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1000 results found for “Phosphorylase”
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Name :
GH ChickenDescription:
GH Chicken Recombinant
GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1,
Product # :
CYT-430Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
GH Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 191 amino acids with an additional Ala at its N-terminus and having a molecular mass of 22255 Dalton. GH Chicken recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.3% NaHCO3 adjusted to pH 8.
Purity
Greater than 99.0% as determined by:
(a) Analysis by SDS-PAGE gel.
(b) Analysis by SEC-HPLC.Biological Activity
GH Chicken Recombinantis fully biologically active in homologous assays and in PDF-P1 3B9 cells stably transfected with rabbit GH receptors.More Info
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Introduction
GH is a member of the prolactin family of hormones which play an important role in growth control. The gene, along with four other related genes, is located at the GH locus on chromosome 17 where they are interspersed in the same transcriptional orientation; an arrangement which is thought to have evolved by a series of gene duplications. The five genes share a remarkably high degree of sequence identity. Alternative splicing generates additional isoforms of each of the five GHs, leading to further diversity and potential for specialization. This particular family member is expressed in the pituitary but not in placental tissue as is the case for the other four genes in the GH locus. Mutations in or deletions of the gene lead to GH deficiency and short stature.
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Synonyms
GH1, GH, GHN, GH-N, hGH-N,Pituitary GH, GH 1,
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized GH Chicken although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and filter sterilization GH can be stored at 4°C for several weeks. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is recommended.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized GH Chicken Recombinant in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml and not more than 3 mg/ml, which can then be further diluted to other aqueous solutions, preferably in presence of carrier protein.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Thr-Phe-Pro-Ala.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.75 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0 This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GH as a Reference Standard.
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 :
LGMN MouseDescription:
Legumain Mouse Recombinant
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
Product # :
ENZ-933Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
LGMN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 426 amino acids (18-435a.a.) and having a molecular mass of 48.6kDa. LGMN is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LGMN protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Legumain, also known as LGMN is a lysosomal cysteine protease which is found in all mouse tissues, however it was mainly abundant in the kidney as well as placenta. LGMN plays an essential role in the endosomal/lysosomal degradation system as the Legumain deficiency causes the accumulation of pro cathepsins B, H & L, another group of lysosomal cysteine proteases. Furthermore, over expression of LGMN in tumors is important for invasion/metastasis.
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Synonyms
Legumain, Asparaginyl endopeptidase, Protease, cysteine 1.
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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
VPVGVDDPED GGKHWVVIVA GSNGWYNYRH QADACHAYQI IHRNGIPDEQ IIVMMYDDIA NSEENPTPGV VINRPNGTDV YKGVLKDYTG EDVTPENFLA VLRGDAEAVK GKGSGKVLKS GPRDHVFIYF TDHGATGILV FPNDDLHVKD LNKTIRYMYE HKMYQKMVFY IEACESGSMM NHLPDDINVY ATTAANPKES SYACYYDEER GTYLGDWYSV NWMEDSDVED LTKETLHKQY HLVKSHTNTS HVMQYGNKSI STMKVMQFQG MKHRASSPIS LPPVTHLDLT PSPDVPLTIL KRKLLRTNDV KESQNLIGQI QQFLDARHVI EKSVHKIVSL LAGFGETAER HLSERTMLTA HDCYQEAVTH FRTHCFNWHS VTYEHALRYL YVLANLCEAP YPIDRIEMAM DKVCLSHYLE 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 :
EPHX1 Human, Sf9Description:
Epoxide Hydrolase 1 Microsomal Human Recombinant, sf9
Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase, EC 3.3.2.9, HYL1
Product # :
ENZ-1076Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EPHX1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 442 amino acids (21-455 a.a.) and having a molecular mass of 51.5kDaEPHX1 is expressed with an 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
EPHX1 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) 50% glycerol,1mM DTT and 0.1M NaCl.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Epoxide Hydrolase 1 Microsomal (EPHX1) is a vital biotransformation enzyme which transfers epoxides from the degradation of aromatic compounds to trans-dihydrodiols that can be conjugated and excreted from the body. Epoxide hydrolase plays a role in both activation and detoxification of epoxides. Mutations in EPHX1 trigger preeclampsia, epoxide hydrolase deficiency or increased epoxide hydrolase activity.
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Synonyms
Epoxide hydrolase 1, Epoxide hydratase, Microsomal epoxide hydrolase, Meh, EPHX1, EPHX, EPOX, Epoxide Hydrolase 1 Microsomal, Microsomal Epoxide Hydrolase,
EC 3.3.2.9, HYL1 -
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
MRDKEETLPL EDGWWGPGTR SAAREDDSIR PFKVETSDEE IHDLHQRIDK FRFTPPLEDS CFHYGFNSNY LKKVISYWRN EFDWKKQVEI LNRYPHFKTK IEGLDIHFIH VKPPQLPAGH TPKPLLMVHG WPGSFYEFYK IIPLLTDPKN HGLSDEHVFE VICPSIPGYG FSEASSKKGF NSVATARIFY KLMLRLGFQE FYIQGGDWGS LICTNMAQLV PSHVKGLHLN MALVLSNFST LTLLLGQRFG RFLGLTERDV ELLYPVKEKV FYSLMRESGY MHIQCTKPDT VGSALNDSPV GLAAYILEKF STWTNTEFRY LEDGGLERKF SLDDLLTNVM LYWTTGTIIS SQRFYKENLG QGWMTQKHER MKVYVPTGFS AFPFELLHTP EKWVRFKYPK LISYSYMVRG GHFAAFEEPE LLAQDIRKFL SVLERQHHHH HH.
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
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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 :
MAP2K6 Human, sf9Description:
Mitogen-Activated Protein Kinase Kinase 6 Human Recombinant, sf9
Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.
