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Search results

1000 results found for “dehydrogenase”

Name

Description

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  • View Data Sheet

    Name :

    UPRT Human

    Description:

    Uracil Phosphoribosyltransferase Human Recombinant

    Uracil phosphoribosyltransferase homolog, Uracil phosphoribosyltransferase (FUR1) homolog (S.cerevisiae), FUR1, Uracil Phosphoribosyltransferase, RP11-311P8.3, UPP, UPRT, UPRTase, UMP pyrophosphorylase, uprt.

    Product # :

    ENZ-742

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    Description

    UPRT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 332 amino acids (1-309 a.a) and having a molecular mass of 36.2kDa.UPRT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPRT protein solution (0. 5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPRT is a uracil phosphoribosyltransferase, that catalyzes the alteration of uracil and 5-phosphoribosyl-1-R-diphosphate to uridine monophosphate (UMP). This reaction is a significant part of nucleotide metabolism, specifically the pyrimidine salvage pathway. UPRT is restricted to the nucleus and cytoplasm and is a possible target for rational design of drugs to cure cancer and parasitic infections.

    • Synonyms

      Uracil phosphoribosyltransferase homolog, Uracil phosphoribosyltransferase (FUR1) homolog (S.cerevisiae), FUR1, Uracil Phosphoribosyltransferase, RP11-311P8.3, UPP, UPRT, UPRTase, UMP pyrophosphorylase, uprt.

    • 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 MGSMATELQC PDSMPCHNQQ VNSASTPSPE QLRPGDLILD HAGGNRASRA KVILLTGYAH SSLPAELDSG ACGGSSLNSE GNSGSGDSSS YDAPAGNSFL EDCELSRQIG AQLKLLPMND QIRELQTIIR DKTASRGDFM FSADRLIRLV VEEGLNQLPY KECMVTTPTG YKYEGVKFEK GNCGVSIMRS GEAMEQGLRD CCRSIRIGKI LIQSDEETQR AKVYYAKFPP DIYRRKVLLM YPILSTGNTV IEAVKVLIEH GVQPSVIILL SLFSTPHGAK SIIQEFPEIT ILTTEVHPVA PTHFGQKYFG TD.

    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.

    Uprt Human
  • View Data Sheet

    Name :

    NMNAT1 Mouse

    Description:

    Nicotinamide Nucleotide Adenylyltransferase 1 Mouse Recombinant

    Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    Product # :

    ENZ-1049

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    Description

    NMNAT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (1-285 a.a) and having a molecular mass of 34.7kDa. NMNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NMNAT1 protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4), 20% glycerol and 1mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    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

      Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1, NMNAT1, NMN/NaMN adenylyltransferase 1, Nicotinamide mononucleotide adenylyltransferase 1, NMN adenylyltransferase, Nicotinate-nucleotide adenylyltransferase 1, NaMN adenylyltransferase 1, D4Cole1e, Nmnat.

    • Physical Appearance

      Sterile filtered colourless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMDSSKKT EVVLLACGSF NPITNMHLRL FELAKDYMHA TGKYSVIKGI ISPVGDAYKK KGLIPAHHRI IMAELATKNS HWVEVDTWES LQKEWVETVK VLRYHQEKLA TGSCSYPQSS PALEKPGRKR KWADQKQDSS PQKPQEPKPT GVPKVKLLCG ITNDISSTKI RRALRRGQSI RYLVPDLVQE YIEKHELYNT ESEGRNAGVT LAPLQRNAAE AKHNHSTL.

    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 Mouse
  • View Data Sheet

    Name :

    ENO2 Mouse

    Description:

    Enolase-2 Mouse Recombinant

    AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    Product # :

    ENZ-1028

    Price :

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    • More Info

    Description

    ENO2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 49.7kDa.ENO2 is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ENO2 solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10,000 pmol/min/µg, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.

    More Info

    • Introduction

      Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.

    • Synonyms

      AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.

