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1000 results found for “Natural Enzymes”
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Name :
RNLS HumanDescription:
Renalase Human Recombinant
Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.
Product # :
ENZ-653Price :
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Description
RNLS Human Recombinant produced in E. coli is a single polypeptide chain containing 349 amino acids (18-342) and having a molecular mass of 38.8 kDa.RNLS is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The RNLS solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Renalase (RNLS) is a flavin adenine dinucleotide-dependent amine oxidase which is secreted into the blood from the kidney. RNLS acts as a hormone which metabolizes circulating catecholamines that have an active role in the sympathetic and parasympathetic nervous systems. High catecholamine concentration activates plasma RNLS and promotes its secretion and synthesis.
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Synonyms
Renalase FAD-Dependent Amine Oxidase, Chromosome 10 Open Reading Frame 59, Monoamine Oxidase-C, C10orf59, FLJ11218, Renalase, MAO-C, EC 1.4.-.-.
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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 MGSMALLRRQ TSGPLYLAVW DKAEDSGGRM TTACSPHNPQ CTADLGAQYI TCTPHYAKKH QRFYDELLAY GVLRPLSSPI EGMVMKEGDC NFVAPQGISS IIKHYLKESG AEVYFRHRVT QINLRDDKWE VSKQTGSPEQ FDLIVLTMPV PEILQLQGDI TTLISECQRQ QLEAVSYSSR YALGLFYEAG TKIDVPWAGQ YITSNPCIRF VSIDNKKRNI ESSEIGPSLV IHTTVPFGVT YLEHSIEDVQ ELVFQQLENI LPGLPQPIAT KCQKWRHSQV TNAAANCPGQ MTLHHKPFLA CGGDGFTQSN FDGCITSALC VLEALKNYI
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 :
COMT HumanDescription:
Catechol-O-Methyltransferase Human Recombinant
COMT, EC 2.1.1.6, Catechol O-methyltransferase.
Product # :
ENZ-400Price :
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Description
COMT Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (51-271 a.a.) & having a molecular mass of 24.4 kDa. The COMT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COMT protein in 20mM Tris-HCl buffer, pH-8, 1mM MgCl2 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
COMT catalyzes the transfer of a methyl group from S-adenosylmethionine (SAM) to catechol substrates such as the neurotransmitters. This O-methylation results in one of the main degradative pathways of the catecholamine transmitters. COMT COMT is located in the postsynaptic neuron and is involved in the metabolism of catechol estrogen drugs used in the treatment of hypertension, asthma, Parkinson disease and the inactivation of catecholamine neurotransmitters though enzymatic degradation. COMT appears in tissues in 2 forms, a soluble form and a membrane-bound form which differ in their N-termini. COMT inhibitors increase its availability and are used in the treatment of patients with Parkinson's disease.
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Synonyms
COMT, EC 2.1.1.6, Catechol O-methyltransferase.
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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
MGDTKEQRIL NHVLQHAEPG NAQSVLEAID TYCEQKEWAM NVGDKKGKIV DAVIQEHQPS VLLELGAYCG YSAVRMARLL SPGARLITIE INPDCAAITQ RMVDFAGVKD KVTLVVGASQ DIIPQLKKKY DVDTLDMVFL DHWKDRYLPD TLLLEECGLL RKGTVLLADN VICPGAPDFL AHVRGSSCFE CTHYQSFLEY REVVDGLEKA IYKGPGSEAG P.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Enterokinase Bovine HisDescription:
Enteropeptidase/ Enterokinase Bovine Recombinant His Tag
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
Product # :
ENZ-655Price :
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Description
Enterokinase Bovine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 241 amino acids with a 6 × His at C-terminus and having a molecular mass of 28.0kDa.The Enterokinase Bovine is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Bovine EK is supplied in 50mM Tris-HCl, pH 8.0, 0.5M NaCl and 50% glycerol.
More Info
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Introduction
Enteropeptidase or enterokinase is an enzymeinvolved in human digestion. It is produced by cells in the duodenum wall, and is secreted from duodenum's glands, the crypts of Lieberk?hn, whenever ingested food enters the duodenum from the stomach. Enteropeptidase has the critical job of turning trypsinogen(a zymogen) to trypsin, indirectly activating a number of pancreaticdigestive enzymes.