Product # :
PKA-079Price :
Quantity :
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Shipped with Ice Packs
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Description
MAP2K6 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 340 amino acids (1-334 a.a.) and having a molecular mass of 38.3kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).MAP2K6 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MAP2K6 protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Mitogen-Activated Protein Kinase 6 (MAP2K6) is a part of the dual specificity protein kinase family. MAP2K6 phosphorylates and activates p38 MAP kinase in response to inflammatory cytokines or environmental stress. MAP2K6 is a vital component of the MAP kinase signal transduction pathway. MAP2K6 takes part in various cellular processes such as stress induced cell cycle arrest and apoptosis.
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Synonyms
Angiopoietin-1 receptor, Endothelial tyrosine kinase, HYK, STK1, Tunica interna endothelial cell kinase, Tyrosine kinase with Ig and EGF homology domains-2, Tyrosine-protein kinase receptor TEK, Tyrosine-protein kinase receptor TIE-2, mTIE2, p140 TEK, CD202b.
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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
MSQSKGKKRN PGLKIPKEAF EQPQTSSTPP RDLDSKACIS IGNQNFEVKA DDLEPIMELG RGAYGVVEKM RHVPSGQIMA VKRIRATVNS QEQKRLLMDL DISMRTVDCP FTVTFYGALF REGDVWICME LMDTSLDKFY KQVIDKGQTI PEDILGKIAV SIVKALEHLH SKLSVIHRDV KPSNVLINAL GQVKMCDFGI SGYLVDSVAK TIDAGCKPYM APERINPELN QKGYSVKSDI WSLGITMIEL AILRFPYDSW GTPFQQLKQV VEEPSPQLPA DKFSAEFVDF TSQCLKKNSK ERPTYPELMQ HPFFTLHESK GTDVASFVKL ILGDHHHHHH.
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 :
DECR1 HumanDescription:
2,4-Dienoyl CoA Reductase 1 Human Recombinant
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
Product # :
ENZ-102Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DECR1 Human Recombinant fused to 21 amino acid His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 322 amino acids (35-335 a.a.) and having a molecular mass of 34.4kDa. The DECR1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DECR1 solution contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
DECR1 is a mitochondrial protein which exists as a homotetramer and is a member of a family of short-chain dehydrogenases/reductases. DECR1 acts as an auxiliary enzyme of beta-oxidation andt partakes in the metabolism of unsaturated fatty enoyl-CoA esters. in particular, DECR1 uses NADP+ to catalyze the reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA that can subsequently be used as an intermediate in the Krebs cycle. Furthermore, DECR1 is believed to work as a tumor suppressor, possibly downregulating the expression of Neu and slowing the rate of tumorigenesis.
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Synonyms
2,4-dienoyl-CoA reductase, mitochondrial, 2,4-dienoyl-CoA reductase [NADPH], 4-enoyl-CoA reductase [NADPH], DECR1, DECR, NADPH, SDR18C1.
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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 MNTEALQSKF FSPLQKAMLP PNSFQGKVAF ITGGGTGLGK GMTTLLSSLG AQCVIASRKM DVLKATAEQI SSQTGNKVHA IQCDVRDPDM VQNTVSELIK VAGHPNIVIN NAAGNFISPT ERLSPNAWKT ITDIVLNGTA FVTLEIGKQL IKAQKGAAFL SITTIYAETG SGFVVPSASA KAGVEAMSKS LAAEWGKYGM RFNVIQPGPI KTKGAFSRLD PTGTFEKEMI GRIPCGRLGT VEELANLAAF LCSDYASWIN GAVIKFDGGE EVLISGEFND LRKVTKEQWD TIEELIRKTK GS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NAGA HumanDescription:
N-Acetylgalactosaminidase Alpha Human Recombinant
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
Product # :
ENZ-963Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NAGA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 400 amino acids (18-411) and having a molecular mass of 45.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).NAGA is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
NAGA protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
N-Acetylgalactosaminidase Alpha (NAGA) is a lysosomal exoglycosidase which removes terminal alpha-N-acetylgalactosamine residues from glycopeptides and glycolipids. NAGA is necessary for the breakdown of glycolipids.
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Synonyms
Alpha-N-acetylgalactosaminidase, N-Acetylgalactosaminidase Alpha, NAGA, Alpha-galactosidase B, NAGA, D22S674, GALB.
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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
LDNGLLQTPP MGWLAWERFR CNINCDEDPK NCISEQLFME MADRMAQDGW RDMGYTYLNI DDCWIGGRDA SGRLMPDPKR FPHGIPFLAD YVHSLGLKLG IYADMGNFTC MGYPGTTLDK VVQDAQTFAE WKVDMLKLDG CFSTPEERAQ GYPKMAAALN ATGRPIAFSC SWPAYEGGLP PRVNYSLLAD ICNLWRNYDD IQDSWWSVLS ILNWFVEHQD ILQPVAGPGH WNDPDMLLIG NFGLSLEQSR AQMALWTVLA APLLMSTDLR TISAQNMDIL QNPLMIKINQ DPLGIQGRRI HKEKSLIEVY MRPLSNKASA LVFFSCRTDM PYRYHSSLGQ LNFTGSVIYE AQDVYSGDII SGLRDETNFT VIINPSGVVM WYLYPIKNLE MSQQHHHHHH.
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 :
HADH HumanDescription:
Hydroxyacyl-Coenzyme A Dehydrogenase Human Recombinant
EC 1.1.1.35, HAD, HADH1, HHF4, MSCHAD, SCHAD, Hydroxyacyl-coenzyme A dehydrogenase, HCDH, Short-chain 3-hydroxyacyl-CoA dehydrogenase, Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase, HADH, HADHSC, MGC8392.
