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1000 results found for “Decarboxylase”
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Name :
UCHL5 HumanDescription:
Ubiquitin Carboxyl-Terminal Esterase L5 Human Recombinant
Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.
Product # :
ENZ-097Price :
Quantity :
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Shipped with Ice Packs
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Description
UCHL5 produced in E.Coli is a single, non-glycosylated polypeptide chain containing349 amino acids (1-329a.a.) and having a molecular mass of 39.7kDa.UCHL5 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The UCHL5 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 5mM DTT, 200mM NaCl, 0.1mM PMSF, 2mM EDTA and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity: > 500 pmole/min/ug. Measured by the hydrolysis of Ubiquitin-AMC at
pH 8.0, at 37°C.More Info
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Introduction
UCHL5 is a member of the peptidase C12 family. UCHL5 protein is a protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains, and deubiquitinating enzyme related to the 19S regulatory subunit of the 26S proteasome.
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Synonyms
Ubiquitin Carboxyl-terminal Hydrolase L5, UCH37, CGI-70, UCH-L5, INO80R, Ubiquitin thioesterase L5, INO80 complex subunit R, EC 3.4.19.12, Ubiquitin Carboxyl-terminal Esterase L5.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHHSSGLVPRGSH MTGNAGEWCL MESDPGVFTE LIKGFGCRGA QVEEIWSLEP ENFEKLKPVH GLIFLFKWQP GEEPAGSVVQ DSRLDTIFFA KQVINNACAT QAIVSVLLNC THQDVHLGET LSEFKEFSQS FDAAMKGLAL SNSDVIRQVH NSFARQQMFE FDTKTSAKEE DAFHFVSYVP VNGRLYELDG LREGPIDLGA CNQDDWISAV RPVIEKRIQK YSEGEIRFNL MAIVSDRKMI YEQKIAELQR QLAEEEPMDT DQGNSMLSAI QSEVAKNQML IEEEVQKLKR YKIENIRRKH NYLPFIMELL KTLAEHQQLI PLVEKAKEKQ NAKKAQETK
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.
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Name :
GMPS HumanDescription:
GMPS Human Recombinant
GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.
Product # :
ENZ-244Price :
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Description
GMPS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 717 amino acids (1-693) and having a molecular mass of 79.2kDa.GMPS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GMPS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GMP synthase (GMPS) is involved in purine biosynthesis. GMPS, which is a homodimer, catalyzes the last step in the GMP synthesis pathway, specifically the ATP-dependent amination of XMP to GMP. GMPS is comprised of one GMP-binding domain and one glutamine amidotransferase type-1 domain through which it communicates its catalytic activity. GMPS is engaged in the de novo synthesis of nucleotides which are not only vital for DNA and RNA synthesis, but also supply GTP, which is involved in sevral cellular processes important for cell division. GMPS gene chromosomal translocations are linked with acute myeloid leukemias, suggesting a possible role for GMPS in carcinogenesis.
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Synonyms
GMP synthase [glutamine-hydrolyzing], GMP synthetase, Glutamine amidotransferase, GMPS, GMP synthase, guanosine 5'-monophosphate synthase, MLL/GMPS fusion protein.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMALCNG DSKLENAGGD LKDGHHHYEG AVVILDAGAQ YGKVIDRRVR ELFVQSEIFP LETPAFAIKE QGFRAIIISG GPNSVYAEDA PWFDPAIFTI GKPVLGICYG MQMMNKVFGG TVHKKSVRED GVFNISVDNT CSLFRGLQKE EVVLLTHGDS
VDKVADGFKV VARSGNIVAG IANESKKLYG AQFHPEVGLT ENGKVILKNF LYDIAGCSGT FTVQNRELEC IREIKERVGT SKVLVLLSGG VDSTVCTALL NRALNQEQVI AVHIDNGFMR KRESQSVEEA LKKLGIQVKV INAAHSFYNG TTTLPISDED RTPRKRISKT LNMTTSPEEK
RKIIGDTFVK IANEVIGEMN LKPEEVFLAQ GTLRPDLIES ASLVASGKAE LIKTHHNDTE LIRKLREEGK VIEPLKDFHK DEVRILGREL GLPEELVSRH PFPGPGLAIR VICAEEPYIC KDFPETNNIL KIVADFSASV KKPHTLLQRV KACTTEEDQE KLMQITSLHS LNAFLLPIKT
VGVQGDCRSY SYVCGISSKD EPDWESLIFL ARLIPRMCHN VNRVVYIFGP PVKEPPTDVT PTFLTTGVLS TLRQADFEAH NILRESGYAG KISQMPVILT PLHFDRDPLQ KQPSCQRSVV IRTFITSDFM TGIPATPGNE IPVEVVLKMV TEIKKIPGIS RIMYDLTSKP PGTTEWE.