Enteropeptidase is a serine proteaseenzyme(EC3.4.21.9). Enteropeptidase is a part of the Chymotrypsin-clan of serine proteases, and is structurally similar to these proteins. -
Synonyms
Enteropeptidase, EC 3.4.21.9, Enterokinase, Serine protease 7, ENTK, MGC133046.
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Physical Appearance
Sterile liquid solution.
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Stability
One year when stored at -20°C. Please avoid freeze-thaw cycles.
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Unit Definition
One unit is defined as the amount of enzyme needed to cleave 50ug of fusion protein in 16 hours to 95% completion at 25°C in a buffer containing 25mM Tris-HCl, pH 7.6, 50mM NaCl, and 2mM CaCl2.
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 :
ACOT13 HumanDescription:
Acyl-CoA Thioesterase 13 Human Recombinant
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
Product # :
ENZ-004Price :
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Description
ACOT13 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 160 amino acids (1-140 a.a.) and having a molecular mass of 17.1kDa. The ACOT13 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACOT13 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
Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.
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Synonyms
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
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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 MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN.
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 :
Rhodanese HumanDescription:
Thiosulfate Sulfurtransferase Human Recombinant
EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.
Product # :
ENZ-459Price :
Quantity :
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Description
Recombinant Human Rhodanese produced in E.Coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-297 a.a) and having a molecular mass of 35.6 kDa. Rhodanese is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Rhodanese protein solution contains 20mM Tris-HCl, pH-8 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Rhodanese is a mitochondrial matrix enzyme that is encoded by the nucleus. Rhodanese is involved in cyanide detoxification, the formation of iron-sulfur proteins, and the modification of sulfur-containing enzymes. Rhodanese catalyzes the chemical reaction of thiosulfate & cyanide to sulfite & thiocyanate (detoxification). Rhodanese is part of the transferase family of proteins. Rhodanese includes two highly conservative domains, identified as rhodanese homology domains. In mammals, the majority of cyanide is converted to thiocyanate. Rhodanese has weak mercaptopyruvate sulfurtransferase activity.
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Synonyms
EC 2.8.1.1, TST, MGC19578, RDS, Thiosulfate sulfurtransferase, Rhodanese.
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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 MVHQVLYRAL VSTKWLAESI RTGKLGPGLR VLDASWYSPG TREARKEYLE RHVPGASFFD IEECRDTASP YEMMLPSEAG FAEYVGRLGI SNHTHVVVYD GEHLGSFYAP RVWWMFRVFG HRTVSVLNGG FRNWLKEGHP VTSEPSRPEP AVFKATLDRS LLKTYEQVLE NLESKRFQLV DSRSQGRFLG TEPEPDAVGL DSGHIRGAVN MPFMDFLTED GFEKGPEELR ALFQTKKVDL SQPLIATCRK GVTACHVALA AYLCGKPDVA VYDGSWSEWF RRAPPESRVS QGKSEKA.
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 :
PGAM2 HumanDescription:
Phosphoglycerate Mutase 2 Human Recombinant
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
Product # :
ENZ-578Price :
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Description
PGAM2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 30.9kDa.PGAM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGAM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Phosphoglycerate mutase 2 (PGAM2) is a member of the phosphoglycerate mutase family. PGAM is a dimeric enzyme which contains in separate tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). PGAM (Phosphoglycerate mutase) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. PGAM2 gene mutations cause muscle phosphoglycerate mutase efficiency, otherwise known as glycogen storage disease X.
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Synonyms
Phosphoglycerate mutase 2, BPG-dependent PGAM 2, Muscle-specific phosphoglycerate mutase, Phosphoglycerate mutase isozyme M, PGAM-M, PGAM2, PGAMM, GSD10.
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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 MATHRLVMVR HGESTWNQEN RFCGWFDAEL SEKGTEEAKR GAKAIKDAKM EFDICYTSVL KRAIRTLWAI LDGTDQMWLP VVRTWRLNER HYGGLTGLNK AETAAKHGEE QVKIWRRSFD IPPPPMDEKH PYYNSISKER RYAGLKPGEL PTCESLKDTI ARALPFWNEE IVPQIKAGKR VLIAAHGNSL RGIVKHLEGM SDQAIMELNL PTGIPIVYEL NKELKPTKPM QFLGDEETVR KAMEAVAAQG KAK.