    • Physical Appearance

      Sterile Filtered clear 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 MGSMSIEKIW AREILDSRGN PTVEVDLYTA KGLFRAAVPS GASTGIYEAL ELRDGDKQRY LGKGVLKAVD HINSRIAPAL ISSGISVVEQ EKLDNLMLEL DGTENKSKFG ANAILGVSLA VCKAGAAERD LPLYRHIAQL AGNSDLILPV PAFNVINGGS HAGNKLAMQE FMILPVGAES FRDAMRLGAE VYHTLKGVIK DKYGKDATNV GDEGGFAPNI LENSEALELV KEAIDKAGYT EKMVIGMDVA ASEFYRDGKY DLDFKSPADP SRYITGDQLG ALYQDFVRNY PVVSIEDPFD QDDWAAWSKF TANVGIQIVG DDLTVTNPKR IERAVEEKAC NCLLLKVNQI GSVTEAIQAC KLAQENGWGV MVSHRSGETE DTFIADLVVG LCTGQIKTGA PCRSERLAKY NQLMRIEEEL GDEARFAGHN FRNPSVL.

    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.

    Eno2 Mouse
  • View Data Sheet

    Name :

    UBE2Z Human

    Description:

    Ubiquitin Conjugating Enzyme E2Z Human Recombinant

    HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    Product # :

    ENZ-804

    Price :

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    Description

    UBE2Z Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 269 amino acids (1-246a.a) and having a molecular mass of 30.5kDa. UBE2Z is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2Z solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ubiquitin Conjugating Enzyme E2Z, also known as UBE2z, is a protein coding gene which is a part of the ubiquitin-conjugating enzyme family. UBE2z catalyzes the covalent attachment of ubiquitin to various proteins. UBE2z takes part in in apoptosis regulation and is also a specific substrate for UBA6, not charged with ubiquitin by UBE1.

    • Synonyms

      HOYS7, USE1, Ubiquitin-conjugating enzyme E2 Z, E2 ubiquitin-conjugating enzyme Z, Uba6-specific E2 conjugating enzyme 1, Ubiquitin carrier protein Z, Ubiquitin-protein ligase Z, UBE2Z.

    • 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 MGSMSIYKEP PPGMFVVPDT VDMTKIHALI TGPFDTPYEG GFFLFVFRCP PDYPIHPPRV KLMTTGNNTV RFNPNFYRNG KVCLSILGTW TGPAWSPAQS ISSVLISIQS LMTENPYHNE PGFEQERHPG DSKNYNECIR HETIRVAVCD MMEGKCPCPE PLRGVMEKSF LEYYDFYEVA CKDRLHLQGQ TMQDPFGEKR GHFDYQSLLM RLGLIRQKVL ERLHNENAEM DSDSSSSGTE TDLHGSLRV.

    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.

    Ube2Z Human
  • View Data Sheet

    Name :

    GSTO2 Human

    Description:

    Glutathione S-Transferase Omega 2 Human Recombinant

    Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

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    ENZ-605

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    Description

    GSTO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243) and having a molecular mass of 30.6kDa.GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 40% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.

    • Synonyms

      Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSGDATR TLGKGSQPPG PVPEGLIRIY SMRFCPYSHR TRLVLKAKDI RHEVVNINLR NKPEWYYTKH PFGHIPVLET SQCQLIYESV IACEYLDDAY PGRKLFPYDP YERARQKMLL ELFCKVPHLT KECLVALRCG RECTNLKAAL RQEFSNLEEI
      LEYQNTTFFG GTCISMIDYL LWPWFERLDV YGILDCVSHT PALRLWISAM KWDPTVCALL MDKSIFQGFL NLYFQNNPNA FDFGLC.

    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.

    Gsto2 Human
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    Name :

    PPCS Human

    Description:

    Phosphopantothenoylcysteine Synthetase Human Recombinant

    Phosphopantothenate--cysteine ligase, Phosphopantothenoylcysteine synthetase, PPC synthetase, PPCS, COAB, RP11-163G10.1.

    Product # :

    ENZ-139

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    Description

    PPCS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-311 a.a.) and having a molecular mass of 36.1kDa.PPCS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Phosphopantothenate-cysteine ligase (PPCS) catalyzes the first step in the biosynthesis of coenzyme A (CoA) from pantothenic acid (vitamin B5), which is a vital universal pathway in prokaryotes and eukaryotes. PPCS, being one of the last enzymes in this pathway, converts phosphopantothenate to phosphopantothenoylcysteine.

