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1000 results found for “Hydratase”
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Name :
PDE6H HumanDescription:
Phosphodiesterase 6H cGMP-Specific Cone Gamma Human Recombinant
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
Product # :
ENZ-819Price :
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Shipped with Ice Packs
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Description
PDE6H Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 106 amino acids (1-83 a.a) and having a molecular mass of 11.5 kDa. PDE6H is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PDE6H protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 40% glycerol, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
PDE6H belongs to the rod/cone cGMP-PDE gamma subunit family, which selectively catalyze the hydrolysis of 3 cyclic phosphate bonds in adenosine and/or guanine 3,5 cyclic monophosphate (cAMP and/or cGMP). This family regulates the cellular levels, localization and duration of action of these second messengers by controlling the rate of their degradation. PDE6H is the inhibitory (or gamma) subunit of the cone-specific cGMP phosphodiesterase, which is atetramer composed of two catalytic chains (alpha and beta), and two inhibitory chains (gamma). PDE6H is particularly expressed in the retina, and is implicated in the transmission and amplification of the visual signal. Mutations in PDE6H have been associated with retinal cone dystrophy type 3A.
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Synonyms
Phosphodiesterase 6H, CGMP-Specific, Cone, Gamma, Retinal Cone Rhodopsin-Sensitive CGMP 3',5'-Cyclic Phosphodiesterase, Subunit Gamma, EC 3.1.4.35, EC 3.1.4.17, RCD3, GMP-PDE Gamma, ACHM6, PDE6H.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSDNTTL PAPASNQGPT TPRKGPPKFK QRQTRQFKSK PPKKGVKGFG DDIPGMEGLG TDITVICPWE AFSHLELHEL AQFGII.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TKT HumanDescription:
Transketolase Human Recombinant
Transketolase, TK, TKT1, EC 2.2.1.1.
Product # :
ENZ-588Price :
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Description
TKT Human Recombinant produced in E. coli is a single polypeptide chain containing 643 amino acids (1-623) and having a molecular mass of 70.0kDa.TKT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TKT solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
TKT is a thiamine-dependent enzyme that takes part in the channeling of leftover sugar phosphates to glycolysis in the pentose phosphate pathway. Multiple alternatively spliced variants are known that encode the same protein.
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Synonyms
Transketolase, TK, TKT1, EC 2.2.1.1.
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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
MGSSHHHHHH SSGLVPRGSH MESYHKPDQQ KLQALKDTAN RLRISSIQAT TAAGSGHPTS CCSAAEIMAV LFFHTMRYKS QDPRNPHNDR FVLSKGHAAP ILYAVWAEAG FLAEAELLNL RKISSDLDGH PVPKQAFTDV ATGSLGQGLG AACGMAYTGK YFDKASYRVY CLLGDGELSE GSVWEAMAFA SIYKLDNLVA ILDINRLGQS DPAPLQHQMD IYQKRCEAFG WHAIIVDGHS VEELCKAFGQ AKHQPTAIIA KTFKGRGITG VEDKESWHGK PLPKNMAEQI IQEIYSQIQS KKKILATPPQ EDAPSVDIAN IRMPSLPSYK VGDKIATRKA YGQALAKLGH ASDRIIALDG DTKNSTFSEI FKKEHPDRFI ECYIAEQNMV SIAVGCATRN RTVPFCSTFA AFFTRAFDQI RMAAISESNI NLCGSHCGVS IGEDGPSQMA LEDLAMFRSV PTSTVFYPSD GVATEKAVEL AANTKGICFI RTSRPENAII YNNNEDFQVG QAKVVLKSKD DQVTVIGAGV TLHEALAAAE LLKKEKINIR VLDPFTIKPL DRKLILDSAR ATKGRILTVE DHYYEGGIGE AVSSAVVGEP GITVTHLAVN RVPRSGKPAE LLKMFGIDRD AIAQAVRGLI TKA.
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 :
CES1 HumanDescription:
Carboxylesterase 1 Human Recombinant
Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.