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 :
CES1G MouseDescription:
Carboxylesterase 1G Mouse Recombinant
Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.
Product # :
ENZ-947Price :
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Description
CES1G produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 556 amino acids (19-565 a.a.) and having a molecular mass of 61.9kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions). CES1G is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CES1G 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.
Biological Activity
Specific activity is > 2,000 pmol/min/ug and is defined as the amount of enzyme that hydrolyze 1pmole of p-nitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37C.
More Info
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Introduction
Carboxylesterase 1 (CES1G) belongs to a large family of carboxylesterases that are liable for the hydrolysis of ester and amide bonds. CES1G is also participates in the detoxification of xenobiotics prodrugs. CES1G shares the serine hydrolase fold observed in other esterases. CES1G found in rats and mice and is expressed mainly in liver, but also in kidney and lung.
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Synonyms
Liver carboxylesterase 1, Acyl-coenzyme A:cholesterol acyltransferase, Carboxylesterase 1G, ES-x, CES1G.
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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
ADPHPSLPPV VHTVHGKVLG KYVTLEGFSQ PVAVFLGVPF AKPPLGSLRF APPEPAEPWS FVKHTTSYPP LCYQNPEAAL RLAELFTNQR KIIPHKFSED CLYLNIYTPA DLTQNSRLPV MVWIHGGGLV IDGASTYDGV PLAVHENVVV VVIQYRLGIW GFFSTEDEHS RGNWGHLDQV AALHWVQDNI ANFGGNPGSV TIFGESAGGE SVSVLVLSPL AKNLFHRAIA QSSVIFNPCL FGRAARPLAK KIAALAGCKT TTSAAMVHCL RQKTEDELLE VSLKMKFGTV DFLGDPRESY PFLPTVIDGV LLPKAPEEIL AEKSFNTVPY MVGINKHEFG WIIPMFLDFP LSERKLDQKT AASILWQAYP ILNISEKLIP AAIEKYLGGT EDPATMTDLF LDLIGDIMFG VPSVIVSRSH RDAGAPTYMY EYQYRPSFVS DDRPQELLGD HADELFSVWG APFLKEGASE EEINLSKMVM KFWANFARNG NPNGEGLPHW PEYDQKEGYL QIGVPAQAAH RLKDKEVDFW TELRAKETAE RSSHREHVEL HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAT2 HumanDescription:
Spermidine/Spermine N1-Acetyltransferase 2 Human Recombinant
Spermidine/spermine N1-acetyltransferase family member 2, Polyamine N-acetyltransferase 2, SSAT2, Thialysine N-epsilon-acetyltransferase, diamine acetyltransferase 2, S, EC 2.3.1.57.
Product # :
ENZ-587Price :
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Description
SAT2 Human Recombinant produced in E. coli is a single polypeptide chain containing 190 amino acids (1-170) and having a molecular mass of 21.0kDa.SAT2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SAT2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Spermidine/Spermine N1-Acetyltransferase 2, also known as SAT2 catalyzes the acetylation of polyamines (Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine).
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Synonyms
Spermidine/spermine N1-acetyltransferase family member 2, Polyamine N-acetyltransferase 2, SSAT2, Thialysine N-epsilon-acetyltransferase, diamine acetyltransferase 2, S, EC 2.3.1.57.
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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 MASVRIREAK EGDCGDILRL IRELAEFEKL SDQVKISEEA LRADGFGDNP FYHCLVAEIL PAPGKLLGPC VVGYGIYYFI YSTWKGRTIY LEDIYVMPEY RGQGIGSKII KKVAEVALDK GCSQFRLAVL DWNQRAMDLY KALGAQDLTE AEGWHFFCFQ GEATRKLAGK
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 :
GSTZ1 HumanDescription:
Glutathione Transferase Zeta 1 Human Recombinant
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
Product # :
ENZ-494Price :
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Description
GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
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Synonyms
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
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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 MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.
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 :
CPE HumanDescription:
Carboxypeptidase-E Human Recombinant
Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.
