Search: 1000 results found for "Heparanase"

Description:

Glutamine--Fructose-6-Phosphate Transaminase 1 Human Recombinant

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 1.

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ENZ-818

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Description

GFPT1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (332-699 a.a) and having a molecular mass of 43.7kDa.GFPT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GFPT1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol, 2mM DTT and 2mM EDTA.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Glutamine--Fructose-6-Phosphate Transaminase 1 (GFPT1) participates in the hexosamine pathway and controls the glucose fluidity into the hexosamine pathway. GFPT1 regulates the availability of precursors for N- and O-linked glycosylation of proteins. GFPT1 controls the circadian expression of clock genes ARNTL/BMAL1 and CRY1.
Synonyms
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1, D-fructose-6-phosphate amidotransferase 1, Glutamine:fructose-6-phosphate amidotransferase 1, GFAT 1, GFAT1, Hexosephosphate aminotransferase 1, GFPT1, GFAT, GFPT, CMSTA1, GFA, GFAT1m, GFPT1L, MSLG, Glutamine--Fructose-6-Phosphate Transaminase 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQQIMKGN FSSFMQKEIF EQPESVVNTM RGRVNFDDYT VNLGGLKDHI KEIQRCRRLI LIACGTSYHA GVATRQVLEE LTELPVMVEL ASDFLDRNTP VFRDDVCFFL SQSGETADTL MGLRYCKERG ALTVGITNTV GSSISRETDC GVHINAGPEI GVASTKAYTS QFVSLVMFAL MMCDDRISMQ ERRKEIMLGL KRLPDLIKEV LSMDDEIQKL ATELYHQKSV LIMGRGYHYA TCLEGALKIK EITYMHSEGI LAGELKHGPL ALVDKLMPVI MIIMRDHTYA KCQNALQQVV ARQGRPVVIC DKEDTETIKN TKRTIKVPHS VDCLQGILSV IPLQLLAFHL AVLRGYDVDF PRNLAKSVTV E.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Esterase D,S-Formylglutathione Hydrolase Human Recombinant

S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.

Product # :

ENZ-447

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Description

Esterase-D Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 302 amino acids (1-282 a.a.) and having a molecular mass of 33.6kDa.The Esterase-D is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Esterase-D solution contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Formylglutathione hydrolase (Esterase D) is a member of the esterase D family. Esterase D is a serine hydrolase involved in the detoxification of formaldehyde. Esterase D is active toward various substrates including O-acetylated sialic acids, and it may possibly be involved in the recycling of sialic acids. Esterase D is used as a genetic marker for retinoblastoma and Wilson's disease.
Synonyms
S-formylglutathione hydrolase, FGH, Esterase D, ESD, FLJ11763, esterase D/formylglutathione hydrolase.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV VFRLQEDYDH SYYFIATFIT DHIRHHAKYL NA.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Monoglyceride Lipase Human Recombinant

Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.

Product # :

ENZ-019

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Description

MGLL 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 333 amino acids (1-313 a.a.) and having a molecular mass of 36.4kDa. The MGLL is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MGLL solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
MGLL is a membrane-associated member of the serine hydrolase superfamily. MGLL is expressed in abundance in skeletal muscle and adipose tissue. MGLL functions jointly with hormone-sensitive lipase (LIPE) to hydrolyze intracellular triglyceride stores in adipocytes and other cells to fatty acids and glycerol. MGLL may also complement lipoprotein lipase (LPL) in completing hydrolysis of monoglycerides resulting from degradation of lipoprotein triglycerides.
Synonyms
Monoglyceride lipase, MGL, HU-K5, Lysophospholipase homolog, Lysophospholipase-like, Monoacylglycerol lipase, MAGL, MGLL, HUK5.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH METGPEDPSS MPEESSPRRT PQSIPYQDLP HLVNADGQYL FCRYWKPTGT PKALIFVSHG AGEHSGRYEE LARMLMGLDL LVFAHDHVGH GQSEGERMVV SDFHVFVRDV LQHVDSMQKD YPGLPVFLLG HSMGGAIAIL TAAERPGHFA GMVLISPLVL ANPESATTFK VLAAKVLNLV LPNLSLGPID SSVLSRNKTE VDIYNSDPLI CRAGLKVCFG IQLLNAVSRV ERALPKLTVP FLLLQGSADR LCDSKGAYLL MELAKSQDKT LKIYEGAYHV LHKELPEVTN SVFHEINMWV SQRTATAGTA SPP.