Product # :
ENZ-499Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HADH Human Recombinant fused to a 21 amino acids His Tag at N-terminal produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (13-314 a.a.) and having a molecular mass of 35.1 kDa. The HADH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HADH solution contains 20mM Tris-HCl pH-8, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
HADH is part of the 3-hydroxyacyl-CoA dehydrogenase enzyme family. HADH is involved in mitochondrial matrix to catalyze the oxidation of straight-chain 3-hydroxyacyl-CoAs as part of the beta-oxidation pathway. HADH enzymatic activity is at its peak with medium-chain-length fatty acids. Mutations in HADH cause familial hyperinsulinemic hypoglycemia. HADH participates in fatty acid oxidation, where some enzymes work in a step-wise fashion to break metabolize fats and convert them to energy.
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Synonyms
EC 1.1.1.35, HAD, HADH1, HHF4, MSCHAD, SCHAD, Hydroxyacyl-coenzyme A dehydrogenase, HCDH, Short-chain 3-hydroxyacyl-CoA dehydrogenase, Medium and short-chain L-3-hydroxyacyl-coenzyme A dehydrogenase, HADH, HADHSC, MGC8392.
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Physical Appearance
Sterile Filtered clear 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 MSSSSTASAS AKKIIVKHVT VIGGGLMGAG IAQVAAATGH TVVLVDQTED ILAKSKKGIE ESLRKVAKKK FAENPKAGDE FVEKTLSTIA TSTDAASVVH STDLVVEAIV ENLKVKNELF KRLDKFAAEH TIFASNTSSL QITSIANATT RQDRFAGLHF FNPVPVMKLV EVIKTPMTSQ KTFESLVDFS KALGKHPVSC KDTPGFIVNR LLVPYLMEAI RLYERGDASK EDIDTAMKLG AGYPMGPFEL LDYVGLDTTK FIVDGWHEMD AENPLHQPSP SLNKLVAENK FGKKTGEGFY KYK.
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 :
OAS1 HumanDescription:
2’-5’ Oligoadenylate Synthetase 1 Human Recombinant
2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.
Product # :
ENZ-445Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OAS1 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 384 amino acids (1-364 a.a.) and having a molecular mass of 43.9kDa.The OAS1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The OAS1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
OAS1 enzyme is a member of the 2’,5’-oligoadenylate synthetase family. OAS1 is induced by interferons and uses adenosine triphosphate in 2’-specific nucleotidyl transfer reactions to synthesize 2’,5’-oligoadenylates(2-5As). These molecules in turn activate latent RNase L resulting in viral RNA degradation and the inhibition of viral replication.
OAS1 may have a role in mediating resistance to virus infection, control of cell growth, differentiation, and apoptosis. OAS1 binds double-stranded RNA and polymerizes ATP into PPP (A2'P5'A)N oligomers, which activate the latent RNase L that, once activated, cleaves single-stranded RNAs.
OAS1 gene mutations are been linked to host susceptibility to viral infection.
OSA1 gene polymorphisms are linked to the outcome of hepatitis C virus infection. Furthermore, OAS1 gene polymorphisms are linked to the susceptibility to severe acute respiratory syndrome. -
Synonyms
2'-5'-oligoadenylate synthetase 1, (2-5')oligo(A) synthetase 1, 2-5A synthetase 1, p46/p42 OAS, E18/E16, OAS1, OIAS, IFI-4, OIASI.
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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 MMDLRNTPAK SLDKFIEDYL LPDTCFRMQI NHAIDIICGF LKERCFRGSS YPVCVSKVVK GGSSGKGTTL RGRSDADLVV FLSPLTTFQD QLNRRGEFIQ EIRRQLEACQ RERAFSVKFE VQAPRWGNPR ALSFVLSSLQ LGEGVEFDVL PAFDALGQLT GSYKPNPQIY VKLIEECTDL QKEGEFSTCF TELQRDFLKQ RPTKLKSLIR LVKHWYQNCK KKLGKLPPQY ALELLTVYAW ERGSMKTHFN TAQGFRTVLE LVINYQQLCI YWTKYYDFKN PIIEKYLRRQ LTKPRPVILD PADPTGNLGG GDPKGWRQLA QEAEAWLNYP CFKNWDGSPV SSWILLVRPP ASSLPFIPAP LHEA.
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 :
GSTO2 HumanDescription:
Glutathione S-Transferase Omega 2 Human Recombinant
Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.
Product # :
ENZ-605Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GSTO2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 266 amino acids (1-243) and having a molecular mass of 30.6kDa.GSTO2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTO2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 40% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Glutathione S-transferase omega 2 (GSTO2) is a member of the GST superfamily. GSTO2 is involved in catalyzing the reaction of glutathione with a broad range of organic compounds to form thioethers, a process which is vital for the metabolism and detoxification of a variety of xenobiotics and carcinogens. GSTO2 displays glutathione-dependent thiol transferase activity. GSTO2 has a high dehydroascorbate reductase activity and may be a factor in the recycling of ascorbic acid. GSTO2 also participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA). GSTO2 is expressed in an array of tissues, including the liver, kidney, skeletal muscle and prostate, while the strongest expression is seen in the testis.
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Synonyms
Glutathione S-transferase omega-2, GSTO-2, Glutathione S-transferase omega 2-2, GSTO 2-2, Glutathione-dependent dehydroascorbate reductase, Monomethylarsonic acid reductase, MMA(V) reductase, GSTO2, bA127L20.1.