Product # :
ENZ-1099Price :
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Description
CES1 Human produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (19-568 a.a.) and having a molecular mass of 61.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CES1 is expressed with a 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CES1 protein solution (0.5mg/ml) contains 25mM Sodium Acetate (pH 4.0), 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
CES1 is a part of the alpha/beta fold hydrolase familyand participates in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. CES1hydrolyzes aromatic and aliphatic esters, although it has no catalytic activity toward amides or a fatty acyl-CoA ester. CES1hydrolyzes the methyl ester group of cocaine to form benzoylecgonine and catalyzes the transesterification of cocaine to form cocaethylene. CES1also plays a role in detoxification in the lung and protection of the central nervous system from ester or amide compounds.CES1 is found in most tissues, mainly in the liver.
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Synonyms
Liver carboxylesterase 1 isoform a, CES1, ACAT, CE-1, CEH, CES2, hCE-1, HMSE, HMSE1, PCE-1, REH, SES1, TGH, Acyl-coenzyme A:cholesterol acyltransferase, Brain carboxylesterase hBr1.
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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
ADLGHPSSPP VVDTVHGKVL GKFVSLEGFA QPVAIFLGIP FAKPPLGPLR FTPPQPAEPW
SFVKNATSYP PMCTQDPKAG QLLSELFTNR KENIPLKLSE DCLYLNIYTP ADLTKKNRLP
VMVWIHGGGL MVGAASTYDG LALAAHENVV VVTIQYRLGI WGFFSTGDEH SRGNWGHLDQ
VAALRWVQDN IASFGGNPGS VTIFGESAGG ESVSVLVLSP LAKNLFHRAI SESGVALTSV
LVKKGDVKPL AEQIAITAGC KTTTSAVMVH CLRQKTEEEL LETTLKMKFL SLDLQGDPRE
SQPLLGTVID GMLLLKTPEE LQAERNFHTV PYMVGINKQE FGWLIPMQLM SYPLSEGQLD
QKTAMSLLWK SYPLVCIAKE LIPEATEKYL GGTDDTVKKK DLFLDLIADV MFGVPSVIVA
RNHRDAGAPT YMYEFQYRPS FSSDMKPKTV IGDHGDELFS VFGAPFLKEG ASEEEIRLSK
MVMKFWANFA RNGNPNGEGL PHWPEYNQKE GYLQIGANTQ AAQKLKDKEV AFWTNLFAKK AVEKPPQTEH IELHHHHHH.
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 :
TPSAB1 HumanDescription:
Tryptase Alpha/Beta 1 Human Recombinant
Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.
Product # :
ENZ-652Price :
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Description
TPSAB1 Human Recombinant produced in E. coli is a single polypeptide chain containing 270 amino acids (31-275) and having a molecular mass of 30.1 kDa.TPSAB1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TPSAB1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Tryptase alpha/beta-1 (TPSAB1) is a tryptase which is the key neutral protease present in mast cells and is discharged upon the coupled activation-degranulation response of this cell type. TPSAB1 is enzymatically active only as a heparin-stabilized tetramer, and is resistant to all known endogenous proteinase inhibitors. TPSAB1 is implicated as a mediator in the pathogenesis of asthma and other allergic and inflammatory disorders.
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Synonyms
Tryptase Alpha/Beta 1, Tryptase Alpha II, Tryptase Beta-1, Tryptase Alpha-1, Tryptase Alpha/Beta-1, Tryptase-I, TPS1, TPS2, TPSB1, Tryptase-III, Mast Cell Alpha II Tryptase, Mast Cell Beta I Tryptase, EC 3.4.21.59.
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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 MGSHMIVGGQ EAPRSKWPWQ VSLRVHGPYW MHFCGGSLIH PQWVLTAAHC VGPDVKDLAA LRVQLREQHL YYQDQLLPVS RIIVHPQFYT AQIGADIALL ELEEPVNVSS HVHTVTLPPA SETFPPGMPC WVTGWGDVDN DERLPPPFPL KQVKVPIMEN HICDAKYHLG AYTGDDVRIV RDDMLCAGNT RRDSCQGDSG GPLVCKVNGT WLQAGVVSWG EGCAQPNRPG IYTRVTYYLD WIHHYVPKKP.