Product # :
ENZ-687Price :
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Description
CPE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (43-476 a.a.) and having a molecular mass of 51.4kDa. CPE is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CPE protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Carboxypeptidase-E (CPE ) is a carboxypeptidase that cleaves C-terminal amino acid residues and is involved in the biosynthesis of peptide hormones and neurotransmitters. CPE is a peripheral membrane protein. CPE specifically connects regulated secretory pathway proteins, including prohormones, but constitutively secreted proteins. Mutations in CPE are implicated in type II diabetes.
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Synonyms
Carboxypeptidase E, Carboxypeptidase H, CPH, CPE, CPE Human, Enkephalin convertase, Prohormone-processing carboxypeptidase.
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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 MGSLQQEDGI SFEYHRYPEL REALVSVWLQ CTAISRIYTV GRSFEGRELL VIELSDNPGV HEPGEPEFKY IGNMHGNEAV GRELLIFLAQ YLCNEYQKGN ETIVNLIHST RIHIMPSLNP DGFEKAASQP GELKDWFVGR SNAQGIDLNR NFPDLDRIVY VNEKEGGPNN HLLKNMKKIV DQNTKLAPET KAVIHWIMDI PFVLSANLHG GDLVANYPYD ETRSGSAHEY SSSPDDAIFQ SLARAYSSFN PAMSDPNRPP CRKNDDDSSF VDGTTNGGAW YSVPGGMQDF NYLSSNCFEI TVELSCEKFP PEETLKTYWE DNKNSLISYL EQIHRGVKGF VRDLQGNPIA NATISVEGID HDVTSAKDGD YWRLLIPGNY KLTASAPGYL AITKKVAVPY SPAAGVDFEL ESFSERKEEE KEELMEWWKM MSETLNF.
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 :
POFUT1 HumanDescription:
Protein O-Fucosyltransferase 1 Human Recombinant
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
Product # :
ENZ-679Price :
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Description
POFUT1 Human Recombinant produced in E. coli is a single polypeptide chain containing 385 amino acids (27-388) and having a molecular mass of 43.7 kDa. POFUT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The POFUT1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDP-fucose protein O-fucosyltransferase 1 (POUFUT1), belongs to the glycosyltransferase O-Fuc family. POUFUT1 encodes a member of the glycosyltransferase O-Fuc family and Expressed mainly in pancreas, kidney, lung, heart, brain, liver, placenta and skeletal muscle.POUFUT1 adds O-fucose through an O-glycosidic linkage to Preserve serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and emitted proteins. POUFUT1 is involved in ligand-induced receptor signaling. Alternative splicing of this gene results in 2 transcript variants encoding different isoforms.POFUT1 participates in Notch signaling, as Notch ligands can use as POFUT1 substrates.
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Synonyms
FUT12, O-Fuc-T, O-FucT-1, O-FUT, GDP-fucose protein O-fucosyltransferase 1, Peptide-O-fucosyltraferase 1,KIAA0180.
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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 MGSGSWDPAG YLLYCPCMGR FGNQADHFLG SLAFAKLLNR TLAVPPWIEY QHHKPPFTNL HVSYQKYFKL EPLQAYHRVI SLEDFMEKLA PTHWPPEKRV AYCFEVAAQR SPDKKTCPMK EGNPFGPFWD QFHVSFNKSE LFTGISFSAS YREQWSQRFS PKEHPVLALP GAPAQFPVLE EHRPLQKYMV WSDEMVKTGE AQIHAHLVRP YVGIHLRIGS DWKNACAMLK DGTAGSHFMA SPQCVGYSRS TAAPLTMTMC LPDLKEIQRA VKLWVRSLDA QSVYVATDSE SYVPELQQLF KGKVKVVSLK PEVAQVDLYI LGQADHFIGN CVSSFTAFVK RERDLQGRPS SFFGMDRPPK LRDEF.
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 :
ENO2 Human, HisDescription:
Enolase-2 Human Recombinant, His Tag
Gamma-enolase, EC 4.2.1.11, 2-phospho-D-glycerate hydro-lyase, Neural enolase, Neuron-specific enolase, NSE, Enolase 2, ENO2.