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.
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Name :
AKR1C3 HumanDescription:
Aldo-Keto Reductase Family 1 Member C3 Human Recombinant
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
Product # :
ENZ-1131Price :
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Description
AKR1C3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 323 amino acids (1-323) and having a molecular mass of 36.8 kDa.AKR1C3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The AKR1C3 solution (1mg/ml) contains 10% Glycerol, 0.1M NaCl, 1mM DTT and 20mM Tris-HCl buffer (pH 8.5).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000pmol/min/ug. It is defined by the amount of enzyme that catalyzes oxidation of 1.0pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25˚C.
More Info
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Introduction
Aldo-keto reductase family 1 member C3 isoform 1 or AKR1C3 is an enzyme, part of the aldo-keto reductase family that promotes conversion of ketones & aldehydes to the alcohol forms while using cofactors such as NADPH & NADH. AKR1C3 promotes the reduction of PG molecule (prostaglandin), PQ (phenanthrenequinone) & PGH2. Another role is oxidation of 9 alpha, 11 beta-PGF2 to PGD2. AKR1C3 holds a crucial part in the pathogenesis of allergic diseases like asthma and can also take part in the regulation of cell growth and differentiation.
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Synonyms
DD3, DDX, HAKRB, HAKRe, HA1753, HSD17B5, hluPGFS, KIAA0119, AKR1C3, Aldo-keto reductase family 1 member C3, 3-alpha-HSD type 2, 17-beta-HSD 5, PGFS, DD-3.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MDSKHQCVKL NDGHFMPVLG FGTYAPPEVP RSKALEVTKL AIEAGFRHID SAHLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWSTFH RPELVRPALE NSLKKAQLDY VDLYLIHSPM SLKPGEELSP TDENGKVIFD IVDLCTTWEA MEKCKDAGLA KSIGVSNFNR RQLEMILNKP GLKYKPVCNQ VECHPYFNRS KLLDFCKSKD IVLVAYSALG SQRDKRWVDP NSPVLLEDPV
LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIRQN VQVFEFQLTA EDMKAIDGLD RNLHYFNSDS FASHPNYPYS DEY
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.
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Name :
GLRX2 YeastDescription:
Glutaredoxin 2 Yeast Recombinant
Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2.
Product # :
ENZ-360Price :
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Description
Glutaredoxin-2 Saccharamyces cerevisiae Recombinant containing 6x His tag at C-terminus produced in E.Coli is a single, non-glycosylated, Polypeptide chain having a molecular mass of 17 kDa.
Source
Escherichia Coli.
Formulation
Glutaredoxin-2 solution contains 25mM Tris-HCl pH-7.5 & 0.01% Na Azide.
Purity
Purity of GRX2 is greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.
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Synonyms
Thioltransferase, Glutathione-dependent oxidoreductase 2, TTR, TTR1, GLRX2, GRX2, GRX-2, GLRX-2, Glutaredoxin 2.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
1 week at 2-10°C. For long term store at -20 to -80°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.
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Name :
GUK1 Human, ActiveDescription:
Guanylate Kinase 1 Human Recombinant, Active
GMK, GMP kinase.
Product # :
PKA-309Price :
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Description
GUK1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (1-197 a.a.)and having a total molecular mass of 23.9 kDa. GUK1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GUK1 1mg/ml protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100 units/mg and is defined as the amount of enzyme that convert 1.0 umole of GMP and ATP to GDP and ADP per minute at pH 7.5 at 37C in coupled system with PK/LDH.More Info
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Introduction
GUK1 is part of the guanylate kinase family. GUK1 occurs as a monomer that catalyzes the ATP-dependent conversion of GMP to GDP, thus takes an important part in the recycling of GMP. Through its catalytic activity, GUK1 functions in regulation of the supply of guanine nucleotides to signal transduction pathways. GUK1 overexpression is related with pituitary adenocarcinomas, implicating that GUK1 is has a role in tumorigenesis.