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 :
ACOT11 HumanDescription:
Acyl-CoA Thioesterase 11 Human Recombinant
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
Product # :
ENZ-756Price :
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Description
ACOT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 268 amino acids (19-250 a.a) and having a molecular mass of 29.9kDa. ACOT11 is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
ACOT11 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
ACOT11 belongs to the acyl-CoA thioesterase family which catalyses the transformation of activated fatty acids to the equivalent non-esterified fatty acid and coenzyme A. Expression of a mouse homolog in brown adipose tissue is induced by low temperatures and inhibited by high temperatures. Obesity-resistant mice demonstrated High levels of expression compared with obesity-prone mice, indicating BFIT takes part in acyl-CoA thioesterase 11 in obesity. BFIT has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.
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Synonyms
Acyl-CoA Thioesterase 11, StAR-Related Lipid Transfer (START) Domain Containing 14, Thioesterase, Adipose Associated, Acyl-CoA Thioester Hydrolase 11, Adipose-Associated Thioesterase, Brown Fat-Inducible Thioesterase, Thioesterase Superfamily Member 1, START Domain Containing 14, Acyl-Coenzyme A Thioesterase 11, STARD14, THEM1, THEA, BFIT, BFIT1, BFIT2, KIAA0707, EC 3.1.2.1.
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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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSNRTS RKSALRAGND SAMADGEGYR NPTEVQMSQL VLPCHTNQRG ELSVGQLLKW IDTTACLSAE RHAGCPCVTA SMDDIYFEHT ISVGQVVNIK AKVNRAFNSS MEVGIQVASE DLCSEKQWNV CKALATFVAR REITKVKLKQ ITPRTEEEKM EHSVAAERRR MRLVYADTIK DLLANCAIQG DLESRDCSRM VPAEKTRVES VELVLPPHAN HQGNTFGGQI MAWMENVA
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 :
CTSZ HumanDescription:
Cathepsin-Z Human Recombinant
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
Product # :
ENZ-748Price :
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Description
CTSZ Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 265 amino acids (62-303) and having a molecular mass of 29.5kDa.CTSZ is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CTSZ solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-Z (CTSZ) is a lysosomal cysteine proteinase and member of the peptidase C1 family. CTSZ, which has been also known as cathepsin X and cathepsin P, exhibits carboxy-monopeptidase and carboxy-dipeptidase activities. CTSZ is expressed ubiquitously in cancer cell lines and primary tumors and, similar to other members of this family, takes part in tumorigenesis.
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Synonyms
Cathepsin Z preproprotein, Cathepsin Z, CTSX, Cathepsin P, Cathepsin X, CTSZ, Cathepsin-Z.
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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 MGSLPKSWDW RNVDGVNYAS ITRNQHIPQY CGSCWAHAST SAMADRINIK RKGAWPSTLL SVQNVIDCGN AGSCEGGNDL SVWDYAHQHG IPDETCNNYQ AKDQECDKFN QCGTCNEFKE CHAIRNYTLW RVGDYGSLSG REKMMAEIYA NGPISCGIMA TERLANYTGG IYAEYQDTTY INHVVSVAGW GISDGTEYWI VRNSWGEPWG ERGWLRIVTS TYKDGKGARY NLAIEEHCTF GDPIV.
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 :
AKR1A1 HumanDescription:
Aldo-Keto Reductase Family 1 Member A1 Human Recombinant
Alcohol dehydrogenase, ALR, ARM, DD3, ALDR1, MGC1380, MGC12529, AKR1A1, Alcohol dehydrogenase [NADP+], Aldehyde reductase, Aldo-keto reductase family 1 member A1.
Product # :
ENZ-464Price :
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Description
AKR1A1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 325 amino acids (1-325 a.a.) and having a molecular mass of 36.5 kDa. AKR1A1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AKR1A1 solution containing 20mM Tris pH-8, 50mM NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
AKR1A1 is part of the aldo/keto reductase superfamily, it catalyzes the NADPH-dependent reduction from a range of aromatic and aliphatic aldehydes to their related alcohols. AKR1A1 corresponds (65% identity) to aldose reductase, an enzyme that takes part in the pathogenesis of some diabetic and galactosemic complications. AKR1A1 is involved in the activation of procarcinogens, such as polycyclic aromatic hydrocarbon trans-dihydrodiols, and in the metabolism of various xenobiotics and drugs.