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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 MGSMSGDATR TLGKGSQPPG PVPEGLIRIY SMRFCPYSHR TRLVLKAKDI RHEVVNINLR NKPEWYYTKH PFGHIPVLET SQCQLIYESV IACEYLDDAY PGRKLFPYDP YERARQKMLL ELFCKVPHLT KECLVALRCG RECTNLKAAL RQEFSNLEEI
LEYQNTTFFG GTCISMIDYL LWPWFERLDV YGILDCVSHT PALRLWISAM KWDPTVCALL MDKSIFQGFL NLYFQNNPNA FDFGLC.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NQO1 Human, ActiveDescription:
NAD(P)H Dehydrogenase Quinone 1, Active 1 Human Recombinant
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
Product # :
ENZ-1107Price :
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Description
NQO1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 294 amino acids ( 1-274aa ) and having a molecular mass of 33.0 kDa. NQO1 is fused to a 20 amino acid His tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NQO1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 pmol/min/ug. One unit will convert 1 pmoles resazurin to resorufin per minute at pH 7.5 at 25°C.
More Info
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Introduction
NQO1 belongs to the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. NQO1 acts as an imperative part of cellular antioxidant defense by detoxifying quinines therefore preventing the formation of reactive oxygen species. It seems that NQO1 serves as a quinone reductase relating to conjugation reactions of hydroquinons involved in detoxification pathways in addition to biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. Altered NQO1 expression is seen in many tumors and also linked to Alzheimer’s disease. NQO1 gene mutations are linked to tardive dyskinesia which is an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer.
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Synonyms
NAD(P)H dehydrogenase (quinone) 1, Quinone reductase 1, QR1, NAD(P)H:quinone oxidoreductase 1, DT-diaphorase, DTD, Azoreductase, Phylloquinone reductase, Menadione reductase, NQO1, DIA4, NMOR1, DHQU, NMORI.
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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 MVGRRALIVL AHSERTSFNY AMKEAAAAAL KKKGWEVVES
DLYAMNFNPI ISRKDITGKL KDPANFQYPA ESVLAYKEGH LSPDIVAEQK KLEAADLVIF
QFPLQWFGVP AILKGWFERV FIGEFAYTYA AMYDKGPFRS KKAVLSITTG GSGSMYSLQG
IHGDMNVILW PIQSGILHFC GFQVLEPQLT YSIGHTPADA RIQILEGWKK RLENIWDETP
LYFAPSSLFD LNFQAGFLMK KEVQDEEKNK KFGLSVGHHL GKSIPTDNQI KARK
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 :
T5 ExonucleaseDescription:
T5 Exonuclease Recombinant
T5 Exonuclease
Product # :
ENZ-1184Price :
Quantity :
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Description
T5 Exonuclease T5 phage D15 gene Recombinant produced in E.Coli is a single, non-glycosylated polypeptide. T5 Exonuclease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
10U/ul, 50mM Tris-HCl (25℃, pH 7.5), 100mM NaCl, 0.1mM EDTA, 1mM DTT, 0.1% Triton X-100 and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
T5 Exonuclease is an important enzyme that belongs to the family of exonucleases and plays a vital role in DNA metabolism and genetic engineering. This research paper aims to provide an overview of T5 Exonuclease, including its structure, function, and diverse applications in molecular biology.
T5 Exonuclease is derived from the bacteriophage T5, and it possesses a remarkable ability to selectively degrade single-stranded DNA in a 5' to 3' direction. It is a highly processive enzyme, meaning it can cleave multiple nucleotides consecutively without dissociating from the DNA substrate. The enzyme exhibits high specificity for single-stranded DNA, making it a valuable tool for various molecular biology applications.
The primary function of T5 Exonuclease is to remove nucleotides from the 5' ends of single-stranded DNA molecules. By digesting DNA in a processive manner, T5 Exonuclease is involved in DNA repair mechanisms, such as the removal of damaged or mismatched nucleotides. It is also widely utilized in molecular cloning techniques to generate DNA fragments with precise ends for subsequent DNA ligation reactions.
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Synonyms
T5 Exonuclease
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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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Applications
Gibson Assembly
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Background
The structural features of T5 Exonuclease play a crucial role in its enzymatic activity. The enzyme consists of distinct functional domains, including an N-terminal domain responsible for DNA binding and a C-terminal domain containing the exonuclease active site. Understanding the three-dimensional structure of T5 Exonuclease provides insights into its catalytic mechanism and substrate specificity.
The versatility of T5 Exonuclease extends beyond DNA repair and cloning applications. It has been employed in various molecular biology techniques, such as site-directed mutagenesis, DNA sequencing, and preparation of DNA templates for in vitro transcription. Additionally, T5 Exonuclease has found utility in research areas like next-generation sequencing library preparation, restriction fragment length polymorphism (RFLP) analysis, and gene expression studies.
In recent years, the use of T5 Exonuclease in genome editing technologies, such as CRISPR-Cas9, has gained attention. T5 Exonuclease can be employed to remove unwanted DNA sequences or overhangs, enabling precise and efficient genome editing. This application highlights the significance of T5 Exonuclease in advancing genetic engineering and synthetic biology research.
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Unit Definition
1 unit of T5 Exonuclease is defined as the amount of enzyme required to cause the change of 0.00032 A260nm/min at 37° C in 1xReaction Buffer: 20mM Tris-acetate (pH 7.9 @ 25°C), 50mM Potassium Acetate, 10mM Magnesium Acetate and 1mM DTT.
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 :
LDHA, E.Coli ActiveDescription:
Lactate Dehydrogenase A, BioActive E.Coli Recombinant
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
Product # :
ENZ-1144Price :
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Description
LDHA E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 39.1 kDa.LDHA E.Coli is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LDHA E.Coli protein (1mg/ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), containing 100mM NaCland 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 200unit/mg. 1 unit converts 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5 at 37˚C
More Info
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Introduction
D-lactate dehydrogenase or ldhA is an enzyme, part of the D-lactate dehydrogenase protein family. IDHA is a cytochrome that enhances the catalyzation of D-lactate dehydrogenase ldhA reaction. This enzyme has 2 substrates ((D) -lactate & ferricytochrome c), thus, it has 2 end products (pyruvate & ferrocytochrome c).
