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Search results

1000 results found for “Phosphatase”

Name

Description

Product #

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  • View Data Sheet

    Name :

    DCPS Human

    Description:

    Decapping Enzyme, Scavenger Human Recombinant

    Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    Product # :

    ENZ-159

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    Description

    DCPS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-337 a.a.) and having a molecular mass of 40.7kDa.DCPS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Scavenger mRNA-decapping enzyme (DCPS) is a member of the HIT family. DCPS is required for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. It was shown that DCPS hydrolyzes the residual m7GpppN cap structure after the complete 3'–5' degradation of the mRNA by the exosome. Furthermore, DCPS releases m7GMP and is incapable of cleaving cap structures attached to a long RNA chain.

    • Synonyms

      Scavenger mRNA-decapping enzyme DcpS, DCS-1, Hint-related 7meGMP-directed hydrolase, Histidine triad protein member 5, HINT-5, DCPS, DCS1, HINT5, HSPC015, HSL1.

    • 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 MADAAPQLGK RKRELDVEEA HAASTEEKEA GVGNGTCAPV RLPFSGFRLQ KVLRESARDK IIFLHGKVNE ASGDGDGEDA VVILEKTPFQ VEQVAQLLTG SPELQLQFSN DIYSTYHLFP PRQLNDVKTT VVYPATEKHL QKYLRQDLRL IRETGDDYRN ITLPHLESQS LSIQWVYNIL DKKAEADRIV FENPDPSDGF VLIPDLKWNQ QQLDDLYLIA ICHRRGIRSL RDLTPEHLPL LRNILHQGQE AILQRYRMKG DHLRVYLHYL PSYYHLHVHF TALGFEAPGS GVERAHLLAE VIENLECDPR HYQQRTLTFA LRADDPLLKL LQEAQQS.

    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.

    Dcps Human
  • View Data Sheet

    Name :

    NMNAT1 Human, Active

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Human Recombinant , Active

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

    Product # :

    ENZ-1002

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Nmnat1 Human Active
  • View Data Sheet

    Name :

    KEL Mouse

    Description:

    Kell Metallo-Endopeptidase Mouse Recombinant

    kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    Product # :

    ENZ-1158

    Price :

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    Description

    KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.

    • Synonyms

      kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.

    • 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

      ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.

    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.

    Cd238 Mouse
  • View Data Sheet

    Name :

    MPST Human

    Description:

    Mercaptopyruvate Sulfurtransferase Human Recombinant

    3-mercaptopyruvate sulfurtransferase, MST, MPST, TST2.

    Product # :

    ENZ-676

    Price :

    Quantity :

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    • description
    • source
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    • Citations

    Description

    MPST Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 321 amino acids (1-297) and having a molecular mass of 35kDa.MPST is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Mercaptopyruvate Sulfurtransferase (MPST) catalyzes the transfer of a sulfur ion from 3-mercaptopyruvate to cyanide or other thiol compounds. MPST might be involved in cysteine degradation and cyanide detoxification. The MPST enzyme is regulated by oxidative stress and thioredoxin. In oxidative stress conditions, the catalytic cysteine site is transformed to a sulfenate which inhibits the MPST enzyme activity. The reduced thioredoxin cleaves an intersubunit disulfide bond to activate the redox switch and reactivate the enzyme. A deficiency in MPST activity is implicated in a rare inheritable condition known as MCDU (mercaptolactate-cysteine disulfiduria).

    • Synonyms

      3-mercaptopyruvate sulfurtransferase, MST, MPST, TST2.

    • 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 MGSHMASPQL CRALVSAQWV AEALRAPRAG QPLQLLDASW YLPKLGRDAR REFEERHIPG AAFFDIDQCS DRTSPYDHML PGAEHFAEYA GRLGVGAATH VVIYDASDQG LYSAPRVWWM FRAFGHHAVS LLDGGLRHWL RQNLPLSSGK SQPAPAEFRA QLDPAFIKTY EDIKENLESR RFQVVDSRAT GRFRGTEPEP RDGIEPGHIP GTVNIPFTDF LSQEGLEKSP EEIRHLFQEK KVDLSKPLVA TCGSGVTACH VALGAYLCGK PDVPIYDGSW VEWYMRARPE DVISEGRGKT H.

    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.

    Mpst Human
  • View Data Sheet

    Name :

    IMMP2L Human

    Description:

    IMP2 Inner Mitochondrial Membrane Peptidase-Like Human Recombinant

    IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 2.