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Synonyms
Alcohol dehydrogenase, ALR, ARM, DD3, ALDR1, MGC1380, MGC12529, AKR1A1, Alcohol dehydrogenase [NADP+], Aldehyde reductase, Aldo-keto reductase family 1 member A1.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
AKR1A1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVQALG LSNFNSRQID DILSVASVRP AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEKYGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV PMLTVDGKRV PRDAGHPLYP FNDPY
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 :
MTHFD2 HumanDescription:
MTHFD2 Human Recombinant
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.
Product # :
ENZ-853Price :
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Description
MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.
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Synonyms
Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.
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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 MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.
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 :
ALDOC HumanDescription:
Aldolase C Fructose-Bisphosphate Human Recombinant
Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 3.
Product # :
ENZ-969Price :
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Description
ALDOC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-364 a.a) and having a molecular mass of 39.4kDa. ALDOC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ALDOC protein solution (1mg/ml) containing 20mM Tris-Hcl Buffer (pH 8.0), 20% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aldolase C Fructose-Bisphosphate (ALDOC) belongs to the class I fructose-bisphosphate aldolase family. ALDOC is a glycolytic enzyme which catalyzes the reversible aldol cleavage of fructose-1,6-biphosphate and fructose 1-phosphate to dihydroxyacetone phosphate and either glyceraldehyde-3-phosphate or glyceraldehydes respectively. ALDOC is expressed exclusively in the hippocampus and Purkinje cells of the brain.
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Synonyms
Aldolase, Fructose-Bisphosphate C, Aldolase C, Fructose-Bisphosphate, Brain-Type Aldolase, EC 4.1.2.13, ALDC, Fructose-1,6-Biphosphate Triosephosphate Lyase, Fructose-Bisphosphate Aldolase C, Fructoaldolase C, Aldolase 3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY.
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 :
DERADescription:
Deoxyribose-Phosphate Aldolase E.Coli Recombinant
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
Product # :
ENZ-127Price :
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Description
DERA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 279 amino acids (1-259 a.a.) and having a molecular mass of 29.9kDa.DERA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DERA solution (1mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Deoxyribose-phosphate aldolase (DERA) is a member of the deoC/fbaB aldolase protein family involved in the carbohydrate degradation pathway. DERA catalyzes the conversion of 2-deoxy-D-ribose 5-phosphate to D-glyceraldehyde 3-phosphate and an acetyldehyde.
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Synonyms
Putative deoxyribose-phosphate aldolase, DERA, 2-deoxy-D-ribose 5-phosphate aldolase, Phosphodeoxyriboaldolase, Deoxyriboaldolase, DERA, CGI-26.
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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 MTDLKASSLR ALKLMDLTTL NDDDTDEKVI ALCHQAKTPV GNTAAICIYP RFIPIARKTL KEQGTPEIRI ATVTNFPHGN DDIDIALAET RAAIAYGADE VDVVFPYRAL MAGNEQVGFD LVKACKEACA AANVLLKVII ETGELKDEAL IRKASEISIK AGADFIKTST GKVAVNATPE SARIMMEVIR DMGVEKTVGF KPAGGVRTAE DAQKYLAIAD ELFGADWADA RHYRFGASSL LASLLKALGH GDGKSASSY.
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 :
NANP HumanDescription:
N-Acetylneuraminic Acid Phosphatase Human Recombinant
N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.
Product # :
ENZ-009Price :
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Description
NANP Human Recombinant fused with a 36 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 284 amino acids (1-248 a.a.) and having a molecular mass of 31.9kDa. The NANP is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NANP solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
N-acylneuraminate-9-phosphatase (NANP) belongs to the haloacid dehalogenase (HAD) family and is responsible for dephosphorylating N-acylneuraminate 9-phosphate to form N-acylneuraminate (N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate). The catalytic activity of NANP is relies on the presence of magnesium and is inhibited by vanadate and calcium, which is typical of the HAD phosphatase family.