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Synonyms
LDH-A, GSD11, LDH1, LDHM, PIG19, EC 1.1.1.27, lactate dehydrogenase M, LDH-M, LDH-1, L-lactate dehydrogenase A chain, LDH muscle subunit, Renal carcinoma antigen NY-REN-59, Cell proliferation-inducing gene 19 protein, LDHA.
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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 MGSHMKLAVY STKQYDKKYL QQVNESFGFE LEFFDFLLTE KTAKTANGCE AVCIFVNDDG SRPVLEELKK HGVKYIALRC AGFNNVDLDA AKELGLKVVR VPAYDPEAVA EHAIGMMMTL NRRIHRAYQR TRDANFSLEG LTGFTMYGKT AGVIGTGKIG VAMLRILKGF GMRLLAFDPY PSAAALELGV EYVDLPTLFS ESDVISLHCP LTPENYHLLN EAAFEQMKNG VMIVNTSRGA LIDSQAAIEA LKNQKIGSLG MDVYENERDL FFEDKSNDVI QDDVFRRLSA CHNVLFTGHQ AFLTAEALTS ISQTTLQNLS NLEKGETCPN ELV
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 :
LAP3 HumanDescription:
Leucine Aminopeptidase 3 Human Recombinant
Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.
Product # :
ENZ-889Price :
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Description
LAP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 539 amino acids (1-519 a.a) and having a molecular mass of 58.3kDa. LAP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LAP3 protein solution (0.5mg/ml) containing 20mM Tris-HCl(pH8.5), 50% glycerol, 5mM DTT and 1mM EDTA.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Leucine Aminopeptidase 3 also known as LAP3 is a member of the peptidase M17 family. LAP3 is implicated in the processing as well as regular turnover of intracellular proteins. LAP3 catalyzes the removal of unsubstituted N-terminal amino acids from different peptides. LAP3 is responsible of releasing an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but could be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are as well readily hydrolyzed; however rates on arylamides are exceedingly low.
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Synonyms
Leucine Aminopeptidase 3, Peptidase S, PEPS, Proline Aminopeptidase, Leucyl Aminopeptidase, Prolyl Aminopeptidase, EC 3.4.11.1, LAP-3, LAPEP, Epididymis Secretory Protein Li 106, Cytosol Aminopeptidase, EC 3.4.11.5, HEL-S-106, EC 3.4.11, LAP, Cytosol aminopeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Proline aminopeptidase, Prolyl aminopeptidase.
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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 MFLLPLPAAG RVVVRRLAVR RFGSRSLSTA DMTKGLVLGI YSKEKEDDVP QFTSAGENFD KLLAGKLRET LNISGPPLKA GKTRTFYGLH QDFPSVVLVG LGKKAAGIDE QENWHEGKEN IRAAVAAGCR QIQDLELSSV EVDPCGDAQA AAEGAVLGLY EYDDLKQKKK MAVSAKLYGS GDQEAWQKGV LFASGQNLAR QLMETPANEM TPTRFAEIIE KNLKSASSKT EVHIRPKSWI EEQAMGSFLS VAKGSDEPPV FLEIHYKGSP NANEPPLVFV GKGITFDSGG ISIKASANMD LMRADMGGAA TICSAIVSAA KLNLPINIIG LAPLCENMPS GKANKPGDVV RAKNGKTIQV DNTDAEGRLI LADALCYAHT FNPKVILNAA TLTGAMDVAL GSGATGVFTN SSWLWNKLFE ASIETGDRVW RMPLFEHYTR QVVDCQLADV NNIGKYRSAG ACTAAAFLKE FVTHPKWAHL DIAGVMTNKD EVPYLRKGMT GRPTRTLIEF LLRFSQDNA.
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 :
UBE2J2 HumanDescription:
Ubiquitin-Conjugating Enzyme E2, J2 Human Recombinant
Ubiquitin-conjugating enzyme E2 J2, ubiquitin-conjugating enzyme E2 J2 (UBC6 homolog east), Non-canonical ubiquitin-conjugating enzyme 2, ubiquitin conjugating enzyme 6, PRO2121, yeast UBC6 homolog, Ubc6p, NCUBE-2, EC 6.3.2.19.
Product # :
ENZ-626Price :
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Description
UBE2J2 Human Recombinant produced in E. coli is a single polypeptide chain containing 250 amino acids (1-226) and having a molecular mass of 28.0 kDa.UBE2J2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The UBE2J2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Ubiquitin-conjugating enzyme E2 J2 (UBE2J2) is a member of the ubiquitin-conjugating enzyme family. UBE2J2 catalyzes the covalent attachment of ubiquitin to other proteins. UBE2J2 is located in the membrane of the endoplasmic reticulum. UBE2J2 participates in the selective degradation of misfolded membrane proteins from the endoplasmic reticulum (ERAD).
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Synonyms
Ubiquitin-conjugating enzyme E2 J2, ubiquitin-conjugating enzyme E2 J2 (UBC6 homolog east), Non-canonical ubiquitin-conjugating enzyme 2, ubiquitin conjugating enzyme 6, PRO2121, yeast UBC6 homolog, Ubc6p, NCUBE-2, EC 6.3.2.19.
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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 MGSHMSSTSS KRAPTTATQR LKQDYLRIKK DPVPYICAEP LPSNILEWHY VVRGPEMTPY EGGYYHGKLI FPREFPFKPP SIYMITPNGR FKCNTRLCLS ITDFHPDTWN PAWSVSTILT GLLSFMVEKG PTLGSIETSD FTKRQLAVQS LAFNLKDKVF CELFPEVVEE IKQKQKAQDE LSSRPQTLPL PDVVPDGETH LVQNGIQLLN GHAPGAVPNL AGLQQANRHH
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 :
FGF 2 Human, sf9Description:
Fibroblast Growth Factor-Basic Human Recombinant, Sf9
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
Product # :
CYT-365Price :
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Description
Fibroblast Growth Factor-2 Human Recombinant (FGF-2) produced in Sf9 insect cells is a single, glycosylated, polypeptide chain containing 155 amino acids and having a molecular mass of 17353 Dalton.The FGF-basic is purified by proprietary chromatographic techniques.