    Product # :

    ENZ-822

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    Description

    IMMP2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 161 amino acids (38-175aa) and having a molecular mass of 18.0kDa. IMMP2L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IMMP2L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (IMMP2L) is implicated in processing the signal peptide sequences, IMMP2L is used to direct mitochondrial proteins to the mitochondria. IMMP2L resides in the mitochondria and is one of the essential proteins for the catalytic activity of the mitochondrial inner membrane peptidase (IMP) complex. Two variants which encode the same protein have been found for IMMP2L.

    • Synonyms

      IMP2 Inner Mitochondrial Membrane Peptidase-Like (S. Cerevisiae), IMP2, IMP2 Inner Mitochondrial Membrane Protease-Like (S. Cerevisiae), IMMP2L Intronic Transcript 1 (Non-Protein Coding), Mitochondrial Inner Membrane Protease Subunit, Inner Mitochondrial Membrane Peptidase 2 Like, IMP2-Like Protein, EC 3.4.21.- , IMMP2L-IT1, IMP2-LIKE, EC 3.4.21, Mitochondrial inner membrane protease subunit 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 MGSRVEGASM QPSLNPGGSQ SSDVVLLNHW KVRNFEVHRG DIVSLVSPKN PEQKIIKRVI ALEGDIVRTI GHKNRYVKVP RGHIWVEGDH HGHSFDSNSF GPVSLGLLHA HATHILWPPE RWQKLESVLP PERLPVQREE E.

    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.

    Immp2L Human
  • View Data Sheet

    Name :

    POLR2D Human

    Description:

    Polymerase II Polypeptide D Human Recombinant

    HSRBP4, HSRPB4, RBP4, RPB16, DNA-directed RNA polymerase II subunit RPB4, RNA polymerase II subunit B4, DNA-directed RNA polymerase II subunit D, RNA polymerase II 16 kDa subunit, POLR2D.

    Product # :

    ENZ-739

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    Description

    POLR2D Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 165 amino acids (1-142) and having a molecular mass of 18.7kDa.POLR2D is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The POLR2D solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Polymerase II Polypeptide D (POLR2D) is a member of the eukaryotic RPB4 RNA polymerase subunit family. POLR2D is the fourth largest subunit of RNA polymerase II. Pol II is the main element of the basal RNA polymerase II transcription machinery. polymerase is responsible forsynthesizing messenger RNA in eukaryotes. In yeast, POLR2D subunit is connected with the polymeraseunder suboptimal growth conditions and might have a stress protective role. POLR2D catalyzes the transcription of DNA into RNA by the 4 ribonucleoside triphosphates as substrates.

    • Synonyms

      HSRBP4, HSRPB4, RBP4, RPB16, DNA-directed RNA polymerase II subunit RPB4, RNA polymerase II subunit B4, DNA-directed RNA polymerase II subunit D, RNA polymerase II 16 kDa subunit, POLR2D.

    • 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 MGSMAAGGSD PRAGDVEEDA SQLIFPKEFE TAETLLNSEV HMLLEHRKQQ NESAEDEQEL SEVFMKTLNY TARFSRFKNR ETIASVRSLL LQKKLHKFEL ACLANLCPET AEESKALIPS LEGRFEDEEL QQILDDIQTK RSFQY.

    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.

    Polr2D Human
  • View Data Sheet

    Name :

    GOT1 Mouse

    Description:

    Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

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

    Product # :

    ENZ-872

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

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

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

    Got1 Mouse
  • View Data Sheet

    Name :

    UFC1 Human

    Description:

    Ubiquitin Fold Modifier Conjugating Enzyme 1 Human Recombinant

    Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    Product # :

    ENZ-138

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    Description

    UFC1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.6kDa.UFC1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UFC1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UFC1 is a member of the ubiquitin-conjugating enzyme family. UFC1 is an E2-like conjugating enzyme for ubiquitin-fold modifier-1. UFM1 is activated by UBA5 (a novel E1-like enzyme) by forming a high-energy thioester bond. Activated UFM1 is subsequently transferred to its cognate E2-like enzyme, UFC1, in a similar thioester linkage.

    • Synonyms

      Ubiquitin-fold modifier-conjugating enzyme 1, Ufm1-conjugating enzyme 1, UFC1, CGI-126, HSPC155.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      UFC1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MADEATRRVV SEIPVLKTNA GPRDRELWVQ RLKEEYQSLI RYVENNKNAD NDWFRLESNK EGTRWFGKCW YIHDLLKYEF DIEFDIPITY PTTAPEIAVP ELDGKTAKMY RGGKICLTDH FKPLWARNVP KFGLAHLMAL GLGPWLAVEI PDLIQKGVIQ HKEKCNQ.