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Synonyms
N-acylneuraminate-9-phosphatase, Haloacid dehalogenase-like hydrolase domain-containing protein 4, Neu5Ac-9-Pase, NANP, HDHD4, MGC26833, C20orf147, dJ694B14.3.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMGLS RVRAVFFDLD NTLIDTAGAS RRGMLEVIKL LQSKYHYKEE AEIICDKVQV KLSKECFHPY NTCITDLRTS HWEEAIQETK GGAANRKLAE ECYFLWKSTR LQHMTLAEDV KAMLTELRKE VRLLLLTNGD RQTQREKIEA CACQSYFDAV VVGGEQREEK PAPSIFYYCC NLLGVQPGDC VMVGDTLETD IQGGLNAGLK ATVWINKNGI VPLKSSPVPH YMVSSVLELP ALLQSIDCKV SMST.
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 :
DUT HumanDescription:
Deoxyuridine Triphosphatase Human Recombinant
Deoxyuridine 5''-triphosphate nucleotidohydrolase mitochondrial, dUTPase, dUTP pyrophosphatase, Deoxyuridine Triphosphatase, DUT, FLJ20622.
Product # :
ENZ-568Price :
Quantity :
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Description
DUT Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (70-252 a.a.) and having a molecular mass of 21.6kDa. The DUT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The DUT solution (1mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Deoxyuridine Triphosphatase (DUT) is a ubiquitous enzyme that functions in nucleotide metabolism. Deoxyuridine Triphosphatase, in the presence of magnesium ions, is responsible for hydrolyzing dUTP to dUMP and diphosphate. This reaction is imperative for keeping the intracellular dUTP concentration low so that uracil does not become incorporated into DNA. Extensive integration of uracil into DNA can eventually lead to cell death. This suggests that DUT is crucial for cell viability, further implying that it is a prospective target for anticancer therapy.
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Synonyms
Deoxyuridine 5''-triphosphate nucleotidohydrolase mitochondrial, dUTPase, dUTP pyrophosphatase, Deoxyuridine Triphosphatase, DUT, FLJ20622.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASTVGAAGW KGELPKAGGS PAPGPETPAI SPSKRARPAE VGGMQLRFAR LSEHATAPTR GSARAAGYDL YSAYDYTIPP MEKAVVKTDI QIALPSGCYG RVAPRSGLAA KHFIDVGAGV IDEDYRGNVG VVLFNFGKEK FEVKKGDRIA QLICERIFYP EIEEVQALDD TERGSGGFGS TGKN.
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 :
ASPA Human, HisDescription:
Aspartoacylase Human Recombinant, His Tag
Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP.
Product # :
ENZ-572Price :
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Description
ASPA Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (1-313) and having a molecular mass of 38.1kDa.ASPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ASPA solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 1mM DTT, 0.1M NaCl and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Aspartoacylase is a homodimer which catalyzes the deacetylation of N-acetylaspartic acid (NAA) (a protein whose hydrolysis is crucial to maintenance of intact white matter) to generate acetate and L-aspartate. Aspartoacylase (ASPA) is expressed in the liver, lung and kidney tissue, as well as in the skeletal muscle and in cerebral white matter. NAA is ample in the brain where hydrolysis by aspartoacylase is believed to aid maintain white matter. In other tissues ASPA functions as a scavenger of NAA from body fluids. ASPA gene mutations cause Canavan disease (CAND or spongy degeneration of the brain).
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Synonyms
Aspartoacylase, Aminoacylase-2, ACY-2, ASPA, ACY2, ASP.
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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 MGSMTSCHIA EEHIQKVAIF GGTHGNELTG VFLVKHWLEN GAEIQRTGLE VKPFITNPRA VKKCTRYIDC DLNRIFDLEN LGKKMSEDLP YEVRRAQEIN HLFGPKDSED SYDIIFDLHN TTSNMGCTLI LEDSRNNFLI QMFHYIKTSL APLPCYVYLI
EHPSLKYATT RSIAKYPVGI EVGPQPQGVL RADILDQMRK MIKHALDFIH HFNEGKEFPP CAIEVYKIIE KVDYPRDENG EIAAIIHPNL QDQDWKPLHP GDPMFLTLDG KTIPLGGDCT VYPVFVNEAA YYEKKEAFAK TTKLTLNAKS IRCCLH.
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 :
ASPH HumanDescription:
Aspartate Beta-Hydroxylase Human Recombinant
AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.