    • Synonyms

      Phosphopantothenate--cysteine ligase, Phosphopantothenoylcysteine synthetase, PPC synthetase, PPCS, COAB, RP11-163G10.1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      PPCS 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 MAEMDPVAEF PQPPGAARWA EVMARFAARL GAQGRRVVLV TSGGTKVPLE ARPVRFLDNF SSGRRGATSA EAFLAAGYGV LFLYRARSAF PYAHRFPPQT WLSALRPSGP ALSGLLSLEA EENALPGFAE ALRSYQEAAA AGTFLAVEFT TLADYLHLLQ AAAQALNPLG PSAMFYLAAA VSDFYVPVSE MPEHKIQSSG GPLQITMKMV PKLLSPLVKD WAPKAFIISF KLETDPAIVI NRARKALEIY QHQVVVANIL ESRQSFVFIV TKDSETKLLL SEEEIEKGVE IEEKIVDNLQ SRHTAFIGDR N.

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    Ppcs Human
  • View Data Sheet

    Name :

    ACY3 Human

    Description:

    AminoAcylase-3 Human Recombinant

    Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    Product # :

    ENZ-153

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    Description

    ACY3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 342 amino acids (1-319 a.a.) and having a molecular mass of 37.6kDa.ACY3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ACY3 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Aspartoacylase 3 (ACY3) belongs to the Aspartoacylase subfamily. ACY3 has a vital role in deacetylating mercapturic acids in kidney proximal tubules. Aspartoacylase 3 localizes to the cytoplasm of S2 and S3 proximal tubules and also to the apical domain of S1 proximal tubules. In addition, ACY3 protein is expressed at low levels in the stomach, testis, heart, brain, lung and liver, and can function as an HCV (Hepatitis C virus) core binding protein.

    • Synonyms

      Aspartoacylase-2, Acylase III, Aminoacylase-3, ACY-3, Hepatitis C virus core-binding protein 1, HCBP1, ACY3, ASPA2.

    • 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 MGSMCSLPVP REPLRRVAVT GGTHGNEMSG VYLARHWLHA PAELQRASFS AVPVLANPAA TSGCRRYVDHDLNRTFTSSF LNSRPTPDDP YEVTRARELN QLLGPKASGQ AFDFVLDLHN TTANMGTCLI AKSSHEVFAM HLCRHLQLQY PELSCQVFLY QRSGEESYNL DSVAKNGLGL ELGPQPQGVL RADIFSRMRT LVATVLDFIE LFNQGTAFPA FEMEAYRPVG VVDFPRTEAG HLAGTVHPQL QDRDFQPLQP GAPIFQMFSG EDLLYEGEST VYPVFINEAA YYEKGVAFVQ TEKFTFTVPA MPALTPAPSP AS.

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    Acy3 Human
  • View Data Sheet

    Name :

    GSTM2 Human

    Description:

    Glutathione S-Transferase MU 2 Human Recombinant

    Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    Product # :

    ENZ-003

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    Description

    GSTM2 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 238 amino acids (1-218 a.a.) and having a molecular mass of 27.9kDa. The GSTM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol,
    0.1M NaCl and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 25 units/mg, and is defined as the amount of enzyme that conjugate 1.0 µmole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25°C.

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    • Introduction

      Glutathione S-transferase Mu 2 (GSTM2) belongs to the glutathione s-transferase (GST) family of proteins. GSTM2 is a glutathione S-transferase that belongs to the mu class. There are 8 families of GST proteins, specifically: alpha, kappa, mu, omega, pi, sigma, theta and zeta, each of which is composed of proteins that have various functions throughout the cell. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are structured in a gene cluster on chromosome 1p13.3 and are proven to be highly polymorphic. These genetic variants can change an individual''s susceptibility to carcinogens and toxins as well as have an effect on the toxicity and efficacy of several drugs.

    • Synonyms

      Glutathione S-transferase Mu 2, GST class-mu 2, GSTM2-2, GSTM2, GST4, GSTM, GTHMUS, MGC117303.

    • 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 MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK.

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    Gstm2 Human
  • View Data Sheet

    Name :

    PRDX6 Human

    Description:

    Peroxiredoxin-6 Human Recombinant

    Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    Product # :

    ENZ-432

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    Description

    Peroxiredoxin- 6 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 244 amino acids (1-224 a.a.) and having a molecular mass of 27.1kDa.The Peroxiredoxin-6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Peroxiredoxin-6 solution contains 20mM Tris-HCl buffer (pH8.0) and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is >2,000pmol/min/ug was defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25C for 1minute. 