    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.

    Ufc1 Human
  • View Data Sheet

    Name :

    LYPLA2 Human

    Description:

    Lysophospholipase II Human Recombinant

    Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    Product # :

    ENZ-076

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    Description

    LYPLA2 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 251 amino acids (1-231 a.a.) and having a molecular mass of 26.9kDa. The LYPLA2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LYPLA2 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Acyl-protein thioesterase 2 (LYPLA2) is lysophospholipase which acts on biological membranes to regulate the multifunctional lysophospholipids. LYPLA2 may hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS.

    • Synonyms

      Acyl-protein thioesterase 2, APT-2, Lysophospholipase II, LPL-II, LysoPLA II, LYPLA2, APT2, DJ886K2.4.

    • 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 MCGNTMSVPL LTDAATVSGA ERETAAVIFL HGLGDTGHSW ADALSTIRLP HVKYICPHAP RIPVTLNMKM VMPSWFDLMG LSPDAPEDEA GIKKAAENIK ALIEHEMKNG IPANRIVLGG FSQGGALSLY TALTCPHPLA GIVALSCWLP LHRAFPQAAN GSAKDLAILQ CHGELDPMVP VRFGALTAEK LRSVVTPARV QFKTYPGVMH SSCPQEMAAV KEFLEKLLPP V.

    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.

    Lypla2 Human
  • View Data Sheet

    Name :

    FBP2 Antibody

    Description:

    Fructose-1,6-Bisphosphatase 2, Mouse Anti Human

    Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.

    Product # :

    ANT-095

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    Formulation

    1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

    Citations

    More Info

    • Introduction

      Fructose-1,6-bisphosphatase isozyme 2 (FBP2) is a part of the FBPase class 1 family. FBP2 is a gluconeogenesis regulatory enzyme Which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate.

    • Synonyms

      Fructose-1,6-bisphosphatase isozyme 2, Fructose-1,6-bisphosphatase isozyme 2, FBPase 2, D-fructose-1,6-bisphosphate 1-phosphohydrolase 2, FBP2.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Immunogen

      Anti-human FBP2 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CMBL 1-339 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and ? light chain.

    • Clone

      PAT1E11AT.

    • Applications

      FBP2 antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:500 ~ 1:5000. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      FBP2 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

    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.

    Fbp2 Antibody
  • View Data Sheet

    Name :

    PRPS1 Antibody

    Description:

    Phosphoribosyl Pyrophosphate Synthetase 1, Mouse Anti Human

    ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.

    Product # :

    ANT-503

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    Citations

    More Info

    • Introduction

      PRPS1 catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis. PRPS1 catalyzes the phosphoribosylation of ribose 5-phosphate to 5-phosphoribosyl-1-pyrophosphate, which is essential for purine metabolism and nucleotide biosynthesis. Defects in PRPS1 result in phosphoribosylpyrophosphate synthetase superactivity, Charcot-Marie-Tooth disease X-linked recessive type 5 and Arts Syndrome.

    • Synonyms

      ARTS, CMTX5, PPRibP, PRSI, DFN2, Ribose-phosphate pyrophosphokinase 1, DFNX1, Phosphoribosyl pyrophosphate synthase I, PRS-I, PRPS1, KIAA0967.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PRPS1 mAb, clone PAT1E11AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PRPS1 protein 1-318 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT1E11AT.

    • Applications

      The antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PRPS1 antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

    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.

    Prps1 Antibody
  • 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

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    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.

    Citations

    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.

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    Dhodh Human
  • View Data Sheet

    Name :

    UGDH Human

    Description:

    UDP-Glucose Dehydrogenase Human Recombinant

    GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    Product # :

    ENZ-535

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    Description

    UGDH Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 533 amino acids (1-494 a.a.) and having a molecular mass of 59.5 kDa. The UGDH is fused to a 39 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UGDH Human solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 1mM EDTA, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 2500pmol/min/ug, and is defined as the amount of enzyme that convert 1.0pmole of UDPglucose to UDP-glucuronate per minute at pH 8.7 at 37C.

    Citations

    More Info

    • Introduction

      UGDH is part of the UDP-glucose/GDP-mannose dehydrogenase family and is a widely expressed enzyme localized in the liver. UGDH transfers UDP-glucose to UDP-glucuronate and thus takes part in the biosynthesis of glycosaminoglycans such as hyaluronan, chondroitin sulfate, and heparan sulfate. These glycosylated products are ordinary molecules of the extracellular matrix and participate in signal transduction, cell migration, and cancer growth and metastasis.

