNIVIN NAAGNFISPT ERLSPNAWKT ITDIVLNGTA FVTLEIGKQL IKAQKGAAFL SITTIYAETG SGFVVPSASA KAGVEAMSKS LAAEWGKYGM RFNVIQPGPI KTKGAFSRLD PTGTFEKEMI GRIPCGRLGT VEELANLAAF LCSDYASWIN GAVIKFDGGE EVLISGEFND LRKVTKEQWD TIEELIRKTK GS.

    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.

    Decr1 Human
  • View Data Sheet

    Name :

    B3GNT2 Human

    Description:

    Beta-1,3-N-Acetylglucosaminyltransferase 2 Human Recombinant

    B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    Product # :

    ENZ-973

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    Description

    B3GNT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 375 amino acids (29-397a.a.) and having a molecular mass of 43.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). B3GNT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    B3GNT2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.

    • Synonyms

      B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      ADPKSSSQEK NGKGEVIIPK EKFWKISTPP EAYWNREQEK LNRQYNPILS MLTNQTGEAG RLSNISHLNY CEPDLRVTSV VTGFNNLPDR FKDFLLYLRC RNYSLLIDQP DKCAKKPFLL LAIKSLTPHF ARRQAIRESW GQESNAGNQT VVRVFLLGQT PPEDNHPDLS DMLKFESEKH QDILMWNYRD TFFNLSLKEV LFLRWVSTSC PDTEFVFKGD DDVFVNTHHI LNYLNSLSKT KAKDLFIGDV IHNAGPHRDK KLKYYIPEVV YSGLYPPYAG GGGFLYSGHL ALRLYHITDQ VHLYPIDDVY TGMCLQKLGL VPEKHKGFRT FDIEEKNKNN ICSYVDLMLV HSRKPQEMID IWSQLQSAHL KCHHHHHH.

    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.

    B3Gnt2 Human
  • View Data Sheet

    Name :

    HSD17B10 Human

    Description:

    Hydroxysteroid (17-beta) Dehydrogenase 10 Human Recombinant

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

    Product # :

    PRO-823

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

    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.

    Hsd17B10 Human
  • View Data Sheet

    Name :

    KLK2 Human, sf9

    Description:

    Kallikrein-2 Human Recombinant, sf9

    hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    Product # :

    ENZ-971

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    Description

    KLK2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 246 amino acids (25-261 aa) and having a molecular mass of 27.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions).KLK2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    KLK2 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      KLK2 is a part of the grandular kallikrein protein family whose Members are engaged in a diverse array of biological functions. Kallikreins are a subgroup of serine proteases which are clustered on chromosome 19. KLK2 is a highly active trypsin-like serine protease which selectively cleaves at arginine remains. KLK2 is mostly expressed in prostatic tissue and is accountable for cleaving pro-prostate-specific antigen into its enzymatically active form. KLK2 is greatly expressed in prostate tumor cells and may possibly be a prognostic maker for prostate cancer risk.

    • Synonyms

      hK2, KLK2A2, Kallikrein-2, Glandular kallikrein-1, hGK-1, issue kallikrein-2, KLK2.

    • 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

      ADPIVGGWEC EKHSQPWQVA VYSHGWAHCG GVLVHPQWVL TAAHCLKKNS QVWLGRHNLF EPEDTGQRVP VSHSFPHPLY NMSLLKHQSL RPDEDSSHDL MLLRLSEPAK ITDVVKVLGL PTQEPALGTT CYASGWGSIE PEEFLRPRSL QCVSLHLLSN DMCARAYSEK VTEFMLCAGL WTGGKDTCGG DSGGPLVCNG VLQGITSWGP EPCALPEKPA VYTKVVHYRK WIKDTIAANP 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.

    Klk2 Human Sf9
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