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Synonyms
GMK, GMP kinase.
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Physical Appearance
Sterile Filtered colorless clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSGPRPVVLS GPSGAGKSTL LKRLLQEHSG IFGFSVSHTT RNPRPGEENG KDYYFVTREV MQRDIAAGDF IEHAEFSGNL YGTSKVAVQA VQAMNRICVL DVDLQGVRNI KATDLRPIYI SVQPPSLHVL EQRLRQRNTE TEESLVKRLA AAQADMESSK EPGLFDVVII NDSLDQAYAE LKEALSEEIK KAQRTGA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GPT2 Mouse, ActiveDescription:
Glutamic-Pyruvate Transaminase 2, Active Mouse Recombinant
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-1110Price :
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Shipped with Ice Packs
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Description
GPT2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 542 amino acids (1-522 aa) and having a molecular mass of 60.1kDa.GPT2 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPT2 solution (1 mg/ml) contains 2mM DTT, 20% Glycerol and 20mM Tris-HCl (pH7.5).
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 50 units/mg. Measured by the amount of enzyme that cleaves 1umole of L-Alanineto L-Glutamate per minute at pH7.5 at 37C˚.
More Info
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Introduction
Glutamic-Pyruvate Transaminase 2 (GPT2) catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids.
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Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQRAAVLVRR GSCPRASGPW GRSHSSAAAE ASAALKVRPE
RSPRDRILTL ESMNPQVKAV EYAVRGPIVL KAGEIEMELQ RGIKKPFTEV IRANIGDAHA
MGQQPITFLR QVMALCTYPN LLNSPSFPED AKKRARRILQ ACGGNSLGSY SASQGVNCIR
EDVAAFITRR DGVPADPDNI YLTTGASDGI STILKLLVSG GGKSRTGVMI PIPQYPLYSA
VISELDAVQV NYYLDEENCW ALNVDELRRA LRQAKDHCDP KVLCIINPGN PTGQVQSRKC
IEDVIHFAWE EKLFLLADEV YQDNVYSPDC RFHSFKKVLY QMGHEYSSNV ELASFHSTSK
GYMGECGYRG GYMEVINLHP EIKGQLVKLL SVRLCPPVSG QAAMDIVVNP PEPGEESFEQ
FSREKEFVLG NLAKKAKLTE DLFNQVPGIQ CNPLQGAMYA FPRILIPAKA VEAAQSHKMA
PDMFYCMKLL EETGICVVPG SGFGQREGTY HFRMTILPPV DKLKTVLHKV KDFHLKFLEQ YS
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.
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Name :
MAT2A HumanDescription:
Methionine Adenosyltransferase II Alpha Human Recombinant
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
Product # :
ENZ-320Price :
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Shipped with Ice Packs
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Description
MAT2A Human Recombinant fused with His tag (20 a.a.) at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 45.8 kDa.The MAT2A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAT2A solution (1mg/ml) contains 20mM Tris pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.
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Synonyms
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY.
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.
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Name :
GPX3 HumanDescription:
Glutathione Peroxidase 3 Human Recombinant
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
Product # :
ENZ-579Price :
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Shipped with Ice Packs
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Description
GPX3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (21-226) and having a molecular mass of 25.7kDa.GPX3 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GPX3 solution contains 20mM Tris-HCl buffer (pH7.5), 40% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Glutathione peroxidase 3 (GPX3) is a member of the glutathione peroxidase family, which acts in the detoxification of hydrogen peroxide. GPX3 shields cells and enzymes from oxidative damage, by catalyzing the reduction of hydrogen peroxide, lipid peroxides and organic hydroperoxide, by glutathione. The GPX3 protein is one of only a few proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by the nonsense (stop) codon TGA.