Source
Baculovirus.
Formulation
The sterile protein solution (0.5mg/ml) contains 20mM Tris pH=7.9, 100mM KCl, 1mM DTT and 20% glycerol.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.More Info
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Introduction
Basic fibroblast growth factor is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. This protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, thus is thought to be involved in organogenesis. Three alternatively spliced variants encoding different isoforms have been described. The heparin-binding growth factors are angiogenic agents in vivo and are potent mitogens for a variety of cell types in vitro. There are differences in the tissue distribution and concentration of these 2 growth factors.
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Synonyms
Prostatropin, HBGH-2, HBGF-2, FGF-2, FGF-b.
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Physical Appearance
Sterile Filtered liquid formulation.
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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
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ala-Gly-Ser-Ile.
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Background
What is the molecular weight/Mw of FGF 2 Protein?
FGF 2 Protein has a total Mw of 17.3kDa.
What is the source or expression system of FGF 2 Protein?
Baculovirus.
What is the Purity of FGF 2 Protein?
FGF 2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF 2 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2MU/mg.
What is the amino acid sequence of FGF 2 Protein?
FGF 2 Protein is composed from155 amino acids.
What applications can FGF 2 Protein be used in?
FGF 2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF 2 Protein?
The endotoxin level is minimal, FGF 2 Protein was purified using conventional chromatography techniques.
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 :
SAE1/SAE2 HumanDescription:
SAE1/SAE2 Human Recombinant
Product # :
ENZ-1161Price :
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Description
SAE1/SAE2 Human Recombinant produced in SF9 is glycosylated, polypeptide chain containing 2 subunits (SAE1 subunit molecular mass is 41kDa & SAE2 subunit molecular mass is 91kDa). The subunits associate to form a complex. The SAE1/SAE2 is expressed with a -10xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
SAE1/SAE2 is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SAE1 and SAE2 form heterodimers which take part in the posttranslational modification of proteins (sumoylation). This process regulates protein structure as well as intracellular localization of the target. SAE1/SAE2 may indicate on dermatomyositis (DM) as autoantibodies against those 2 proteins have been found in patients.
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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. Avoid multiple freeze-thaw cycles.
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Immunological Functions
1. Binds IgG-type human auto-antibodies.2. Standard ELISA test (checkerboard analysis of positive/negative samples) and immunodot test with positive/negative samples.
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coating concentration
0.3-0.8 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.
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Applications
Western blot with anti SAE1/SAE2 autoantibody positive sample & Polyclonal anti-SAE1 and anti-SAE2 antibodies.
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 :
CYP2E1 HumanDescription:
Cytochrome P450 2E1 Human Recombinant
Cytochrome P450, Family 2, Subfamily E, Polypeptide 1, CYP2E, Cytochrome P450, Subfamily IIE (Ethanol-Inducible), Polypeptide 1, 4-Nitrophenol 2-Hydroxylase, Cytochrome P450-J, P450C2E, CYPIIE1, Flavoprotein-Linked Monooxygenase, Microsomal Monooxygenase, Xenobiotic Monooxygenase, Cytochrome P450 2E1, EC 1.14.13.n7, EC 1.14.14.1, EC 1.14.13.-, P450-J, CPE1, Cytochrome P450 2E1.
Product # :
ENZ-862Price :
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Description
CYP2E1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 488 amino acids (29-493 a.a) and having a molecular mass of 56.2kDa. CYP2E1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CYP2E1 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CYP2E1, also known as Cytochrome P450 2E1 belongs to the cytochrome P450 mixed-function oxidase system which is involved in the metabolism of xenobiotics in the body. While CYP2E1 is implicated in the oxidative metabolism of small range substrates, commonly small polar molecules, there are many significant drug interactions which are mediated by CYP2E1.
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Synonyms
Cytochrome P450, Family 2, Subfamily E, Polypeptide 1, CYP2E, Cytochrome P450, Subfamily IIE (Ethanol-Inducible), Polypeptide 1, 4-Nitrophenol 2-Hydroxylase, Cytochrome P450-J, P450C2E, CYPIIE1, Flavoprotein-Linked Monooxygenase, Microsomal Monooxygenase, Xenobiotic Monooxygenase, Cytochrome P450 2E1, EC 1.14.13.n7, EC 1.14.14.1, EC 1.14.13.-, P450-J, CPE1, Cytochrome P450 2E1.
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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 MGSSWNLPPG PFPLPIIGNL FQLELKNIPK SFTRLAQRFG PVFTLYVGSQ RMVVMHGYKA VKEALLDYKD EFSGRGDLPA FHAHRDRGII FNNGPTWKDI RRFSLTTLRN YGMGKQGNES RIQREAHFLL EALRKTQGQP FDPTFLIGCA PCNVIADILF RKHFDYNDEK FLRLMYLFNE NFHLLSTPWL QLYNNFPSFL HYLPGSHRKV IKNVAEVKEY VSERVKEHHQ SLDPNCPRDL TDCLLVEMEK EKHSAERLYT MDGITVTVAD LFFAGTETTS TTLRYGLLIL MKYPEIEEKL HEEIDRVIGP SRIPAIKDRQ EMPYMDAVVH EIQRFITLVP SNLPHEATRD TIFRGYLIPK GTVVVPTLDS VLYDNQEFPD PEKFKPEHFL NENGKFKYSD YFKPFSTGKR VCAGEGLARM ELFLLLCAIL QHFNLKPLVD PKDIDLSPIH IGFGCIPPRY KLCVIPRS.