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Description:

Tyrosyl-tRNA Synthetase Human Recombinant

Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.

Product # :

ENZ-134

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Description

YARS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-528 a.a.) and having a molecular mass of 61.3kDa.YARS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tyrosyl-tRNA synthetase (YARS) is a member of the class I tRNA synthetase family. YARS is a vital enzyme which catalyzes the aminoacylation of tRNATrp with tryptophan, a critical function of the cell’s protein synthesis machinery. Expression of YARS is highly stimulated in human cells by the addition of IFN-gamma.
Synonyms
Tyrosyl-tRNA synthetase cytoplasmic, Tyrosyl--tRNA ligase, TyrRS, YARS, YRS, YTS, CMTDIC.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGDAPSPEEK LHLITRNLQE VLGEEKLKEI LKERELKIYW GTATTGKPHV AYFVPMSKIA DFLKAGCEVT ILFADLHAYL DNMKAPWELL ELRVSYYENV IKAMLESIGV PLEKLKFIKG TDYQLSKEYT LDVYRLSSVV TQHDSKKAGA EVVKQVEHPL LSGLLYPGLQ ALDEEYLKVD AQFGGIDQRK IFTFAEKYLP ALGYSKRVHL MNPMVPGLTG SKMSSSEEES KIDLLDRKED VKKKLKKAFC EPGNVENNGV LSFIKHVLFP LKSEFVILRD EKWGGNKTYT AYVDLEKDFA AEVVHPGDLK NSVEVALNKL LDPIREKFNT PALKKLASAA YPDPSKQKPM AKGPAKNSEP EEVIPSRLDI RVGKIITVEK HPDADSLYVE KIDVGEAEPR TVVSGLVQFV PKEELQDRLV VVLCNLKPQK MRGVESQGML LCASIEGINR QVEPLDPPAG SAPGEHVFVK GYEKGQPDEE LKPKKKVFEK LQADFKISEE CIAQWKQTNF MTKLGSISCK SLKGGNIS.

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Description:

Cathepsin-S Human Recombinant

Cathepsin S, MGC3886, CTSS, Cathepsin-S.

Product # :

ENZ-686

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Description

CTSS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 336 amino acids (17-331) and having a molecular mass of 38.1kDa. CTSS is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CTSS solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Cathepsin S (CTSS) belongs to the peptidase C1 family. CTSS is a lysosomal cysteine proteinase that participates in the degradation of antigenic proteins to peptides for presentation on MHC class II molecules. CTSS functions as an elastase over a broad pH range in alveolar macrophages.
Synonyms
Cathepsin S, MGC3886, CTSS, Cathepsin-S.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQLHKDPTLD HHWHLWKKTY GKQYKEKNEE AVRRLIWEKN LKFVMLHNLE HSMGMHSYDL GMNHLGDMTS EEVMSLMSSL RVPSQWQRNI TYKSNPNWIL PDSVDWREKG CVTEVKYQGS CGACWAFSAV GALEAQLKLK TGKLVSLSAQ NLVDCSTEKY GNKGCNGGFM TTAFQYIIDN KGIDSDASYP YKAMDQKCQY DSKYRAATCS KYTELPYGRE DVLKEAVANK GPVSVGVDAR HPSFFLYRSG VYYEPSCTQN VNHGVLVVGY GDLNGKEYWL VKNSWGHNFG EEGYIRMARN KGNHCGIASF PSYPEI.

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Description:

Hemoglobin-Zeta Mouse Recombinant

Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.