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Synonyms
Glutathione peroxidase 3, GPx-3, GSHPx-3, Extracellular glutathione peroxidase, Plasma glutathione peroxidase, GPx-P, GSHPx-P, GPX3, GPXP.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGQEKSK MDCHGGISGT IYEYGALTID GEEYIPFKQY AGKYVLFVNV ASYCGLTGQY IELNALQEEL APFGLVILGF PCNQFGKQEP GENSEILPTL KYVRPGGGFV PNFQLFEKGD VNGEKEQKFY TFLKNSCPPT SELLGTSDRL FWEPMKVHDI RWNFEKFLVG PDGIPIMRWH HRTTVSNVKM DILSYMRRQA ALGVKRK.
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.
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Name :
MSRB2 HumanDescription:
Methionine Sulfoxide Reductase B2 Human Recombinant
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
Product # :
ENZ-036Price :
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Description
MSRB2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (21-182a.a.) and having a molecular mass of 19.5kDa.MSRB2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MSRB2 protein solution (1mg/1ml) is formulated in In 20 mM Tris-HCl Buffer (pH 7.5), 1 mM DTT, 0.1 mM PMSF and 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
MSRB2 is a member of the methionine sulfoxide reductases(MSRs) family which are antioxidant repair enzymes. MSRB2 protein catalyzes the decrease of free and protein-bound methionine sulfoxide to methionine. MSRB2 has a part in protecting against oxidative stress in numerous organs.
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Synonyms
CBS-1, PILB, Pilin-like Transcription Factor, MSRB, CGI-131, Mmethionine Sulfoxide Reductase B2, Methionine-R-Sulfoxide Reductase B2 Mitochondrial, MGC26104, MsrB2. EC 1.8.4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVRGQAGGGG PGTGPGLGEA GSLATCELPL AKSEWQKKLT PEQFYVTREK GTEPPFSGIY LNNKEAGMYH CVCCDSPLFS SEKKYCSGTG WPSFSEAHGT SGSDESHTGI LRRLDTSLGS ARTEVVCKQC EAHLGHVFPD GPGPNGQRFC INSVALKFKP RKH
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.
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Name :
UBE2L6 HumanDescription:
Ubiquitin Conjugating Enzyme E2L 6 Human Recombinant
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
Product # :
ENZ-347Price :
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Shipped with Ice Packs
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Description
UBE2L6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a.) & having a molecular mass of 21.7 kDa. The UBE2L6 is fused to a 36 amino acid His Tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris pH-8, 0.1mM PMSF, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
UBE2L6 belongs to the E2 ubiquitin-conjugating enzyme family. UBE2L6 enzyme is very similar in its primary structure to the enzyme encoded by UBE2L3 gene. UBE2L6 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2L6 functions in the e6/e6-ap-induced ubiquitination of p53/tp53.
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Synonyms
RIG-B, UBCH8, MGC40331, UBE2L6, Ubiquitin/ISG15-conjugating enzyme E2 L6, Ubiquitin-protein ligase L6, Ubiquitin carrier protein L6, Retinoic acid-induced gene B protein.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMASM RVVKELEDLQ KKPPPYLRNL SSDDANVLVW HALLLPDQPP YHLKAFNLRI SFPPEYPFKP PMIKFTTKIY HPNVDENGQI CLPIISSENW KPCTKTCQVL EALNVLVNRP NIREPLRMDL ADLLTQNPEL FRKNAEEFTL RFGVDRPS.
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.
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Name :
GSS HumanDescription:
Glutathione Synthetase Human Recombinant
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
Product # :
ENZ-021Price :
Quantity :
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Description
GSS 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 494 amino acids (1-474 a.a.) and having a molecular mass of 54.5kDa. The GSS is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Glutathione synthetase (GSS) is the second enzyme in the glutathione biosynthesis pathway. GSS catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Defects in the GSS are the cause of glutathione synthetase deficiency aka GSS deficiency or 5-oxoprolinuria or pyroglutamic aciduria, which is a severe form characterized by an increased rate of hemolysis and defective function of the central nervous system.