    • Synonyms

      GDH, UDP-GlcDH, UDPGDH, UGD, EC=1.1.1.22, UDP-Glc dehydrogenase, UDP-glucose 6-dehydrogenase, UGDH.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSELEM FEIKKICCIG AGYVGGPTCS VIAHMCPEIR VTVVDVNESR INAWNSPTLP IYEPGLKEVV ESCRGKNLFF STNIDDAIKE ADLVFISVNT PTKTYGMGKG RAADLKYIEA CARRIVQNSN GYKIVTEKST VPVRAAESIR RIFDANTKPN LNLQVLSNPE FLAEGTAIKD LKNPDRVLIG GDETPEGQRA VQALCAVYEH WVPREKILTT NTWSSELSKL AANAFLAQRI SSINSISALC EATGADVEEV ATAIGMDQRI GNKFLKASVG FGGSCFQKDV LNLVYLCEAL NLPEVARYWQ QVIDMNDYQR RRFASRIIDS LFNTVTDKKI AILGFAFKKD TGDTRESSSI YISKYLMDEG AHLHIYDPKV PREQIVVDLS HPGVSEDDQV SRLVTISKDP YEACDGAHAV VICTEWDMFK ELDYERIHKK MLKPAFIFDG RRVLDGLHNE LQTIGFQIET IGKKVSSKRI PYAPSGEIPK FSLQDPPNKK PKV.

    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.

    Ugdh Human
  • View Data Sheet

    Name :

    TPO Human, Biotin

    Description:

    Thyroid Peroxidase Human Recombinant, Biotinylated

    Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    Product # :

    ENZ-1082

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    Description

    Thyroid Peroxidase Human Recombinant produced in SF9 is a Biotinylated, glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 93 kDa (excluding glycosylation). The TPO is expressed with a -6xHis tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

    • Synonyms

      Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    • 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 Functions

      1. Binds IgG-type human auto-antibodies.2. Auto-antibodies to TPO recognize conformation-dependent epitopes.3. Functional Streptavidin based ELISA test (analysis of 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.

    Thyroid Peroxidase Enzyme
  • View Data Sheet

    Name :

    p85a Bovine

    Description:

    Phosphoinositide 3-kinase a, regulatory subunit Bovine Recombinant

    Phosphatidylinositol 3-kinase regulatory subunit alpha, PI3-kinase p85 subunit alpha, PtdIns-3-kinase p85-alpha, PI3K, P85a.

    Product # :

    PKA-328

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    Description

    Phosphoinositide 3-kinase subunit p85a Bovine Recombinant has a molecular weight of 83.5 kDa.

    Source

    Leishmania tarentolae.

    Formulation

    Supplied as a 1 mg/ml solution in 25mM HEPES, pH 8.0, 25mM NaCl, 2.5mM MgCl2 and 50% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      P85a functions as the regulatory subunit of the class IA PI3-kinase isoforms a, b, and d.
      It contains two SH2 domains that bind to tyrosine-phosphorylated growth factor receptors or substrate adaptor proteins.
      It also contains a BH (breakpoint cluster region homology) domain that shows GAP activity towards the small GTPases Rab4, Rab5, Cdc42, Rac1 and to a lesser extend towards Rab6 and Rab11.
      It was shown that PI3Ka catalytic subunit mediated phosphorylation of the p85a adapter reduces the lipid kinase activity of the heterodimer and this gives hints for PI3K-dependent signaling events not requiring production of 3’-phosphorylated phosphoinositides.
      PI3Ka protein kinase activity has been implicated in IRS-1 serine phosphorylation in insulin-treated adipocytes and in STAT3 and IRS-1 phosphorylation upon activation of the type 1 IFN receptor by IFN-a.

    • Synonyms

      Phosphatidylinositol 3-kinase regulatory subunit alpha, PI3-kinase p85 subunit alpha, PtdIns-3-kinase p85-alpha, PI3K, P85a.

    • Physical Appearance

      Sterile filtered liquid formualtion.

    • 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.

    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.

    P85A Bovine
  • View Data Sheet

    Name :

    PKAkt1/PKBa Human

    Description:

    Protein Kinase Akt1/PKB alpha, Inactive enzyme Human Recombinant

    RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.