Product # :
ENZ-488Price :
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Description
ASPH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 217 amino acids (75-270 a.a.) and having a molecular mass of 24.5 kDa. The ASPH is fused to a 20 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The ASPH protein solution contains 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
ASPH hydroxylates an Asp or Asn residue in EGF domains. ASPH is involved in calcium homeostasis. ASPH is expressed from two promoters and goes through extensive alternative splicing. The encoded set of ASPH proteins share varying quantities of overlap near their N-termini although have considerable differences in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the EGF domain, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Further isoforms diverge mainly in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum.
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Synonyms
AAH, BAH, CASQ2BP1, HAAH, JCTN, Junctin, EC 1.14.11.16, Aspartyl/asparaginyl beta-hydroxylase, Aspartate beta-hydroxylase, Peptide-aspartate beta-dioxygenase, ASP beta-hydroxylase, ASPH.
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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 MFDLVDYEEV LGKLGIYDAD GDGDFDVDDA KVLLGLKERS TSEPAVPPEE AEPHTEPEEQ VPVEAEPQNI EDEAKEQIQS LLHEMVHAEH ETEHSYHVEE TVSQDCNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT YQVYEEQAVY EPLENEGIEI TEVTAPPEDN PVEDSQVIVE EVSIFPVEEQ QEVPPDT.
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 :
ENOPH1 HumanDescription:
Enolase-Phosphatase-1 Human Recombinant
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
Product # :
ENZ-077Price :
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Description
ENOPH1 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 281 amino acids (1-261 a.a.) and having a molecular mass of 31kDa. The ENOPH1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ENOPH1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Enolase-phosphatase E1 (ENOPH1) belongs to the MasA family of the HAD (halo-acid dehalogenase)-like hydrolase superfamily. ENOPH1 is a bifunctional enzyme which demonstrates both phosphatase and atypical enolase activities. ENOPH1 has a significant role in the ubiquitous methionine salvage pathway which is a biochemical pathway found in all organisms that regulate methionine levels in the cell.
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Synonyms
Enolase-phosphatase E1, 2,3-diketo-5-methylthio-1-phosphopentane phosphatase, MASA homolog, ENOPH1, MASA, E1, MST145, FLJ12594, DKFZp586M0524.
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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 MVVLSVPAEV TVILLDIEGT TTPIAFVKDI LFPYIEENVK EYLQTHWEEE ECQQDVSLLR KQAEEDAHLD GAVPIPAASG NGVDDLQQMI QAVVDNVCWQ MSLDRKTTAL KQLQGHMWRA AFTAGRMKAE FFADVVPAVR KWREAGMKVY IYSSGSVEAQ KLLFGHSTEG DILELVDGHF DTKIGHKVES ESYRKIADSI GCSTNNILFL TDVTREASAA EEADVHVAVV VRPGNAGLTD DEKTYYSLIT SFSELYLPSS T.
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 :
FBP1 HumanDescription:
Fructose-1,6-Bisphosphatase 1 Human Recombinant
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 1.
Product # :
ENZ-454Price :
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Description
The FBP1 Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 39kDa and containing 358 amino acids (1-338 a.a.). The FBP1 enzyme is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatography techniques.
Source
Escherichia Coli.
Formulation
The FBP1 protein solution is formulated in 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
FBP1 is a gluconeogenesis regulatory protein which catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate and inorganic phosphate. FBP1 deficiency is associated with hypoglycemia and metabolic acidosis. FBP1 regulates mouse endogenous glucose production. FBP1 coupled with phosphofructokinase (PFK) takes part in the metabolism of pancreatic islet cells.
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Synonyms
FBP1, FBP, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, FBPase 1, Fructose-1,6-bisphosphatase 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 MADQAPFDTD VNTLTRFVME EGRKARGTGE LTQLLNSLCT AVKAISSAVR KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVMNMLKSSF ATCVLVSEED KHAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSVGTIFGIY RKKSTDEPSE KDALQPGRNL VAAGYALYGS ATMLVLAMDC GVNCFMLDPA IGEFILVDKD VKIKKKGKIY SLNEGYARDF DPAVTEYIQR KKFPPDNSAP YGARYVGSMV ADVHRTLVYG GIFLYPANKK SPNGKLRLLY ECNPMAYVME KAGGMATTGK EAVLDVIPTD IHQRAPVILG SPDDVLEFLK VYEKHSAQ.