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Synonyms
Glutathione synthetase, GSH synthetase, GSH-S, Glutathione synthase, GSHS, MGC14098, GSS.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHQH SSGLVPRGSH MATNWGSLLQ DKQQLEELAR QAVDRALAEG VLLRTSQEPT SSEVVSYAPF TLFPSLVPSA LLEQAYAVQM DFNLLVDAVS QNAAFLEQTL SSTIKQDDFT ARLFDIHKQV LKEGIAQTVF LGLNRSDYMF QRSADGSPAL KQIEINTISA SFGGLASRTP AVHRHVLSVL SKTKEAGKIL SNNPSKGLAL GIAKAWELYG SPNALVLLIA QEKERNIFDQRAIENELLAR NIHVIRRTFE DISEKGSLDQ DRRLFVDGQE IAVVYFRDGY MPRQYSLQNW EARLLLERSH AAKCPDIATQ LAGTKKVQQE LSRPGMLEML LPGQPEAVAR LRATFAGLYS LDVGEEGDQA IAEALAAPSR FVLKPQREGG GNNLYGEEMV QALKQLKDSE ERASYILMEK IEPEPFENCL LRPGSPARVV QCISELGIFG VYVRQEKTLV MNKHVGHLLR TKAIEHADGG VAAGVAVLDN PYPV.
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.
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Name :
AHCY Human, Sf9Description:
Adenosylhomocysteinase Human Recombinant, Sf9
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
Product # :
ENZ-1034Price :
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Description
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
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Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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.
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Name :
TARS HumanDescription:
Threonyl-tRNA Synthetase Human Recombinant
Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.
Product # :
ENZ-571Price :
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Description
TARS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 743 amino acids (1-723) and having a molecular mass of 85.6kDa.TARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TARS solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 150mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Threonyl-tRNA synthetase, cytoplasmic (TARS) is a member of the class-II aminoacyl-tRNA synthetase family. The main role of TARS is in tRNA aminoacylation. The N-terminal domain of the TARS enzyme is responsible for the competition with the ribosome whereas the catalytic and the C-terminal domain are involved in binding the 2 anticodon arm-like structures in the operator.
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Synonyms
Threonine--tRNA ligase, cytoplasmic, Threonyl-tRNA synthetase, ThrRS, TARS.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MFEEKASSPS GKMGGEEKPI GAGEEKQKEG GKKKNKEGSG DGGRAELNPW PEYIYTRLEM YNILKAEHDS ILAEKAEKDS KPIKVTLPDG KQVDAESWKT TPYQIACGIS QGLADNTVIA KVNNVVWDLD RPLEEDCTLE LLKFEDEEAQ AVYWHSSAHI MGEAMERVYG GCLCYGPPIE NGFYYDMYLE EGGVSSNDFS SLEALCKKII KEKQAFERLE VKKETLLAMF KYNKFKCRIL NEKVNTPTTT VYRCGPLIDL CRGPHVRHTG KIKALKIHKN SSTYWEGKAD METLQRIYGI SFPDPKMLKE WEKFQEEAKN RDHRKIGRDQ ELYFFHELSP
GSCFFLPKGA YIYNALIEFI RSEYRKRGFQ EVVTPNIFNS RLWMTSGHWQ HYSENMFSFE VEKELFALKP MNCPGHCLMF DHRPRSWREL PLRLADFGVL HRNELSGALT GLTRVRRFQQ DDAHIFCAME QIEDEIKGCL DFLRTVYSVF GFSFKLNLST RPEKFLGDIE VWDQAEKQLE NSLNEFGEKW ELNSGDGAFY GPKIDIQIKD AIGRYHQCAT IQLDFQLPIR FNLTYVSHDG DDKKRPVIVH RAILGSVERM IAILTENYGG KWPFWLSPRQ VMVVPVGPTC DEYAQKVRQQ FHDAKFMADI DLDPGCTLNK KIRNAQLAQY NFILVVGEKE KISGTVNIRT RDNKVHGERT ISETIERLQQ LKEFRSKQAE EEF.
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.
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Name :
ENO2 ProteinDescription:
Enolase-2 Human
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-371Price :
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Description
Human Neurone Specific Enolase produced in Human CNS having a molecular mass of 45kDa.
Source
Human CNS.
Formulation
The protein solution is in 10mM NaH2PO4 buffer pH 7.4 containing 150mM NaCl and 5mM MgSO4.
Purity
Greater than 96.0%.
More Info
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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.
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Synonyms
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Human NSE although stable at 4°C for 1 week, should be stored at -18°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.