    Product # :

    PKA-207

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    Description

    PKAkt1 is a glycosilated polypeptide having a molecular mass of 59.1 kDa, fused with a polyhistidine tag at N-terminus (to facilitate removal of Akt1 kinase from the reaction mixture).Inactive enzyme, suitable for negative control experiments or for phosphorylation as a substrate.Recombinant Protein Kinase B is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PKAkt1 in 50mM Tris-HCl, 100mM NaCl, 1mM DTT, 25mM beta glycerophosphate, 50% glycerol, pH 8.5.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Biological Activity

    No protease activity (Twinning test). 
    The Specific activity is 235 U/mg.

    Citations

    More Info

    • Introduction

      Akt1, also known as "Akt" or protein kinaseB (PKB) is an important molecule in mammaliancellular signaling.
      In humans, there are three genes in the "Akt family": Akt1, Akt2, and Akt3. These enzymesare members of the serine/threonine-specific protein kinasefamily (EC2.7.11.1).
      Akt1 is involved in cellular survival pathways, by inhibiting apoptoticprocesses. Akt1 is also able to induce protein synthesispathways, and is therefore a key signaling protein in the cellular pathways that lead to skeletal muscle hypertrophy, and general tissue growth. Since it can block apoptosis, and thereby promote cell survival, Akt1 has been implicated as a major factor in many types of cancer. Akt (now also called Akt1) was originally identified as the oncogenein the transforming retrovirus, AKT8.

    • Synonyms

      RAC-alpha serine/threonine-protein kinase, EC 2.7.11.1, RAC-PK-alpha, Protein kinase B, PKB, C-AKT, AKT1, AKT, RAC, PRKBA, MGC99656, RAC-ALPHA.

    • 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.

    • Unit Definition

      1 Unit is defined as 1 picomole phosphate transferred to the synthetic peptide (RPRAATF) per min at 30°C.

    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.

    Akt1 Human Inactive Enzyme
  • View Data Sheet

    Name :

    NAPSA Human

    Description:

    Napsin A Aspartic Peptidase Human Recombinant

    Napsin A Aspartic Peptidase, NAP1, NAPA, Kidney-Derived Aspartic Protease-Like Protein, Aspartyl Protease 4, TA01/TA02, Napsin-1, SNAPA, Asp 4, ASP4, CTB-191K22.6, EC 3.4.23.15, Pronapsin A, EC 3.4.23.5, EC 3.4.23.3, EC 3.4.23.-, EC 3.4.23, Napsin-A, KDAP, KAP,Napsin-A.

    Product # :

    ENZ-841

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    Description

    NAPSA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 380 amino acids (64-420 a.a) and having a molecular mass of 40.9kDa. NAPSA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAPSA protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Napsin A Aspartic Peptidase, also known as NAPSA is a member of the peptidase A1 family. NAPSA is involved in the processing of pneumocyte surfactant precursors. Furthermore the activation peptides of aspartic proteinases take part as inhibitors of the active site. These peptide segments/pro-parts are considered essential for correct folding, targeting, as well as control of the activation of aspartic proteinase zymogens. The pronapsin A gene is expressed mostly in lung and kidney. In addition, NAPSA translation product is expected to be a fully functional, glycosylated aspartic proteinase precursor which contains an RGD motif as well as an additional 18 residues at its C-terminus.

    • Synonyms

      Napsin A Aspartic Peptidase, NAP1, NAPA, Kidney-Derived Aspartic Protease-Like Protein, Aspartyl Protease 4, TA01/TA02, Napsin-1, SNAPA, Asp 4, ASP4, CTB-191K22.6, EC 3.4.23.15, Pronapsin A, EC 3.4.23.5, EC 3.4.23.3, EC 3.4.23.-, EC 3.4.23, Napsin-A, KDAP, KAP,Napsin-A.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSKPIFVPL SNYRDVQYFG EIGLGTPPQN FTVAFDTGSS NLWVPSRRCH FFSVPCWLHH RFDPKASSSF QANGTKFAIQ YGTGRVDGIL SEDKLTIGGI KGASVIFGEA LWEPSLVFAF AHFDGILGLG FPILSVEGVR PPMDVLVEQG LLDKPVFSFY LNRDPEEPDG GELVLGGSDP AHYIPPLTFV PVTVPAYWQI HMERVKVGPG LTLCAKGCAA ILDTGTSLIT GPTEEIRALH AAIGGIPLLA GEYIILCSEI PKLPAVSFLL GGVWFNLTAH DYVIQTTRNG VRLCLSGFQA LDVPPPAGPF WILGDVFLGT YVAVFDRGDM KSSARVGLAR ARTRGADLGW GETAQAQFPG.