Product # :

PRO-2517

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Description

HBZ Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 162 amino acids (1-142 a.a) and having a molecular mass of 18.3kDa.HBZ is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HBZ protein solution (0.25mg/ml) containing 20mM MES(pH6.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Hemoglobin Subunit Zeta (Hbz) or Hba-x is a alpha-like hemoglobin and part of the globin family. The protein is expressed and produced in the the yolk sac in early stages of embryonic development. Hemoglobin subunit zeta has 2 pseudogenes and 5 functional genes.
Synonyms
Hemoglobin subunit zeta, Hba-x, Hbz1, AI450015, Alpha-like embryonic globin chain x, Zeta-globin.
Physical Appearance
Sterile Filtered clear colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLMKNERAI IMSMWEKMAA QAEPIGTETL ERLFCSYPQT KTYFPHFDLH HGSQQLRAHG FKIMTAVGDA VKSIDNLSSA LTKLSELHAY ILRVDPVNFK LLSHCLLVTM AARFPADFTP EVHEAWDKFM SILSSILTEK YR.

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Description:

Hydroxysteroid (17-beta) Dehydrogenase 10 Human Recombinant

17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.

Product # :

PRO-823

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Description

HSD17B10 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 271 amino acids (12-261 a.a.) and having a molecular mass of 28.1 kDa. HSD17B10 protein is fused to a 21 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

HSD17B10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT & 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
HSD17B10 functions in mitochondrial tRNA maturation. HSD17B10 is part of mitochondrial ribonuclease P, an enzyme composed of MRPP1/RG9MTD1, MRPP2/HSD17B10 and MRPP3/KIAA0391, which cleaves tRNA molecules in their 5''-ends. HSD17B10 interacts with intracellular amyloid-beta, and contributes to the neuronal dysfunction associated with Alzheimer disease.
Synonyms
17b-HSD10, ABAD, CAMR, DUPXp11.22, ERAB, HADH2, HCD2, MHBD, MRPP2, MRX17, MRX31, SCHAD, MRXS10, SDR5C1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVAVITGGAS GLGLATAERL VGQGASAVLL DLPNSGGEAQ AKKLGNNCVF APADVTSEKD VQTALALAKG KFGRVDVAVN CAGIAVASKT YNLKKGQTHT LEDFQRVLDV NLMGTFNVIR LVAGEMGQNE PDQGGQRGVI INTASVAAFE GQVGQAAYSA SKGGIVGMTL PIARDLAPIG IRVMTIAPGL FGTPLLTSLP EKVCNFLASQ VPFPSRLGDP AEYAHLVQAI IENPFLNGEV IRLDGAIRMQ P.

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Description:

Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant

Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.

Product # :

ENZ-872

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Description

GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
Synonyms
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.

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.

Description:

Glutathione Transferase Zeta 1 Human Recombinant

MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.

Product # :

ENZ-494

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Description

GSTZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 236 amino acids (1-216 a.a.) and having a molecular mass of 26.2 kDa. The GSTZ1 is fused to a 20 amino acid His-Tag at N-terminus and purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The GSTZ1 protein solution contains 1x PBS pH-7.4 and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GSTZ1 is part of the glutathione S-transferase super-family which encodes multifunctional enzymes vital in the detoxification of electrophilic molecules, including carcinogens, mutagens, and several therapeutic drugs, by conjugation with glutathione. GSTZ1 participates in the catabolism of phenylalanine and tyrosine. Thus defects in GSTZ1 cause harsh metabolic disorders including alkaptonuria, phenylketonuria and tyrosinaemia. GSTZ1 is a bifunctional protein which has minimal glutathione-conjugating activity with 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. GSTZ1 has low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. GSTZ1 catalyzes the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid.
Synonyms
MAAI, GSTZ-1, MAI, Maleylacetone Isomerase, EC 2.5.1.18, Maleylacetoacetate isomerase, Glutathione S-transferase zeta 1, EC 5.2.1.2, GSTZ1-1, MGC2029, GSTZ1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQAGKPILYS YFRSSCSWRV RIALALKGID YETVPINLIK DGGQQFSKDF QALNPMKQVP TLKIDGITIH QSLAIIEYLE ETRPTPRLLP QDPKKRASVR MISDLIAGGI QPLQNLSVLK QVGEEMQLTW AQNAITCGFN ALEQILQSTA GIYCVGDEVT MADLCLVPQV ANAERFKVDL TPYPTISSIN KRLLVLEAFQ VSHPCRQPDT PTELRA.