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Name :
GPT2 HumanDescription:
Glutamic-Pyruvate Transaminase 2 Human Recombinant
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
Product # :
ENZ-680Price :
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Description
GPT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 546 amino acids (1-523) and having a molecular mass of 60.3 kDa. GPT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 7.5), 30% glycerol, 0.2M NaCl and 2mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Alanine aminotransferase 2 (GPT2), catalyzes the reversible transamination among alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT2 expressed mainly in muscle, fat and kidney and participates in the intermediary metabolism of glucose and amino acids. Multiple transcript variants encoding various isoforms have been found for GPT2.
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Synonyms
ALT2, AAT2, Alanine aminotransferase 2, Glutamate pyruvate transaminase 2, Glutamic--alanine transaminase 2, Glutamic--pyruvic transaminase 2.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQRAAAL VRRGCGPRTP SSWGRSQSSA AAEASAVLKV RPERSRRERI LTLESMNPQV KAVEYAVRGP IVLKAGEIEL ELQRGIKKPF TEVIRANIGD AQAMGQQPIT FLRQVMALCT YPNLLDSPSF PEDAKKRARR ILQACGGNSL GSYSASQGVN CIREDVAAYI TRRDGGVPAD PDNIYLTTGA SDGISTILKI LVSGGGKSRT GVMIPIPQYP LYSAVISELD AIQVNYYLDE ENCWALNVNE LRRAVQEAKD HCDPKVLCII NPGNPTGQVQ SRKCIEDVIH FAWEEKLFLL ADEVYQDNVY SPDCRFHSFK KVLYEMGPEY SSNVELASFH STSKGYMGEC GYRGGYMEVI NLHPEIKGQL VKLLSVRLCP PVSGQAAMDI VVNPPVAGEE SFEQFSREKE SVLGNLAKKA KLTEDLFNQV PGIHCNPLQG AMYAFPRIFI PAKAVEAAQA HQMAPDMFYC MKLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPVEKLKTV LQKVKDFHIN FLEKYA.
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.
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Name :
ADAT1 HumanDescription:
Adenosine Deaminase tRNA-Specific 1 Human Recombinant
tRNA-specific adenosine deaminase 1, hADAT1, tRNA-specific adenosine- 37 deaminase, ADAT1, ADAT-1.
Product # :
ENZ-307Price :
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Description
Adenosine Deaminase tRNA-Specific 1 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide chain containing amino acids 1-502 and having a total molecular mass of 57.7 kda. ADAT-1 contains T7 tag at N-terminus. ADAT1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Adenosine Deaminase tRNA-Specific-1 at 0.1mg/ml, 10mM Tris, pH 8.0, 0.1% Triton X-100, 0.002% NaN3.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
This gene is a member of the ADAR (adenosine deaminase acting on RNA) family. Using site-specific adenosine modification, proteins encoded by these genes participate in the pre-mRNA editing of nuclear transcripts. The protein encoded by this gene, tRNA-specific adenosine deaminase 1, is responsible for the deamination of adenosine 37 to inosine in eukaryotic tRNA.
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Synonyms
tRNA-specific adenosine deaminase 1, hADAT1, tRNA-specific adenosine- 37 deaminase, ADAT1, ADAT-1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Name :
Esterase D HumanDescription:
Esterase D,S-Formylglutathione Hydrolase Human Recombinant
S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.
Product # :
ENZ-447Price :
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Description
Esterase-D 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 302 amino acids (1-282 a.a.) and having a molecular mass of 33.6kDa.The Esterase-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Esterase-D solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.
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Synonyms
S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEDYDH SYYFIATFIT DHIRHHAKYL NA.
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.
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Name :
PFKM HumanDescription:
Phosphofructokinase, Muscle Human Recombinant
EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.
Product # :
PKA-365Price :
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Description
PFKM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 800 amino acids (1-780 a.a.) and having a molecular mass of 87.3 kDa. PFKM protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
PFKM Human solution containing 20mM Trsi HCl pH-8, 5mM DTT, 0.2M NaCl and 20% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PFKM is a regulatory glycolytic enzyme that converts fructose 6-phosphate and ATP into fructose 1,6-bisphosphate (through PFK-1), fructose 2,6-bisphosphate (through PFK-2) and ADP. Three phosphofructokinase isozymes exist in humans: muscle, liver and platelet. Mutations in PFKM gene have been related with glycogen storage disease type VII, also identified as Tarui disease.