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 :
FUCA2 HumanDescription:
Fucosidase Alpha-L- 2 Plasma Human Recombinant
Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.
Product # :
ENZ-840Price :
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Description
FUCA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 462 amino acids (29-467 a.a) and having a molecular mass of 53.3kDa.FUCA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FUCA2 protein solution (1mg/ml) containing 20mM phosphate (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Fucosidase Alpha-L- 2 Plasma (FUCA2) is a plasma alpha-L-fucosidase, which represents 10-20% of the total cellular fucosidase activity. FUCA2 protein belongs to the glycosyl hydrolase 29 family, and catalyzes the hydrolysis of the alpha-1,6-linked fucose fused to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. FUCA2 is crucial for Helicobacter pylori adhesion to human gastric cancer cells.
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Synonyms
Fucosidase, alpha-L- 2, plasma, dJ20N2.5, RP1-20N2.5, Plasma alpha-L-fucosidase, Alpha-L-fucoside fucohydrolase 2, Alpha-L-fucosidase 2, PSEC0151, UNQ227/PRO260.
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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 MGSHSATRFD PTWESLDARQ LPAWFDQAKF GIFIHWGVFS VPSFGSEWFW WYWQKEKIPK YVEFMKDNYP PSFKYEDFGP LFTAKFFNAN QWADIFQASG AKYIVLTSKH HEGFTLWGSE YSWNWNAIDE GPKRDIVKEL EVAIRNRTDL RFGLYYSLFE WFHPLFLEDE SSSFHKRQFP VSKTLPELYE LVNNYQPEVL WSDGDGGAPD QYWNSTGFLA WLYNESPVRG TVVTNDRWGA GSICKHGGFY TCSDRYNPGH LLPHKWENCM TIDKLSWGYR REAGISDYLT IEELVKQLVE TVSCGGNLLM NIGPTLDGTI SVVFEERLRQ MGSWLKVNGE AIYETHTWRS QNDTVTPDVW YTSKPKEKLV YAIFLKWPTS GQLFLGHPKA ILGATEVKLL GHGQPLNWIS LEQNGIMVEL PQLTIHQMPC KWGWALALTN VI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
GLRX1 HumanDescription:
Glutaredoxin 1 Human Recombinant
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.
Product # :
ENZ-391Price :
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Description
Glutaredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 106 amino acids having a molecular mass of 11.7 kDa.
Source
Escherichia Coli.
Formulation
Glutaredoxin solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT & 10% Glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.
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Synonyms
Thioltransferase, GRX, GLRX1, GRX1, GRX-1, GLRX-1, Glutathione-dependent oxidoreductase 1, Glutaredoxin-1, Thioltransferase-1, TTase-1, GLRX, MGC117407.
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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
MAQEFVNCKI QPGKVVVFIK PTCPYCRRAQ EILSQLPIKQ GLLEFVDITA TNHTNEIQDY LQQLTGARTV PRVFIGKDCI GGCSDLVSLQ QSGELLTRLK QIGALQ.
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 :
PRSS3 HumanDescription:
Protease Serine 3 Human Recombinant
Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.
Product # :
ENZ-735Price :
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Description
PRSS3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (81-304) and having a molecular mass of 26.0kDa.PRSS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PRSS3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
PRSS3 is a trypsinogen, and a member of the trypsin family of serine proteases. PRSS3 is expressed in the pancreas and brain and is unaffected by common trypsin inhibitors. It is active on peptide linkages involving the carboxyl group of lysine or arginine. PRSS3 is restricted to the locus of T cell receptor beta variable orphans on chromosome 9. 4 different isoforms encoded by 4 transcript variants were identified for this gene.
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Synonyms
Protease Serine 3 (Mesotrypsin), Protease Serine 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Trypsin III, Trypsinogen IV, Trypsinogen 5, Pancreatic Trypsinogen III, MTG, TRY3, PRSS4, T9, EC 3.4.21.
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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 MGSIVGGYTC EENSLPYQVS LNSGSHFCGG SLISEQWVVS AAHCYKTRIQ VRLGEHNIKV LEGNEQFINA AKIIRHPKYN RDTLDNDIML IKLSSPAVIN ARVSTISLPT APPAAGTECL ISGWGNTLSF GADYPDELKC LDAPVLTQAE CKASYPGKIT NSMFCVGFLE GGKDSCQRDS GGPVVCNGQL QGVVSWGHGC AWKNRPGVYT KVYNYVDWIK DTIAANS
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 :
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 :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
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.