    More Info

    • Introduction

      Peroxiredoxin 6 (PRDX6) belongs to the thiol-specific antioxidant protein family. PRDX6 is a bifunctional enzyme with 2 distinct active sites. PRDX6 is involved in redox regulation of the cell and can reduce Hydrogen peroxide and short chain organic, fatty acid, and phospholipid hydroperoxides. PRDX6 may have a role in the regulation of phospholipid turnover as well as in protection against oxidative injury. Furthermore, PRDX6 eases the oxidative stress and TGF-beta-induced abnormalities of human trabecular meshwork cells. In addition, PRDX6 is necessary for blood vessel integrity in injured skin.
      At acidic pH, PRDX6 binds to reduced phospholipids, however at cytosolic pH PRDX6 binds only to phospholipids that are oxidized which is compatible with the role for PRDX6 in the repair of peroxidized cell membranes. Hydrogen peroxide-mediated hyperoxidation of PRDX6 induces cell cycle arrest at the G2/M transition via up-regulation of iPLA2 activity. Overexpression of PRDX6 is linked to oligodendroglioma.

    • Synonyms

      Peroxiredoxin-6, Antioxidant protein 2, 1-Cys peroxiredoxin, Acidic calcium-independent phospholipase A2, Non-selenium glutathione peroxidase, 24 kDa protein, Liver 2D page spot 40, Red blood cells page spot 12, 1-Cys PRX, aiPLA2, NSGPx, PRDX6, AOP2, KIAA0106, PRX, p29, 1-Cys, MGC46173.

    • 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 MPGGLLLGDV APNFEANTTV GRIRFHDFLG DSWGILFSHP RDFTPVCTTE LGRAAKLAPE FAKRNVKLIA LSIDSVEDHL AWSKDINAYN CEEPTEKLPF PIIDDRNREL AILLGMLDPA EKDEKGMPVT ARVVFVFGPD KKLKLSILYP ATTGRNFDEI LRVVISLQLT AEKRVATPVD WKDGDSVMVL PTIPEEEAKK LFPKGVFTKE LPSGKKYLRY TPQP.

    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.

    Prdx6 Human
  • View Data Sheet

    Name :

    ENTPD3 Human, sf9

    Description:

    Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9

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

    Product # :

    ENZ-958

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    Description

    ENTPD3 Human Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 451 amino acids (44-485a.a) and having a molecular mass of 50.7kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). ENTPD3 is fused to a 6 amino acids His-tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ENTPD3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered 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

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

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    Entpd3 Human Sf9
  • View Data Sheet

    Name :

    UBA5 Human

    Description:

    Ubiquitin-Like Modifier Activating Enzyme 5 Human Recombinant

    Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    Product # :

    ENZ-602

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    Description

    UBA5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-404) and having a molecular mass of 47.4kDa.UBA5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBA5 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 50mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      Ubiquitin-like modifier activating enzyme 5 (UBA5) is a member of the ubiquitin-activating E1 family and UBA5 subfamily. Ubiquitin and ubiquitin-like proteins are recognized as covalently conjugated to various cellular substrates by a three-step enzymatic pathway. The ubiquitin-activating enzyme (E1) has a vital role in the first step of ubiquitination pathway to activate ubiquitin or ubiquitin-like proteins. UBA5 activates an ubiquitin-like protein, ubiquitin-fold modifier 1 (Ufm1), by forming a high-energy thioester bond. UBA5 is located primarily in cytoplasm, while it generally localizes to the nucleus in presence of SUMO2.

    • Synonyms

      Ubiquitin-like modifier-activating enzyme 5, Ubiquitin-activating enzyme 5, ThiFP1, UFM1-activating enzyme, Ubiquitin-activating enzyme E1 domain-containing protein 1, UBA5, UBE1DC1.

    • 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 MGSHMAESVE RLQQRVQELE RELAQERSLQ VPRSGDGGGG RVRIEKMSSE VVDSNPYSRL MALKRMGIVS DYEKIRTFAV AIVGVGGVGS VTAEMLTRCG IGKLLLFDYD KVELANMNRL FFQPHQAGLS KVQAAEHTLR NINPDVLFEV HNYNITTVEN
      FQHFMDRISN GGLEEGKPVD LVLSCVDNFE ARMTINTACN ELGQTWMESG VSENAVSGHI QLIIPGESAC FACAPPLVVA ANIDEKTLKR EGVCAASLPT TMGVVAGILV QNVLKFLLNF GTVSFYLGYN AMQDFFPTMS MKPNPQCDDR NCRKQQEEYK KKVAALPKQE VIQEEEEIIH
      EDNEWGIELV SEVSEEELKN FSGPVPDLPE GITVAYTIPK KQEDSVTELT VEDSGESLED LMAKMKNM.