    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.

    Napsa Human
  • View Data Sheet

    Name :

    FAP Human

    Description:

    Fibroblast Activation Protein Alpha Human Recombinant

    Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP,  FAP

    Product # :

    ENZ-1160

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    Description

    FAP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 744 amino acids (26-760aa) and having a molecular mass of 86.1 kDa.FAP is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The FAP solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity > 5,000 pmol/min/ug. It is defined by the amount of enzyme that hydrolyzes 1.0 pmole of ZGP-AMC per minute at pH 7.5, at 37˚C.

    Citations

    More Info

    • Introduction

      DPP4 also called adenosine deaminase complexing protein-2, and T-cell activation antigen CD26 is a serine exopeptidase and complex enzyme that is expressed on the surface of most cell types. DPPIV is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. DPP4 plays a role in t-cell activation. DPP4 is associated with intracellular signal transduction, apoptosis and involved in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and GLP-1.

    • Synonyms

      Prolyl endopeptidase FAP, 170 kDa melanoma membrane-bound gelatinase, Dipeptidyl peptidase FAP, Fibroblast activation protein alpha, FAPalpha, Gelatine degradation protease FAP, Integral membrane serine protease, Post-proline cleaving enzyme, Serine integral membrane protease, Surface-expressed protease, Seprase, SIMP, FAP

    • 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

      ADPLRPSRVH NSEENTMRAL TLKDILNGTF SYKTFFPNWI SGQEYLHQSA DNNIVLYNIE TGQSYTILSN RTMKSVNASN YGLSPDRQFV YLESDYSKLW RYSYTATYYI YDLSNGEFVR GNELPRPIQY LCWSPVGSKL AYVYQNNIYL KQRPGDPPFQ ITFNGRENKI FNGIPDWVYE EEMLATKYAL WWSPNGKFLA YAEFNDTDIP VIAYSYYGDE QYPRTINIPY PKAGAKNPVV RIFIIDTTYP AYVGPQEVPV PAMIASSDYY FSWLTWVTDE RVCLQWLKRV QNVSVLSICD FREDWQTWDC PKTQEHIEES RTGWAGGFFV STPVFSYDAI SYYKIFSDKD GYKHIHYIKD TVENAIQITS GKWEAINIFR VTQDSLFYSS NEFEEYPGRR NIYRISIGSY PPSKKCVTCH LRKERCQYYT ASFSDYAKYY ALVCYGPGIP ISTLHDGRTD QEIKILEENK ELENALKNIQ LPKEEIKKLE VDEITLWYKM ILPPQFDRSK KYPLLIQVYG GPCSQSVRSV FAVNWISYLA SKEGMVIALV DGRGTAFQGD KLLYAVYRKL GVYEVEDQIT AVRKFIEMGF IDEKRIAIWG WSYGGYVSSL ALASGTGLFK CGIAVAPVSS WEYYASVYTE RFMGLPTKDD NLEHYKNSTV MARAEYFRNV DYLLIHGTAD DNVHFQNSAQ IAKALVNAQV DFQAMWYSDQ NHGLSGLSTN HLYTHMTHFL KQCFSLSDHH HHHH

    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.

    Fap Human
  • View Data Sheet

    Name :

    TPO Human

    Description:

    Thyroid Peroxidase Human Recombinant

    Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    Product # :

    ENZ-285

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    Description

    Thyroid Peroxidase Human Recombinant produced in SF9 is a glycosylated, polypeptide chain containing 834 amino acids and having a molecular mass of 92,872 Dalton (excluding glycosylation), 101 kDa total mass.The TPO is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    TPO is supplied in 16mM HEPES pH-7.6, 160mM NaCl, 0.08mM Kl and 20% glycerol.

    Purity

    Greater than 95% as determined by Densitometric Analysis

    Citations

    More Info

    • Introduction

      Thyroid Peroxidase (TPO) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. Its identity with the formerly so-called `microsomal antigen` has been shown several years ago. As an integral membrane glycoprotein it is restricted to the apical plasma membrane of the follicular epithelial cells and comprises two identical subunits of approx. 100 kDa molecular weight. The hemoprotein TPO plays a key role in the thyroid hormone biosynthesis by catalysing both the iodination of tyrosyl residues and the coupling of iodotyrosyl residues in thyroglobulin (TG) to form precursors of the thyroid hormones T4 and T3.

    • Synonyms

      Thyroid peroxidase, EC 1.11.1.8, TPO, MSA, TPX.