Product # :
ENZ-298Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Neuron Specific Enolase Human Recombinant is expressed in E. coli containing 433 amino acids 2-434 fused to an amino terminal hexahistidine tag.The NSE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Enolase 2 is supplied in 10mM Tris-HCl (pH 8), 250mM NaCl, 0.5mM DTT, 1.5mM Cysteine, and 50% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.More Info
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Introduction
NSE is the ?? isoform of the glycolytic enzyme enolase and is expressed primarily in neurons, in normal and neoplastic neuroendocrine cells. NSE is a highly soluble cytoplasmic protein that is readily secreted into the CSF and serum following tissue damage. NSE shows neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons and binds in a calcium-dependent manner to cultured neocortical neurons promoting cell survival.
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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.
-
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
NPL HumanDescription:
N-acetylneuraminate Pyruvate Lyase Human Recombinant
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
Product # :
ENZ-125Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NPL protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.
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Synonyms
N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.
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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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.
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 :
NIT2 HumanDescription:
Nitrilase Family Member 2 Human Recombinant
Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.
Product # :
ENZ-039Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NIT2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276a.a.) and having a molecular mass of 33kDa.NIT2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NIT2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 0.1M NaCl, and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
NIT2 is a member of the nitrilase superfamily. NIT2 protein has an omega-amidase activity which removes potentially toxic intermediates by converting alpha-ketoglutaramate and alpha-ketosuccinamate to biologically useful alpha-ketoglutarate and oxaloacetate, respectively. In addition, Nit2 is widely distributed in nature and is thought to be a tumor suppressor protein.
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Synonyms
Nitrilase homolog 2, Nitrilase family member 2, omega-amidase NIT2, MGC111199, Nit protein 2, EC 3.5.1.3.
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Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSFRLA LIQLQISSIK SDNVTRACSF IREAATQGAK IVSLPECFNS PYGAKYFPEY AEKIPGESTQ KLSEVAKECS IYLIGGSIPE EDAGKLYNTC AVFGPDGTLL AKYRKIHLFD IDVPGKITFQ ESKTLSPGDS FSTFDTPYCR VGLGICYDMR FAELAQIYAQ RGCQLLVYPG AFNLTTGPAH WELLQRSRAV DNQVYVATAS PARDDKASYV AWGHSTVVNP WGEVLAKAGT EEAIVYSDID LKKLAEIRQQ IPVFRQKRSD LYAVEMKKP
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 :
SRR HumanDescription:
Serine Racemase Human Recombinant
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
Product # :
ENZ-232Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SRR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-340) and having a molecular mass of 39.1kDa.SRR is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SRR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine racemase (SRR) is an enzyme which generates D-serine from L-serine. D-serine functions as a neuronal signaling molecule by activating NMDA receptors in the brain. Mammalian SRR is a pyridoxal 5'-phosphate dependent enzyme which catalyzes both the racemization of L-serine to D-serine and also the elimination of water from L-serine, producing pyruvate and ammonia. The SRR enzyme is physiologically stimulated by divalent cations (e.g., magnesium) and is allosterically activated by the magnesium/ATP complex.
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Synonyms
Serine racemase, D-serine ammonia-lyase, D-serine dehydratase, L-serine ammonia-lyase, L-serine dehydratase, SRR, ILV1, ISO1.
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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 MGSHMCAQYC ISFADVEKAH INIRDSIHLT PVLTSSILNQ LTGRNLFFKC ELFQKTGSFK IRGALNAVRS LVPDALERKP KAVVTHSSGN HGQALTYAAK LEGIPAYIVV PQTAPDCKKL AIQAYGASIV YCEPSDESRE NVAKRVTEET EGIMVHPNQE PAVIAGQGTI ALEVLNQVPL VDALVVPVGG GGMLAGIAIT VKALKPSVKV YAAEPSNADD CYQSKLKGKL MPNLYPPETI ADGVKSSIGL NTWPIIRDLV DDIFTVTEDE IKCATQLVWE RMKLLIEPTA GVGVAAVLSQ HFQTVSPEVK NICIVLSGGN VDLTSSITWV KQAERPASYQ SVSV.
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 :
FUT5 HumanDescription:
Fucosyltransferase 5 Human Recombinant
FUT-5
Product # :
ENZ-1199Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
FUT-5
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized FUT5 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; it does not show any change after two weeks at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.