    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.

    Uba5 Human
  • View Data Sheet

    Name :

    NAT6 Human

    Description:

    N-Acetyltransferase 6 Human Recombinant

    Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.

    Product # :

    ENZ-410

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    Description

    Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.

    • Synonyms

      Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-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 MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.

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    Nat6 Human
  • View Data Sheet

    Name :

    C1GALT1 Human

    Description:

    Core 1 Beta3-Gal-T1 Human Recombinant

    Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

    Product # :

    ENZ-721

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    Description

    C1GALT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (30-363 a.a) and having a molecular mass of 41.4kDa.C1GALT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    C1GALT1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Core 1 Beta3-Gal-T1 also known as,C1GALT1 creates the common core 1 O-glycan structure, Gal-beta-1-3GalNAc-R, by the transfer of Gal from UDP-Gal to GalNAc-alpha-1-R. Core 1 is a precursor for lots of extended mucin-type O-glycans on cell surface and secreted glycoproteins. Studies in mice have shown that this gene takes a main role in angiogenesis, thrombopoiesis and kidney homeostasis.

    • Synonyms

      Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Core 1 Beta3-Gal-T1, Core 1 O-Glycan T-Synthase, Core 1 UDP-Galactose:N-Acetylgalactosamine-Alpha-R Beta 1,3 Galactosyltransferase 1, B3Gal-T8, EC 2.4.1.122, Core 1 Beta3-Gal-T, C1GALT, T-synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, Beta-1,3-galactosyltransferase, C1GalT1, Core 1 Beta1,3-Galactosyltransferase 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSLLGEKVD TQPNVLHNDP HARHSDDNGQ NHLEGQMNFN ADSSQHKDEN TDIAENLYQK VRILCWVMTG PQNLEKKAKH VKATWAQRCN KVLFMSSEEN KDFPAVGLKT KEGRDQLYWK TIKAFQYVHE HYLEDADWFL KADDDTYVIL DNLRWLLSKY DPEEPIYFGR RFKPYVKQGY MSGGAGYVLS KEALKRFVDA FKTDKCTHSS SIEDLALGRC MEIMNVEAGD SRDTIGKETF HPFVPEHHLI KGYLPRTFWY WNYNYYPPVE GPGCCSDLAV SFHYVDSTTM YELEYLVYHL RPYGYLYRYQ PTLPERILKE ISQANKNEDT KVKLGNP.

    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.

    C1Galt1 Human
  • View Data Sheet

    Name :

    UCHL3 Mouse

    Description:

    Ubiquitin Carboxyl-Terminal Esterase L3 Mouse Recombinant

    Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    Product # :

    ENZ-978

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    Description

    UCHL3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 238 amino acids (1-230) and having a molecular mass of 27.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).UCHL3 is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    UCHL3 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 9,000 pmol/min/mg, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of ubiquitin-AMC per minute at pH 7.5, at 37°C.

    More Info

    • Introduction

      Ubiquitin carboxyl-terminal hydrolase isozyme L3 belongs to a gene family whose products hydrolyze small C-terminal adducts of ubiquitin to produce the ubiquitin monomer. UCHL3 takes part in the regulation of neuronal development and spermatogenesis and is associated to neurodegenerative diseases. UCHL3 has a 54% homology to UCHL1.

    • Synonyms

      Ubiquitin carboxyl-terminal hydrolase isozyme L3, UCH-L3, UCHL3, Ubiquitin Carboxyl-Terminal Esterase L3, Ubiquitin thioesterase L3, Uchl3, Ubiquitin carboxyl-terminal esterase L3.

    • 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

      MEGQRWLPLE ANPEVTNQFL KQLGLHPNWQ FVDVYGMEPE LLSMVPRPVC AVLLLFPITE KYEVFRTEEE EKIKSQGQDV TSSVYFMKQT ISNACGTIGL IHAIANNKDK MHFESGSTLK KFLEESVSMS PEERAKFLEN YDAIRVTHET SAHEGQTEAP SIDEKVDLHF IALVHVDGHL YELDGRKPFP INHGKTSDET LLEDAIEVCK KFMERDPDEL RFNAIALSAA 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.