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 :
PRSS28 MouseDescription:
Protease Serine 28 Mouse Recombinant
Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.
Product # :
ENZ-987Price :
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Description
PRSS28 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 256 amino acids (27-274a.a.) and having a molecular mass of 28.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PRSS28 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PRSS28 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Serine protease 28, also known as Prss28, is a member of the S1 serine proteinase family with a conserved Histidine-Aspartic Acid-Serine catalytic triad. Prss28 shows mixed substrate specificity which silences signaling through proteinase-activated receptors. Furthermore, Prss28 is involved with embryo hatching and its activity is vital for successful implantation.
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Synonyms
Serine protease 28, Implantation serine proteinase 1, ISP-1, Strypsin, Tryptase-like proteinase.
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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
KPVGIVGGQC TPPGKWPWQV SLRMYSYEVN SWVHICGGSI IHPQWILTAA HCIQSQDADP AVYRVQVGEV YLYKEQELLN ISRIIIHPDY NDVSKRFDLA LMQLTALLVT STNVSPVSLP KDSSTFDSTD QCWLVGWGNL LQRVPLQPPY QLHEVKIPIQ DNKSCKRAYR KKSSDEHKAV AIFDDMLCAG TSGRGPCFGD SGGPLVCWKS NKWIQVGVVS KGIDCSNNLP SIFSRVQSSL AWIHQHIQLE 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.
- View Data Sheet
Name :
NNMT MouseDescription:
Nicotinamide N-Methyltransferase Mouse Recombinant
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
Product # :
ENZ-1037Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
NNMT Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids (1-264a.a) and having a molecular mass of 32.1kDa.NNMT is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NNMT protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
NNMT is part of the family of transferases, especially those transferring one-carbon group methyltransferases. NNMT is mostly expressed in the liver, and a lower expression is seen in the kidney, lung, skeletal muscle, placenta and heart. NNMT catalyzes the N-methylation of nicotinamide and other pyridines to form pyridinium ions. This activity is significant for biotransformation of many drugs and xenobiotic compounds. NNMT is accountable for the enzymatic activity which uses S-adenosyl methionine as the methyl donor. NNMT expression is related with tumor stage and DFS time in hepatocellular carcinoma cases. NNMT is a good candidate as a tumor marker of various kinds of cancers. NNMT serum levels have significance in the premature detection and in the management of patients with colorectal cancer.
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Synonyms
Nicotinamide N-methyltransferase , Nnmt, icotinamide N-methyltransferase isoform1.
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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 MGSHMESGFT SKDTYLSHFN PRDYLEKYYS FGSRHCAENE ILRHLLKNLF KIFCLGAVKG ELLIDIGSGP TIYQLLSACE SFTEIIVSDY TDQNLWELQK WLKKEPGAFD WSPVVTYVCD LEGNRMKGPE KEEKLRRAIK QVLKCDVTQS QPLGGVSLPP ADCLLSTLCL DAACPDLPAY RTALRNLGSL LKPGGFLVMV DALKSSYYMI GEQKFSSLPL GWETVRDAVE EAGYTIEQFE VISQNYSSTT SNNEGLFSLV GRKPGRSE.
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 :
SEPSECS MouseDescription:
Selenocysteinyl-tRNA(Sec) synthase Mouse Recombinant
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
Product # :
ENZ-1081Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SEPSECS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 527 amino acids (1-504 a.a.) and having a molecular mass of 57.7kDa.SEPSECS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SEPSECS protein solution (0.25 mg/ml) is formulated in 20mM Tris-HCl buffer (pH7.5) 1mM DTT, 0.2M NaCl and 50% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPSECS catalyzes the last step of sec synthesis by converting O-phosphoseryl-tRNA(sec) to selenocysteinyl-tRNA(sec) using selenophosphate as the selenium donor. Furthermore, SEPSECS protein is considered a specific marker of autoimmune hepatitis.
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Synonyms
AA986712, D5Ertd135e, SecS, SLA, SLA/LP autoantigen, SLA-p35, Selenocysteinyl-tRNA(Sec) synthase, Selenocysteine synthase, Liver-pancreas antigen, Soluble liver antigen, Sec synthase, UGA suppressor tRNA-associated protein, SepSecS.
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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 MGSMNPESFA AGERRVSPAY VRQGCEARRA HEHLIRLLLE QGKCPEDGWD ESTLELFLHE LAVMDSNNFL GNCGVGEREG RVASALVARR HYRFIHGIGR SGDISAVQPK AAGSSLLNKI TNSLVLNVIK LAGVHSVASC FVVPMATGMS LTLCFLTLRH
KRPKAKYIIW PRIDQKSCFK SMVTAGFEPV VIENVLEGDE LRTDLKAVEA KIQELGPEHI LCLHSTTACF APRVPDRLEE LAVICANYDI PHVVNNAYGL QSSKCMHLIQ QGARVGRIDA FVQSLDKNFM VPVGGAIIAG FNEPFIQDIS KMYPGRASAS PSLDVLITLL SLGCSGYRKL
LKERKEMFVY LSTQLKKLAE AHNERLLQTP HNPISLAMTL KTIDGHHDKA VTQLGSMLFT RQVSGARAVP LGNVQTVSGH TFRGFMSHAD NYPCAYLNAA AAIGMKMQDV DLFIKRLDKC LNIVRKEQTR ASVVSGADRN KAEDADIEEM ALKLDDVLGD VGQGPAL.
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 :
PRDX5 HumanDescription:
Peroxiredoxin-5 Human Recombinant
Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.