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 :
NAE1 HumanDescription:
NEDD8 Activating Enzyme E1 Subunit 1 Human Recombinant
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
Product # :
ENZ-227Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAE1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 557 amino acids (1-534) and having a molecular mass of 62.7kDa.NAE1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NAE1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NEDD8-activating enzyme E1 regulatory subunit (NAE1) is a member of the ubiquitin-activating E1 family. NAE1 binds to the beta-amyloid precursor protein. Beta-amyloid precursor protein is a cell surface protein with signal-transducing properties, and it is believed to have a role in the pathogenesis of Alzheimer's disease. NAE1 participates in a unique ubiquitinylation-related pathway involving the ubiquitin-like molecule NEDD8. Furthermore, the NAE1 protein is essential for cell cycle progression through the S/M checkpoint.
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Synonyms
NEDD8-activating enzyme E1 regulatory subunit, Amyloid beta precursor protein-binding protein 1 59 kDa, APP-BP1, Amyloid protein-binding protein 1, Proto-oncogene protein 1, NAE1, APPBP1, HPP1, ula-1, A-116A10.1.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQLGKL LKEQKYDRQL RLWGDHGQEA LESAHVCLIN ATATGTEILK NLVLPGIGSF TIIDGNQVSG EDAGNNFFLQ RSSIGKNRAE AAMEFLQELN SDVSGSFVEE SPENLLDNDP SFFCRFTVVV ATQLPESTSL RLADVLWNSQ IPLLICRTYG LVGYMRIIIK EHPVIESHPD NALEDLRLDK PFPELREHFQ SYDLDHMEKK DHSHTPWIVI IAKYLAQWYS ETNGRIPKTY KEKEDFRDLI RQGILKNENG APEDEENFEE AIKNVNTALN TTQIPSSIED IFNDDRCINI TKQTPSFWIL ARALKEFVAK EGQGNLPVRG TIPDMIADSG KYIKLQNVYR EKAKKDAAAV GNHVAKLLQS IGQAPESISE KELKLLCSNS AFLRVVRCRS LAEEYGLDTI NKDEIISSMD NPDNEIVLYL MLRAVDRFHK QQGRYPGVSN YQVEEDIGKL KSCLTGFLQE YGLSVMVKDD YVHEFCRYGA AEPHTIAAFL GGAAAQEVIK IITKQFVIFN NTYIYSGMSQ TSATFQL.
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 :
ACAT2 HumanDescription:
Acetyl-Coenzyme A acetyltransferase 2 Human Recombinant
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
Product # :
ENZ-295Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACAT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kDa. The ACAT2 is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACAT2 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus.
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Synonyms
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNAG SDPVVIVSAA RTIIGSFNGA LAAVPVQDLG STVIKEVLKR ATVAPEDVSE
VIFGHVLAAG CGQNPVRQAS VGAGIPYSVP AWSCQMICGS GLKAVCLAVQ SIGIGDSSIV VAGGMENMSK APHLAYLRTG VKIGEMPLTD SILCDGLTDA FHNCHMGITA ENVAKKWQVS REDQDKVAVL SQNRTENAQK AGHFDKEIVP VLVSTRKGLI EVKTDEFPRH GSNIEAMSKL KPYFLTDGTG TVTPANASGI NDGAAAVVLM KKSEADKRGL TPLARIVSWS QVGVEPSIMG IGPIPAIKQA VTKAGWSLED VDIFEINEAF AAVSAAIVKE LGLNPEKVNI EGGAIALGHP LGASGCRILV TLLHTLERMG RSRGVAALCI GGGMGIAMCV QR.
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 :
GLO1 HumanDescription:
Glyoxalase-I Human Recombinant
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
Product # :
ENZ-398Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
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Synonyms
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
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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
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.
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 :
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- biological activity
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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.
-
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.
- View Data Sheet
Name :
LCAT HumanDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-380Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LCAT Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 441 amino acids (25-440) which includes a 25 amino acid His Tag fused at N-terminus and having a total molecular mass of 49.8 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LCAT protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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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 MGSHMFWLLN VLFPPHTTPK AELSNHTRPV ILVPGCLGNQ LEAKLDKPDV VNWMCYRKTE DFFTIWLDLN MFLPLGVDCW IDNTRVVYNR SSGLVSNAPG VQIRVPGFGK TYSVEYLDSS KLAGYLHTLV QNLVNNGYVR DETVRAAPYD WRLEPGQQEE YYRKLAGLVE EMHAAYGKPV FLIGHSLGCL HLLYFLLRQP QAWKDRFIDG FISLGAPWGG SIKPMLVLAS GDNQGIPIMS SIKLKEEQRI TTTSPWMFPS RMAWPEDHVF ISTPSFNYTG RDFQRFFADL HFEEGWYMWL QSRDLLAGLP APGVEVYCLY GVGLPTPRTY IYDHGFPYTD PVGVLYEDGD DTVATRSTEL CGLWQGRQPQ PVHLLPLHGI QHLNMVFSNL TLEHINAILL GAYRQGPPAS PTASPEPPPP 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.