    Uchl3 Mouse
  • View Data Sheet

    Name :

    PHOSPHO1 Human

    Description:

    Phosphatase Orphan-1 Human Recombinant

    Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    Product # :

    ENZ-363

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    Description

    Human Phospho1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 31.3 kDa. The Human Phospho1 is fused to a 14 aa His tag at N-Terminus. Human Phosphocholine Phosphatase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
      PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
      Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
      Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
      PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
      PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

    • Synonyms

      Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    • Physical Appearance

      Filtered lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMSGCFP VSGLRCLSRD GRMAAQGAPR FLLTFDFDET IVDENSDDSI VRAAPGQRLP ESLRATYREG FYNEYMQRVF KYLGEQGVRP RDLSAIYEAI PLSPGMSDLL QFVAKQGACF EVILISDANT FGVESSLRAA GHHSLFRRIL SNPSGPDARG LLALRPFHTH SCARCPANMC KHKVLSDYLR ERAHDGVHFE RLFYVGDGAN DFCPMGLLAG GDVAFPRRGY PMHRLIQEAQ KAEPSSFRAS VVPWETAADV RLHLQQVLKSC.

    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.

    Phospho1 Human
  • View Data Sheet

    Name :

    Phosphotransacetylase

    Description:

    Phosphotransacetylase Bacillus S. Recombinant

    Phosphate Acetyltransferase, EC 2.3.1.8, Phosphotransacetylase, phosphoacylase.

    Product # :

    ENZ-1205

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    Description

    Phosphotransacetylase Bacillus Stearothermophilus Recombinant produced in E.Coli is a single, non glycosylated polypeptide chain containing 325 amino acids and having a total molecular mass of 34.7kDa.
    Phosphotransacetylase Recombinant is purified by proprietary chromatographic techniques.

    Source

    E.Coli

    Formulation

    The protein was lyophilized with 0.15M NaCl and 20mM Tris pH-8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Phosphotransacetylase activity is assessed by using the DTNB spectrophotometric method which was found to be greater than 3,000 Units/mg.

    More Info

    • Introduction

      Phosphotransacetylase (PTA) is a metabolic enzyme (EC 2.3.1.8) that catalyzes the reversible conversion: acetyl-CoA + Pi ⇄ acetyl-phosphate + CoA. The reversible reaction of acetyl-CoA to acetate node and back, is useful in R&D and biotech assays such as Metabolic engineering, Synthetic biology, Production of biopolymers, Enzymatic synthesis of acetyl-phosphate, bacterial signaling
      and Fermentation.  Phosphotransacetylase controls acetate formation and manipulates acetyl-CoA flux thus is widely used in protein expression, metabolic engineering, and synthetic pathways.

    • Synonyms

      Xylosyltransferase 2, Peptide O-xylosyltransferase 1, Xylosyltransferase II, XT-II, XylT-II, XYLT2, XT2.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Phosphate Acetyltransferase although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Phosphate Acetyltransferase should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Phosphate Acetyltransferase in
      sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be
      further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TTDLFTALKA KVTGTARKIV FPEGTDDRIL TAASRLATEQ VLQPIVLGDE QAIRVKAAAL GLPLEGVEIV NPRRYGGFDE LVSAFVERRK GKVTEETARE LLFDENYFGT MLVYMGAADG LVSGAAHSTA DTVRPALQII KTKPGVGKTS GVFIMVRGDE KYVFADCAIN IAPNSQDLAE IAVESARTAK MFGLKPRVAL LSFSTKGSAS SPETEKVVEA VRLAKEMAPD LILDGEFQFD AAFVPEVAKK KAPDSVIQGD ANVFIFPSLE AGNIGYKIAQ RLGGFEAVGP ILQGLNKPVN DLSRGCSAED AYKLALITAA QSLGE

    • Unit Definition

      1 unit will convert 1umole of Coenzyme A to acetyl coenzyme A /min/pH-7.5/30˚C using acetyl phosphate as substrate

    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.

    Phosphotransacetylase
  • 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 :

    FUCA2 Human

    Description:

    Fucosidase Alpha-L- 2 Plasma Human Recombinant

    Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    Product # :

    ENZ-840

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    Description

    FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.