    • 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.

    • coating concentration

      0.15-0.375 µg/ml (depending on the type of ELISA plate and coating buffer).Suitable for biotinylation and iodination.

    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.

    Thyroid Peroxidase Human
  • View Data Sheet

    Name :

    GPT Mouse

    Description:

    Glutamic-Pyruvate Transaminase Mouse Recombinant

    Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1.

    Product # :

    ENZ-1030

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    Description

    GPT Mouse 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 57.5kDa.GPT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GPT protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4), 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 40units/mg, and is defined as the amount of enzyme that convert 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C. 

    Citations

    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

      Alanine aminotransferase 1, ALT1, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic 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 MGSMASQRND RIQASRNGLK GKVLTLDTMN PCVRRVEYAV RGPIVQRALE LEQELRQGVK KPFTEVIRAN IGDAQAMGQR PITFFRQVLA LCVYPNLLSS PDFPEDAKRR AERILQACGG HSLGAYSISS GIQPIREDVA QYIERRDGGI PADPNNIFLS TGASDAIVTM LKLLVAGEGR ARTGVLIPIP QYPLYSAALA ELDAVQVDYY LDEERAWALD IAELRRALCQ ARDRCCPRVL CVINPGNPTG QVQTRECIEA VIRFAFEEGL FLMADEVYQD NVYAEGSQFH SFKKVLTEMG PPYATQQELA SFHSVSKGYM GECGFRGGYV EVVNMDAEVQ KQMAKLMSVR LCPPVPGQAL MGMVVSPPTP SEPSFKQFQA ERQEVLAELA AKAKLTEQVF NEAPGIRCNP VQGAMYSFPQ IQLPLKAVQR AQDLGLAPDM FFCLCLLEET GICVVPGSGF GQQEGTYHFR MTILPPMEKL RVLLEKLRHF HAKFTHEYS.

    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 Mouse
  • View Data Sheet

    Name :

    MMP 1 Human, HEK

    Description:

    Matrix Metalloproteinase-1 Human Recombinant, HEK

    Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    Product # :

    ENZ-099

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    • Citations

    Description

    MMP-1 Human Recombinant produced in HEK293 cells is a proform of the Human MMP1 (Met1-Asn469) and fused with a ployhistide tag at the C-terminus, having an Mw of 52kDa. MMP-1 is purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    The MMP-1 is supplied as a 0.2µm filtered solution in MES, NaCl, Glycerol and Brij35.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    The activity was measured by its ability to cleave fluorogenic peptide substrate, Mca-KPLGL-Dpa-AR-NH2, The specific activity is > 400 pmoles/min/µg.
    Recombinant Human MMP-1 protein pro form needs to be activated with p-aminophenylmercuric acetate (APMA).
    Activation Protocol:
    1. Dilute MMP1 to 50µg/ml in the Assay Buffer: 50mM Tris, 10mM CaCl2, 150mM NaCl, 0.05% (w/v) and Brij 35, pH 7.5.
    2. Activate MMP1 by adding APMA to a final concentration of 1mM. (Sigma, Catalog # A9563) and 100mM stock in DMSO.
    3. Incubate at 37°C for 2 hours.

    sds-page

    mmp1 human hek sds-page - Product image 1

    Citations

    More Info

    • Introduction

      MMP-1 (interstitial collagenase) can break down a wide range of substrates including types I, II, III, VII, VIII, and X collagens as well as L-Selectin, pro-TNF, IL-1?, IGFBP-3, IGFBP-5, casein, gelatin, ?1 antitrypsin, myelin basic protein, pro-MMP2 and pro-MMP9. A significant function of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling. MMP-1 is expressed in fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. MMP1 can be divided into a number of distinct domains: a prodomain which is cleaved on activation, a catalytic domain containing the zinc binding site and a short hinge region with a carboxyl terminal domain. MMP1 is part of a cluster of MMP genes which localize to chromosome 11q22.3.

    • Synonyms

      Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, MMP1, CLG, CLGN.

    • 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.Avoid multiple 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.

    Mmp 1 Human
  • View Data Sheet

    Name :

    NFNB E.Coli

    Description:

    Dihydropteridine Reductase E.Coli Recombinant

    DPRA, NFSB, NFSI, NTR.

    Product # :

    ENZ-423

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    Description

    NFNB Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 237 amino acids (1-217 a.a.) and having a molecular mass of 26 kDa. The NFNB is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1mg/ml solution containing 20mM Tris pH-8, 1mM DTT, 0.05M NaCl & 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NFNB demonstrates the capability to reduce quinines. NFNB enzyme activates prodrugs in antibody directed enzyme prodrug therapy. NFNB reduces nitrofurazone, quinones and anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.