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Synonyms
EC 2.7.1.11, GSD7, PFK-1, PFK1, PFKA, PFKX, Phosphofructokinase-M, Phosphofructokinase 1, Phosphohexokinase, Phosphofructo-1-kinase isozyme A, MGC8699, PFKM.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD GGDHIKEATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAYNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLSDLQ KAGKITDEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIMEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK AMDEKKFDEA LKLRGRSFMN NWEVYKLLAH VRPPVSKSGS HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF QPVAELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI TRKRSGEAAV.
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.
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Name :
ACE2 RatDescription:
Angiotensin Converting Enzyme 2 Rat Recombinant
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
Product # :
ENZ-1124Price :
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Description
ACE2 Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.7kDa. ACE2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of McaYVADAPK(Dnp)-OH per minute at pH 7.5, at 25C.
More Info
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Introduction
Angiotensin converting enzyme 2 or ACE-2 is an enzyme that is located in the cell membranes in different organs such as kidney, intestines, lungs, heart & arteries. ACE2 acts as an entry receptor of SARS coronaviruses & SARS-CoV-2.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen bound to the external envelope of the virion that has a role in a crucial part in viral infection by identifying host cell receptors and starting fusion of the viral and cellular membranes. Couple of main domains in coronavirus S1 have been identified, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains acts as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 has a signal peptide, a transmembrane domain & a single metalloproteinase active site holds an HEXXH zinc-binding domain. ACE-2 takes part as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Synonyms
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVTLEHHHHH 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.
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Name :
FN3K HumanDescription:
Fructosamine 3 Kinase Human Recombinant
Fructosamine-3-kinase, FN3K.
Product # :
PKA-049Price :
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Description
FN3K 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 37kDa.FN3K is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FN3K protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fructosamine 3 Kinase (FN3K) catalyzes the phosphorylation of fructosamines which may result in deglycation, the non-enzymatic reaction of glucose with primary amines followed by Amadori re-arrangement. Phosphorylation of fructosamines instigates metabolism of the modified amine and brings about the de-glycation of fructoselysine and of glycated proteins. A high concentration of glucose may affect non-enzymatic oxidation of proteins by reaction of glucose and lysine residues (glycation). Fructosamines, the proteins altered in this way, are less active or functional.
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Synonyms
Fructosamine-3-kinase, FN3K.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEQLLRA ELRTATLRAF GGPGAGCISE GRAYDTDAGP VFVKVNRRTQ ARQMFEGEVA SLEALRSTGL VRVPRPMKVI DLPGGGAAFV MEHLKMKSLS SQASKLGEQM ADLHLYNQKL REKLKEEENT VGRRGEGAEP QYVDKFGFHT VTCCGFIPQV NEWQDDWPTF FARHRLQAQL DLIEKDYADR EARELWSRLQ VKIPDLFCGL EIVPALLHGD LWSGNVAEDD VGPIIYDPAS FYGHSEFELA IALMFGGFPR SFFTAYHRKI PKAPGFDQRL LLYQLFNYLN HWNHFGREYR SPSLGTMRRL LK.
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.
- View Data Sheet
Name :
ADA HumanDescription:
Adenosine Deaminase Human Recombinant
Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.
Product # :
ENZ-147Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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- biological activity
- More Info
Description
ADA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 383 amino acids (1-363) and having a molecular mass of 42.9 kDa.The ADA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ADA protein 0.5mg/ml is supplied in 20mM Tris-HCL, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: approximately >25 units/mg. Enzymatic activity was confirmed by measuring the amount of enzyme that deaminates 1.0 umol of adenosine to inosine per minute at pH 7.5 at 25C.More Info
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Introduction
ADA catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. ADA has a vital part in purine metabolism and in adenosine homeostasis. ADA performs as a positive regulator of T-cell coactivation, by binding DPP4 which regulates lymphocyte-epithelial cell adhesion.
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Synonyms
Adenosine deaminase, Adenosine aminohydrolase, ADA1, EC 3.5.4.4.