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Description:

Lactate Dehydrogenase B Mouse Recombinant

L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.

Product # :

ENZ-1052

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Description

LDHB Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-334 a.a) and having a molecular mass of 39kDa.LDHB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 150 units/mg, in which one unit will 1.0 umole of pyruvate to L-lactate and beta-NAD per minute at pH 7.5.

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Introduction
Lactate dehydrogenase (LDH) is an enzyme(EC1.1.1.27) present in a wide variety of organisms, including plants and animals.
A tetrameric enzyme that catalyses the interconversion of pyruvateand lactate with concomitant interconversion of NADH and NAD+. At high concentrations of pyruvate, the enzyme exhibits feedback inhibition and the rate of conversion of pyruvate to lactate is decreased. In vertebrates, genes for three different subunits (LDH-A, LDH-B and LDH-C) exist.
Synonyms
L-lactate dehydrogenase B chain, LDH-B, LDH heart subunit, LDH-H, Ldh-2, Ldh2, Ldhb.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage, it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMATLKEK LIASVADDEA AVPNNKITVV GVGQVGMACA ISILGKSLAD ELALVDVLED KLKGEMMDLQ HGSLFLQTPK IVADKDYSVT ANSKIVVVTA GVRQQEGESR LNLVQRNVNV FKFIIPQIVK YSPDCTIIVV SNPVDILTYV TWKLSGLPKH RVIGSGCNLD SARFRYLMAE KLGIHPSSCH GWILGEHGDS SVAVWSGVNV AGVSLQELNP EMGTDNDSEN WKEVHKMVVD SAYEVIKLKG YTNWAIGLSV ADLIESMLKN LSRIHPVSTM VKGMYGIENE VFLSLPCILN ARGLTSVINQ KLKDDEVAQL RKSADTLWDI QKDLKDL.

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.

Description:

Uracil DNA Glycosilase

Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.

Product # :

ENZ-352

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Description

E.Coli Uracil DNA Glycosilase (UNG) catalyses the release of free Uracil from Uracil-containing DNA. UNG efficiently hydrolyzes uracil from signle-stranded or double-stranded DNA, but not from oligomers (6 fewer bases).

Source

Escherichia Coli strain that carries the UNG gene from E.coli.

Formulation

UNG solution in 10mM Tris-HCl (pH-7.4 at 25°C), 50mM KCl, 1mM DTT, 0.1mM EDTA, 0.1 mg/ml BSA and 50% glycerol.

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Synonyms
Uracil DNA Glycosilase, Uracil DNA Glycosylase, UNG.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Uracil DNA Glycosilase although stable at 15°C for 1 week, should be stored below -18°C. Please prevent freeze-thaw cycles.
Reaction Conditions
1X UNG Reaction Buffer, incubate at 37°C.UNG is active over a broad pH rabge with an optimum at pH-8.0, doesn't require divalent cation, and is inhibited by high ionic strength (>200mM). The abasic sites formed in DNA by UNG may be cleaved by heat, alkali-treatment or endonucleases that cleave specifically at abasic sites.
Inactivation
Inactivated by heating at 95°C for 10min. Enzyme activity is partially restored at temperatures lower than 55°C.
Unit Definition
1 Unit of the enzyme catalyzes the release of 1 nanomole of uracil-containing DNA template in 60 min at 37°C.
Specific Activity
The Specific Activity was found to be 5U/µl.

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.