- View Data Sheet
Name :
CHST10 HumanDescription:
Carbohydrate Sulfotransferase 10 Human Recombinant
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
Product # :
ENZ-894Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHST10 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
Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.
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Synonyms
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
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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 MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.
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 :
CTSA MouseDescription:
Cathepsin-A Mouse Recombinant
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
Product # :
ENZ-945Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
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Description
CTSA produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 459 amino acids (24-474 a.a.) and having a molecular mass of 52.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).CTSA is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9 Insect cells.
Formulation
CTSA protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cathepsin-A (CTSA) is a protective protein which is crucial for both the activity of beta-galactosidase and neuraminidase, CTSA associates with these enzymes and exerts a protective function required for their stability and activity. The CTSA protein is also a carboxypeptidase and can deamidate tachykinins. CTSA is a component of the lysosomal multienzyme complex along with beta-galactosidase and sialidase Neu1. CTSA is a multicatalytic enzyme with deamidase and esterase in addition to carboxypeptidase activities.
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Synonyms
Lysosomal protective protein (EC:3.4.16.5), Carboxypeptidase C, Carboxypeptidase, Cathepsin A, Protective protein cathepsin A, PPCA, Protective protein for beta-galactosidase.
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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
APDQDEIDCL PGLAKQPSFR QYSGYLRASD SKHFHYWFVE SQNDPKNSPV VLWLNGGPGC SSLDGLLTEH GPFLIQPDGV TLEYNPYAWN LIANVLYIES PAGVGFSYSD DKMYVTNDTE VAENNYEALK DFFRLFPEYK DNKLFLTGES YAGIYIPTLA VLVMQDPSMN LQGLAVGNGL ASYEQNDNSL VYFAYYHGLL GNRLWTSLQT HCCAQNKCNF YDNKDPECVN NLLEVSRIVG KSGLNIYNLY APCAGGVPGR HRYEDTLVVQ DFGNIFTRLP LKRRFPEALM RSGDKVRLDP PCTNTTAPSN YLNNPYVRKA LHIPESLPRW DMCNFLVNLQ YRRLYQSMNS QYLKLLSSQK YQILLYNGDV DMACNFMGDE WFVDSLNQKM EVQRRPWLVD YGESGEQVAG FVKECSHITF LTIKGAGHMV PTDKPRAAFT MFSRFLNKEP YVEHHHHHH.
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 :
ADH1C Human, sf9Description:
Alcohol Dehydrogenase 1C, Human Recombinant, sf9
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
Product # :
ENZ-1010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
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Description
ADH1C Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 381 amino acids (1-375) and having a molecular mass of 40.6kDa. ADH1C is fused to a 6 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADH1C protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
ADH1C is a member of the zinc-containing alcohol dehydrogenase family which metabolizes a large assortment of substrates, such as ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH1 is a monomorphic and a key factor in fetal and infant livers, becoming less active in gestation and only weakly active during adulthood.
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Synonyms
ADH1, ADH1C, ADH3, Alcohol dehydrogenase 1C, Alcohol dehydrogenase subunit gamma.
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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
MSTAGKVIKC KAAVLWELKK PFSIEEVEVA PPKAHEVRIK MVAAGICRSD EHVVSGNLVT PLPVILGHEA AGIVESVGEG VTTVKPGDKV IPLFTPQCGK CRICKNPESN YCLKNDLGNP RGTLQDGTRR FTCSGKPIHH FVGVSTFSQY TVVDENAVAK IDAASPLEKV CLIGCGFSTG YGSAVKVAKV TPGSTCAVFG LGGVGLSVVM GCKAAGAARI IAVDINKDKF AKAKELGATE CINPQDYKKP IQEVLKEMTD GGVDFSFEVI GRLDTMMASL LCCHEACGTS VIVGVPPDSQ NLSINPMLLL TGRTWKGAIF GGFKSKESVP KLVADFMAKK FSLDALITNI LPFEKINEGF DLLRSGKSIR
TVLTFHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.