- View Data Sheet
Name :
phrB E.ColiDescription:
Deoxyribodipyrimidine photo-lyase E.Coli Recombinant
800x600 ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708. Normal 0 false false false EN-US X-NONE HE MicrosoftInternetExplorer4 /* Style Definitions */ table.MsoNormalTable {mso-style-name:"Table Normal"; mso-tstyle-rowband-size:0; mso-tstyle-colband-size:0; mso-style-noshow:yes; mso-style-priority:99; mso-style-parent:""; mso-padding-alt:0cm 5.4pt 0cm 5.4pt; mso-para-margin:0cm; mso-para-margin-bottom:.0001pt; mso-pagination:widow-orphan; font-size:10.0pt; font-family:"Calibri","sans-serif";}
Product # :
ENZ-362Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
800x600 800x600 phrB E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 495 amino acids (1-472) and having a molecular mass of 56.1kDa.phrB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The phrB solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Deoxyribodipyrimidine photo-lyase (phrB) is a member of the DNA photolyase class-1 family. phrB takes part in repair of UV radiation-inducedDNA damage. phrB catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidinedimers (in cis-syn configuration), which are formed between closest bases on the same DNA strand uponexposure to ultraviolet radiation.
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Synonyms
ECK0697, JW0698, phrB, phr, Deoxyribodipyrimidine photo-lyase, DNA photolyase, Photoreactivating enzyme, EC=4.1.99.3, b0708.
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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).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTTHLVW FRQDLRLHDN LALAAACRNS SARVLALYIA TPRQWATHNM SPRQAELINA QLNGLQIALA EKGIPLLFRE VDDFVASVEI VKQVCAENSV THLFYNYQYE VNERARDVEV ERALRNVVCE GFDDSVILPP GAVMTGNHEM YKVFTPFKNA WLKRLREGMP ECVAAPKVRS SGSIEPSPSI TLNYPRQSFD TAHFPVEEKA AIAQLRQFCQ NGAGEYEQQR DFPAVEGTSR LSASLATGGL SPRQCLHRLL AEQPQALDGG AGSVWLNELI WREFYRHLIT YHPSLCKHRP FIAWTDRVQW QSNPAHLQAW QEGKTGYPIV DAAMRQLNST GWMHNRLRMI TASFLVKDLL IDWREGERYF MSQLIDGDLA ANNGGWQWAA STGTDAAPYF RIFNPTTQGE KFDHEGEFIR QWLPELRDVP GKVVHEPWKW AQKAGVTLDY PQPIVEHKEA RVQTLAAYEA ARKGK.
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 :
Ecotin E.ColiDescription:
Ecotin E.Coli Recombinant
E. coli serine protease inhibitor.
Product # :
ENZ-058Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- formulation
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Description
Ecotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids (21-162a.a.) and having a molecular mass of 18.3kDa.Ecotin is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ecotin protein solution (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Ecotin inhibits pancreatic serine proteases. Ecotin protein inhibits chymotrypsin, trypsin, elastases, factor X, kallikrein as well as a variety of other proteases. The power of inhibition is not linked to a specific protease specificity.
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Synonyms
E. coli serine protease inhibitor.
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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 MAESVQPLEK IAPYPQAEKG MKRQVIQLTP QEDESTLKVE LLIGQTLEVD CNLHRLGGKL ENKTLEGWGY DYYVFDKVSS PVSTMMACPD GKKEKKFVTA YLGDAGMLRY NSKLPIVVYT PDNVDVKYRV WKAEEKIDNA VVR
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 :
FUT3 HumanDescription:
Fucosyltransferase 3 Human Recombinant
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
Product # :
ENZ-745Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.
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Synonyms
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
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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
MGSSHHHHHH SSGLVPRGSH MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.
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.