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Physical Appearance
ADA is supplied as a sterile filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQTPAFDKP KVELHVHLDG SIKPETILYY GRRRGIALPA NTAEGLLNVI GMDKPLTLPD FLAKFDYYMP AIAGCREAIK RIAYEFVEMK AKEGVVYVEV RYSPHLLANS KVEPIPWNQA EGDLTPDEVV ALVGQGLQEG ERDFGVKARS ILCCMRHQPN WSPKVVELCK KYQQQTVVAI DLAGDETIPG SSLLPGHVQA YQEAVKSGIH RTVHAGEVGS AEVVKEAVDI LKTERLGHGY HTLEDQALYN RLRQENMHFE ICPWSSYLTG AWKPDTEHAV IRLKNDQANY SLNTDDPLIF KSTLDTDYQM TKRDMGFTEE EFKRLNINAA KSSFLPEDEK RELLDLLYKA YGMPPSASAG QNL
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.
- View Data Sheet
Name :
PDE6H HumanDescription:
Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
Product # :
ENZ-819Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
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- purity
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Description
PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.
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Synonyms
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.
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.
- View Data Sheet
Name :
CLPP HumanDescription:
ClpP Caseinolytic Peptidase Human Recombinant
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
Product # :
ENZ-115Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
CLPP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (57-277 a.a.) and having a molecular mass of 24.2kDa.CLPP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CLPP solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 2mM DTT, 20% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
ATP-dependent Clp protease proteolytic subunit (CLPP) is a member of the peptidase family S14. CLPP cleaves peptides in a variety of proteins in a manner which requires ATP hydrolysis. CLPP being the catalytic core of the Clp proteolytic complex is commonly involved in many cellular processes via the regulation of intracellular protein quality. CLPP is responsible for a somewhat general and central housekeeping function rather than for the degradation of specific substrates.
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Synonyms
Putative ATP-dependent Clp protease proteolytic subunit mitochondrial, Endopeptidase Clp, CLPP.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MPLIPIVVEQ TGRGERAYDI YSRLLRERIV CVMGPIDDSV ASLVIAQLLF LQSESNKKPI HMYINSPGGV VTAGLAIYDT MQYILNPICT WCVGQAASMG SLLLAAGTPG MRHSLPNSRI MIHQPSGGAR GQATDIAIQA EEIMKLKKQL YNIYAKHTKQ SLQVIESAME RDRYMSPMEA QEFGILDKVL VHPPQDGEDE PTLVQKEPVE AAPAAEPVPA ST.
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.
- View Data Sheet
Name :
MAT1A HumanDescription:
Methionine Adenosyltransferase I Alpha Human Recombinant
EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.
Product # :
ENZ-493Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
MAT1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 414 amino acids (1-395 a.a.) and having a molecular mass of 45.6 kDa. The MAT1A is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The MAT1A protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, 100mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAT1A catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. MAT1A is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in MAT1A gene are associated with methionine adenosyltransferase deficiency. MAT1A expression also correlates with a differentiated phenotype, whereas liver cells expressing MAT2A present a dedifferentiated phenotype and lowered AdoMet synthesis. Likewise, NFκB and TNFα cause a switch from MAT1A to MAT2A expression in human hepatocellular carcinoma (HCC), which facilitates cancer cell growth.
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Synonyms
EC 2.5.1.6, MAT, MATA1, SAMS, SAMS1, Methionine adenosyltransferase 1, S-adenosylmethionine synthase isoform type-1, AdoMet synthase 1, MAT 1, Methionine adenosyltransferase I/III, MAT-I/III, MAT1A, AMS1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHS SGLVPRGSHM NGPVDGLCDH SLSEGVFMFT SESVGEGHPD KICDQISDAV LDAHLKQDPN AKVACETVCK TGMVLLCGEI TSMAMVDYQR VVRDTIKHIG YDDSAKGFDF KTCNVLVALE QQSPDIAQCV HLDRNEEDVG AGDQGLMFGY ATDETEECMP LTIILAHKLN ARMADLRRSG LLPWLRPDSK TQVTVQYMQD NGAVIPVRIH TIVISVQHNE DITLEEMRRA LKEQVIRAVV PAKYLDEDTV YHLQPSGRFV IGGPQGDAGV TGRKIIVDTY GGWGAHGGGA FSGKDYTKVD RSAAYAARWV AKSLVKAGLC RRVLVQVSYA IGVAEPLSIS IFTYGTSQKT ERELLDVVHK NFDLRPGVIV RDLDLKKPIY QKTACYGHFG RSEFPWEVPR KLVF.
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.