    • Synonyms

      Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.

    • 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 MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.

    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.

    Fuca2 Human
  • View Data Sheet

    Name :

    UPP1 Human

    Description:

    Uridine Phosphorylase 1 Human Recombinant

    UP, UPASE, UPP, UrdPase 1.

    Product # :

    ENZ-560

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    Description

    UPP1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UPP1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.2M NaCl and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.

    • Synonyms

      UP, UPASE, UPP, UrdPase 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 MAATGANAEK AESHNDCPVR LLNPNIAKMK EDILYHFNLT TSRHNFPALF GDVKFVCVGG SPSRMKAFIR CVGAELGLDC PGRDYPNICA GTDRYAMYKV GPVLSVSHGM GIPSISIMLH ELIKLLYYAR
      CSNVTIIRIG TSGGIGLEPG TVVITEQAVD TCFKAEFEQI VLGKRVIRKT DLNKKLVQEL LLCSAELSEF TTVVGNTMCT LDFYEGQGRL DGALCSYTEK DKQAYLEAAY AAGVRNIEME SSVFAAMCSA CGLQAAVVCV TLLNRLEGDQ
      ISSPRNVLSE YQQRPQRLVS YFIKKKLSKA.

    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.

    Upp1 Human
  • View Data Sheet

    Name :

    NAA10 Human

    Description:

    N Alpha-Acetyltransferase 10, NatA Catalytic Subunit Human Recombinant

    N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    Product # :

    ENZ-158

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    Description

    NAA10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 255 amino acids (1-235 a.a.) and having a molecular mass of 28.6kDa (the molecular weight on SDS-PAGE will appear higher).NAA10 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAA10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 10% glycerol and 200mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NAA10 is a member of the acetyltransferase family. NAA10 interacts with NAA15, HIF-1 and with the ribosome. In its binding to HIF-1, NAA10 functions as a protein acetyltransferase by regulating its stability. In various cell lines, NAA10 is downregulated in response to hypoxia. NAA10 is expressed during the course of the development of the brain.

    • Synonyms

      N-alpha-acetyltransferase 10, N-terminal acetyltransferase complex ARD1 subunit homolog A, NatA catalytic subunit, NAA10, ARD1, ARD1A, TE2, NATD, DXS707.

    • 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 MNIRNARPED LMNMQHCNLL CLPENYQMKY YFYHGLSWPQ LSYIAEDENG KIVGYVLAKM EEDPDDVPHG HITSLAVKRS HRRLGLAQKL MDQASRAMIE NFNAKYVSLH VRKSNRAALH LYSNTLNFQI SEVEPKYYAD GEDAYAMKRD LTQMADELRR HLELKEKGRH VVLGAIENKV ESKGNSPPSS GEACREEKGL AAEDSGGDSK DLSEVSETTE STDVKDSSEA SDSAS.

    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.

    Naa10 Human
  • View Data Sheet

    Name :

    PCOLCE Human

    Description:

    Procollagen C-Endopeptidase Enhancer Human Recombinant

    Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 1.

    Product # :

    ENZ-863

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    Description

    PCOLCE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids (26-449 a.a) and having a molecular mass of 47.9kDa. PCOLCE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Procollagen C-endopeptidase enhancer 1, also known as PCOLCE binds to the C-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity. In addition, C-terminal processed part of PCPE (CT-PCPE) has a metalloproteinase inhibitory activity. Among the diseases which are associated with PCOLCE: bone fracture & oculopharyngeal muscular dystrophy.