Product # :
ENZ-426Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- biological activity
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Description
PRDX5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 162 amino acids (53-214 a.a.) and having a molecular mass of 17 kDa.The PRDX5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRDX5 solution contains 20mM HEPES buffer (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The specific activity was found to be approximately 117-136 pmole/min/µg. The enzymatic activity was confirmed by measuring the remaining peroxide after incubation of PRDX5 and peroxide for 20 min at room temperature. Specific activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.More Info
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Introduction
PRDX5 belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides with reducing equivalents supplied through the thioredoxin system. PRDX5 has an antioxidant protective function in different tissues under normal conditions and during inflammatory processes. Peroxiredoxin-5 interacts with peroxisome receptor 1 and is involved in intracellular redox signaling. PRDX5 is involved in intracellular redox signaling. Peroxiredoxin-5 is a significant antioxidant protein of lung epithelial cells for its expression in the human lung increases during inflammation. PRDX5 expression is upregulated in osteoarthritis. PRDX5 may be significant in mitochondrial genome stability. Peroxiredoxin-5 has a protective role in human tendon cells against oxidative stress by reducing apoptosis and upholding collagen synthesis.
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Synonyms
Peroxiredoxin-5 mitochondrial, Prx-V, Peroxisomal antioxidant enzyme, Thioredoxin reductase, Thioredoxin peroxidase PMP20, Antioxidant enzyme B166, TPx type VI, Liver tissue 2D-page spot 71B, Alu corepressor 1, PLP, ACR1, B166, PRXV, PMP20, PRDX6, SBBI10, AOEB166, MGC117264, MGC142283, MGC142285, PRDX5.
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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
MAPIKVGDAI PAVEVFEGEP GNKVNLAELF KGKKGVLFGV PGAFTPGCSK THLPGFVEQA EALKAKGVQV VACLSVNDAF VTGEWGRAHK AEGKVRLLAD PTGAFGKETD LLLDDSLVSI FGNRRLKRFS MVVQDGIVKA LNVEPDGTGL TCSLAPNIIS QL.
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 :
ACADSB HumanDescription:
Acyl-CoA Dehydrogenase, Short Chain Human Recombinant
Short/branched chain specific acyl-CoA dehydrogenase mitochondrial, SBCAD, 2-methyl branched chain acyl-CoA dehydrogenase, 2-MEBCAD, 2-methylbutyryl-coenzyme A dehydrogenase, 2-methylbutyryl-CoA dehydrogenase, ACADSB, ACAD7, SBCAD, 2-MEBCAD.
Product # :
ENZ-643Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
ACADSB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (34-432) and having a molecular mass of 46.4kDa.ACADSB is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACADSB solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Short/branched chain specific acyl-CoA dehydrogenase (ACADSB) belongs to the acyl-CoA dehydrogenase family of enzymes which catalyze the dehydrogenation of acyl-CoA derivatives in the metabolism of fatty acids or branch chained amino acids. ACADSB catalyzes the degradation of L-isoleucine while having the highest affinity for (s)-2-methylbutyryl-CoA, isobutyryl-CoA and 2-methylhexanoyl-CoA as substrates. ACADSB may use valproyl-CoA as substrate. ACADSB gene defects cause the short/branched-chain acyl-CoA dehydrogenase deficiency (SBCADD), which is an autosomal recessive disorder characterized by an increase of 2-methylbutyrylglycine and 2-methylbutyrylcarnitine in blood and urine.
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Synonyms
Short/branched chain specific acyl-CoA dehydrogenase mitochondrial, SBCAD, 2-methyl branched chain acyl-CoA dehydrogenase, 2-MEBCAD, 2-methylbutyryl-coenzyme A dehydrogenase, 2-methylbutyryl-CoA dehydrogenase, ACADSB, ACAD7, SBCAD, 2-MEBCAD.
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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 MGSHMKSSQS EALLNITNNG IHFAPLQTFT DEEMMIKSSV KKFAQEQIAP LVSTMDENSK MEKSVIQGLF QQGLMGIEVD PEYGGTGASF LSTVLVIEEL AKVDASVAVF CEIQNTLINT LIRKHGTEEQ KATYLPQLTT EKVGSFCLSE AGAGSDSFAL KTRADKEGDY YVLNGSKMWI SSAEHAGLFL VMANVDPTIG YKGITSFLVD RDTPGLHIGK PENKLGLRAS STCPLTFENV KVPEANILGQ IGHGYKYAIG SLNEGRIGIA AQMLGLAQGC FDYTIPYIKE RIQFGKRLFD FQGLQHQVAH VATQLEAARL LTYNAARLLE AGKPFIKEAS MAKYYASEIA GQTTSKCIEW MGGVGYTKDY PVEKYFRDAK IGTIYEGASN IQLNTIAKHI DAEY.
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 :
GSTP2 MouseDescription:
Glutathione S-Transferase pi 2 Mouse Recombinant
Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.
Product # :
ENZ-943Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- purity
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Description
GSTP2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 210 amino acids (1-210 a.a.) and having a molecular mass of 23.5kDa. The GSTP2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTP2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Gltathione S-transferase PI 2, also known as GSTP2 is multifunctional enzyme which is involved in the protection of cellular components against anti-cancer drugs or peroxidative stress. Furthermore, down regulation of GSTP2 induces an increase of oxidative damage in the pyramidal cells of the CA1&CA3 regions as well as in the granular layer of the dentate gyrus, which at the end leads to structural and functional damage.
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Synonyms
Glutathione S-transferase P 2, Gst P2, GST YF-YF, GST class-pi, GST-piA.
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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
MPPYTIVYFP SPGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD LTLYQSNAIL RHLGRSLGLY GKNQREAAQV DMVNDGVEDL RGKYGTMIYR NYENGKNDYV KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY VARLSARPKI KAFLSSPEHV NRPINGNGKQ.
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.