Description:

Fucosyltransferase 5 Human Recombinant

FUT-5

Product # :

ENZ-1199

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Description

The FUT5 Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The FUT5 His-Tagged Fusion Protein produced in E. coli, is a 30kDa protein containing 172 amino acid residues of the FUT5 Human, 203-374 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Synonyms
FUT-5
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized FUT5 at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Background
Fucosyltransferase 5 also known as FUT5 is a glycosyltransferase which takes part in the biosynthesis of glycolipids and glycoproteins. FUT5 mainly catalyzes the transfer of fucose (a monosaccharide) to the type 2 chain of oligosaccharides (Galβ1-4GlcNAc). FUT5 takes an important part in various biological processes which include regulation of inflammation, cell-cell interactions and immune response modulation. FUT5 is expressed mainly in tissues such as the pancreas, liver and various immune cells.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Acyl-CoA Thioesterase 13 Human Recombinant

Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.

Product # :

ENZ-004

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Description

ACOT13 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids (1-140 a.a.) and having a molecular mass of 17.1kDa. The ACOT13 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ACOT13 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Acyl-coenzyme A thioesterase 13 (ACOT13) belongs to the thioesterase subfamily of esterase family. ACOT13 is highly expressed in the kidney with moderate expression in the brain, liver and intestines. ACOT13 contains a hotdog-fold and is thought to co-localize with microtubules, possibly having a role in cellular proliferation events. Deletion of a segment of the q arm of chromosome 6 is linked to early onset intestinal cancer, suggesting the presence of a cancer susceptibility locus.
Synonyms
Acyl-coenzyme A thioesterase 13, Acyl-CoA thioesterase 13, Thioesterase superfamily member 2, ACOT13, THEM2, HT012, MGC4961, PNAS-27, ACOT13.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTSMTQSLRE VIKAMTKARN FERVLGKITL VSAAPGKVIC EMKVEEEHTN AIGTLHGGLT ATLVDNISTM ALLCTERGAP GVSVDMNITY MSPAKLGEDI VITAHVLKQG KTLAFTSVDL TNKATGKLIA QGRHTKHLGN.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Alcohol Dehydrogenase 6 Human Recombinant

Alcohol dehydrogenase 6, ADH6, ADH-5.

Product # :

ENZ-619

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Description

ADH6 Human Recombinant produced E. coli is a single polypeptide chain containing 399 amino acids (1-375) and having a molecular mass of 42.4kDa.ADH6 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The ADH6 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Alcohol dehydrogenase 6 (ADH6) belongs to the alcohol dehydrogenase family. Alcohol dehydrogenase family members metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. ADH6 is expressed in the stomach as well as in the liver, and it contains a glucocorticoid response element upstream of its 5’ UTR, which is a steroid hormone receptor binding site.
Synonyms
Alcohol dehydrogenase 6, ADH6, ADH-5.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSTTGQ VIRCKAAILW KPGAPFSIEE VEVAPPKAKE VRIKVVATGL CGTEMKVLGS KHLDLLYPTI LGHEGAGIVE SIGEGVSTVK PGDKVITLFL PQCGECTSCL NSEGNFCIQF KQSKTQLMSD GTSRFTCKGK SIYHFGNTST FCEYTVIKEI SVAKIDAVAP LEKVCLISCG FSTGFGAAIN TAKVTPGSTC AVFGLGGVGL SVVMGCKAAG AARIIGVDVN KEKFKKAQEL GATECLNPQD LKKPIQEVLF DMTDAGIDFC FEAIGNLDVL AAALASCNES YGVCVVVGVL PASVQLKISG QLFFSGRSLK GSVFGGWKSR QHIPKLVADY MAEKLNLDPL ITHTLNLDKI NEAVELMKTG KCIRCILLL.

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.

Description:

Cysteine Conjugate-Beta Lyase Cytoplasmic Human Recombinant

Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.