    • Synonyms

      DPRA, NFSB, NFSI, NTR.

    • 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 MDIISVALKR HSTKAFDASK KLTPEQAEQI KTLLQYSPSS TNSQPWHFIV ASTEEGKARV AKSAAGNYVF NERKMLDASH VVVFCAKTAM DDVWLKLVVD QEDADGRFAT PEAKAANDKG RKFFADMHRK DLHDDAEWMA KQVYLNVGNF LLGVAALGLD AVPIEGFDAA ILDAEFGLKE KGYTSLVVVP VGHHSVEDFN ATLPKSRLPQ NITLTEV.

    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.

    Nfnb Ecoli
  • View Data Sheet

    Name :

    ST3GAL5 Human

    Description:

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5 Human Recombinant

    ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    Product # :

    ENZ-755

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    Description

    ST3GAL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 359 amino acids (83-418a.a) and having a molecular mass of 41kDa. ST3GAL5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ST3GAL5 protein solution (1mg/ml) containing In 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, also know as ST3GAL5 belongs to the glycosyltransferase family 29 and localized to the Golgi apparatus. ST3GAL5 is known to play a part in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. ST3GAL5 is a type II membrane protein which catalyzes the formation of GM3 with lactosylceramide as the substrate. Mutation in this ST3GAL5 has been connected with Amish infantile epilepsy syndrome. Transcript variants encoding various isoforms have been found for this gene.

    • Synonyms

      ST3 Beta-Galactoside Alpha-2,3-Sialyltransferase 5, SIAT9, Sialyltransferase 9 (CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase; GM3 Synthase), Ganglioside GM3 Synthase, ST3GalV, CMP-NeuAc:Lactosylceramide Alpha-2,3-Sialyltransferase, ST3Gal V, EC 2.4.99.9, SATI, SIATGM3S, Alpha 2,3-Sialyltransferase V, Lactosylceramide Alpha-2,3-Sialyltransferase, Sialyltransferase 9, ST3GALV, GM3 Synthase.

    • 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 MGSLKLNYTT EECDMKKMHY VDPDHVKRAQ KYAQQVLQKE CRPKFAKTSM ALLFEHRYSV DLLPFVQKAP KDSEAESKYD PPFGFRKFSS KVQTLLELLP EHDLPEHLKA KTCRRCVVIG SGGILHGLEL GHTLNQFDVV IRLNSAPVEG YSEHVGNKTT IRMTYPEGAP LSDLEYYSND LFVAVLFKSV DFNWLQAMVK KETLPFWVRL FFWKQVAEKI PLQPKHFRIL NPVIIKETAF DILQYSEPQS RFWGRDKNVP TIGVIAVVLA THLCDEVSLA GFGYDLNQPR TPLHYFDSQC MAAMNFQTMH NVTTETKFLL KLVKEGVVKD LSGGIDREF

    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.

    St3Gal5 Human
  • View Data Sheet

    Name :

    CDK5 Human

    Description:

    Cyclin-dependent Kinase 5 Human Recombinant

    Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.

    Product # :

    PKA-047

    Price :

    Quantity :

    Shipping Method :

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    CDK5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 316 amino acids (1-292) and having a molecular mass of 35.8kDa. CDK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CDK5 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol 0.4M Urea.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.

    • Synonyms

      Cyclin-dependent kinase 5, Cell division protein kinase 5, Serine/threonine-protein kinase PSSALRE, Tau protein kinase II catalytic subunit, CDK5, CDKN5, TPKII catalytic subunit, cyclin dependent kinase 5.

    • 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 MGSHMQKYEK LEKIGEGTYG TVFKAKNRET HEIVALKRVR LDDDDEGVPS SALREICLLK ELKHKNIVRL HDVLHSDKKL TLVFEFCDQD LKKYFDSCNG DLDPEIVKSF LFQLLKGLGF CHSRNVLHRD LKPQNLLINR NGELKLADFG LARAFGIPVR CYSAEVVTLW YRPPDVLFGA KLYSTSIDMW SAGCIFAELA NAGRPLFPGN DVDDQLKRIF RLLGTPTEEQ WPSMTKLPDY KPYPMYPATT SLVNVVPKLN ATGRDLLQNL LKCNPVQRIS AEEALQHPYF SDFCPP.

    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.

    Cdk5 Human
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