    • Synonyms

      Procollagen C-Endopeptidase Enhancer, Procollagen C-Proteinase Enhancer 1, Type I Procollagen COOH-Terminal Proteinase Enhancer, Type 1 Procollagen C-Proteinase Enhancer Protein, Procollagen COOH-Terminal Proteinase Enhancer 1, PCPE-1, PCPE1, Procollagen, Type 1, COOH-Terminal Proteinase Enhancer, Procollagen C-Endopeptidase Enhancer 1, COOH-Terminal Proteinase Enhancer, Procollagen, Type 1, PCPE, Procollagen C-endopeptidase enhancer 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 MGSQTPNYTR PVFLCGGDVK GESGYVASEG FPNLYPPNKE CIWTITVPEG QTVSLSFRVF DLELHPACRY DALEVFAGSG TSGQRLGRFC GTFRPAPLVA PGNQVTLRMT TDEGTGGRGF LLWYSGRATS GTEHQFCGGR LEKAQGTLTT PNWPESDYPP GISCSWHIIA PPDQVIALTF EKFDLEPDTY CRYDSVSVFN GAVSDDSRRL GKFCGDAVPG SISSEGNELL VQFVSDLSVT ADGFSASYKT LPRGTAKEGQ GPGPKRGTEP KVKLPPKSQP PEKTEESPSA PDAPTCPKQC RRTGTLQSNF CASSLVVTAT VKSMVREPGE GLAVTVSLIG AYKTGGLDLP SPPTGASLKF YVPCKQCPPM KKGVSYLLMG QVEENRGPVL PPESFVVLHR PNQDQILTNL SKRKCPSQPV RAAASQD.

    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.

    Pcolce Human
  • View Data Sheet

    Name :

    UNG E.Coli

    Description:

    Uracil DNA Glycosylase E.Coli Recombinant

    UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.

    Product # :

    ENZ-752

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    Description

    UNG E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (1-229 a.a) and having a molecular mass of 28.1kDa.UNG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      UNG is a member of the Uracil-DNA glycosylase family. One of his functions is to prevent mutagenesis by eliminating uracil from DNAmolecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil basesare formed as a result of cytosine deamination or misincorporation of dUMP residues. After a mutation is formed, the mutagenicthreat of uracil propagates through any subsequent DNA replication steps. Among the diseases associated with UNG are: congenital rubella, and immunodeficiency with hyper igm type 4.

    • Synonyms

      UDG, b2580, JW2564, EC 3.2.2.27, DGU, UNG15, HIGM5, Uracil-DNA Glycosylase 1, EC 3.2.2, HIGM4, UNG2.

    • 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 MGSMANELTW HDVLAEEKQQ PYFLNTLQTV ASERQSGVTI YPPQKDVFNA FRFTELGDVK VVILGQDPYH GPGQAHGLAF SVRPGIAIPP SLLNMYKELE NTIPGFTRPN HGYLESWARQ GVLLLNTVLT VRAGQAHSHA SLGWETFTDK VISLINQHRE GVVFLLWGSH AQKKGAIIDK QRHHVLKAPH PSPLSAHRGF FGCNHFVLAN QWLEQRGETP IDWMPVLPAE SE

    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.

    Ung Ecoli
  • View Data Sheet

    Name :

    GGPS1 Human

    Description:

    Geranylgeranyl Diphosphate Synthase 1 Human Recombinant

    GGPPS, GGPPS1, GGPP synthetase.

    Product # :

    ENZ-555

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    • description
    • source
    • formulation
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    Description

    GGPS1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 320 amino acids (1-300 a.a.) and having a molecular mass of 37 kDa. The GGPS1 is fused to a 20 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GGPS1 Human recombinant (1mg/ml) protein solution contains 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GGPS1 is PART of the prenyltransferase family. GGPS1 is widely expressed in testis, heart and skeletal muscle, GGPS1 is localized in the cytoplasm and catalyzes the formation of geranylgeranyl pyrophosphate, a precursor of geranylgeranylated proteins and carotenoids. GGPS1 is a significant enzyme that is responsible for the C20-prenylation of proteins and for the regulation of a nuclear hormone receptor.

    • Synonyms

      GGPPS, GGPPS1, GGPP synthetase.

    • 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 MEKTQETVQR ILLEPYKYLL QLPGKQVRTK LSQAFNHWLK VPEDKLQIII EVTEMLHNAS LLIDDIEDNS KLRRGFPVAH SIYGIPSVIN SANYVYFLGL EKVLTLDHPD AVKLFTRQLL ELHQGQGLDI YWRDNYTCPT EEEYKAMVLQ KTGGLFGLAV
      GLMQLFSDYK EDLKPLLNTL GLFFQIRDDY ANLHSKEYSE NKSFCEDLTE GKFSFPTIHA IWSRPESTQV QNILRQRTEN IDIKKYCVHY LEDVGSFEYT RNTLKELEAK AYKQIDARGG NPELVALVKH LSKMFKEENE.

    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.

    Ggps1 Human
  • 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

    Price :

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    • description
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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.

    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.

    Gfpt1 Human
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