Product # :

ENZ-878

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Description

CCBL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 445 amino acids (1-422 a.a) and having a molecular mass of 50.3kDa. CCBL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CCBL1 protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Cysteine Conjugate-Beta Lyase Cytoplasmic also known as CCBL1 is a member of the class-I pyridoxal-phosphate-dependent aminotransferase family. CCBL1 catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA) it also metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Furthermore, CCBL1 catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno) cysteine, resulting in the cleavage of the C-S or C-Se bond.
Synonyms
Cysteine Conjugate-Beta Lyase, Cytoplasmic, Glutamine Transaminase K, Cysteine Conjugate-Beta Lyase; Cytoplasmic (Glutamine Transaminase K, Kyneurenine Aminotransferase), Kynurenine--Oxoglutarate Transaminase I, Glutamine--Phenylpyruvate Transaminase, Cysteine-S-Conjugate Beta-Lyase, Kynurenine Aminotransferase I, Kyneurenine Aminotransferase, KATI, GTK, Glutamine-Phenylpyruvate Aminotransferase, Kynurenine--Oxoglutarate Transaminase 1, Beta-Lysase, Kidney, EC 4.4.1.13, EC 2.6.1.64, EC 2.6.1.7, KAT1, Kynurenine--oxoglutarate transaminase 1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKQLQA RRLDGIDYNP WVEFVKLASE HDVVNLGQGF PDFPPPDFAV EAFQHAVSGD FMLNQYTKTF GYPPLTKILA SFFGELLGQE IDPLRNVLVT VGGYGALFTA FQALVDEGDE VIIIEPFFDC YEPMTMMAGG RPVFVSLKPG PIQNGELGSS SNWQLDPMEL AGKFTSRTKA LVLNTPNNPL GKVFSREELE LVASLCQQHD VVCITDEVYQ WMVYDGHQHI SIASLPGMWE RTLTIGSAGK TFSATGWKVG WVLGPDHIMK HLRTVHQNSV FHCPTQSQAA VAESFEREQL LFRQPSSYFV QFPQAMQRCR DHMIRSLQSV GLKPIIPQGS YFLITDISDF KRKMPDLPGA VDEPYDRRFV KWMIKNKGLV AIPVSIFYSV PHQKHFDHYI RFCFVKDEAT LQAMDEKLRK WKVEL.

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.

Description:

Glutaminase 1 E.Coli Recombinant

Glutaminase 1, ybaS.

Product # :

ENZ-133

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Description

GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa. The GLSA1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GLSA1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.
Synonyms
Glutaminase 1, ybaS.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG

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.

Description:

Asparagine tRNA Synthetase Brugia Malayi Recombinant

Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.

Product # :

ENZ-941

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Description

AsnRS Brugia Malayi Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 568 amino acids (including a 6xHis Tag at N-terminus) and having a molecular mass of 64.5kDa.The AsnRS is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AsnRS 0.2µm filtered solution containing 20mM HEPES, pH7.4, 100mM NaCl, 5mM MgCl2, 5mM b-Mercaptoethanol and 10 % Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The AsnRS enzyme is a member of the ligases family, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. An asparagine-tRNA ligase is an enzyme which catalyzes the chemical reaction: ATP + L-asparagine + tRNAAsn AMP + diphosphate + L-asparaginyl-tRNAAsn. The three substrates of the AsnRS enzyme are ATP, L-asparagine, and tRNA(Asn), whereas its three products are AMP, diphosphate, and L-asparaginyl-tRNA(Asn).
Synonyms
Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22), Asparaginyl-tRNA synthetase, AsnRS, Potentially protective 63 kDa antigen.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTVYICPETG DDGNDGSELK PLRTLYQAMI ITKSSKGDFL IRTKKDGKQV WEAASKTALK KSWKRYEQEM LKNEKVAAKM LEKDATEVGV KAALEEAKKV QIELDTSLSY ITGVKIRDLV KHRNERVCIK GWIHRMRRQG KSLMFFILRD GTGFLQVLLM DKLCQTYDAL TVNTECTVEI YGAIKEVPEG KEAPNGHELI ADFWKIIGNA PSGGIDNVLN EEASVDKMLD NRHLVIRGEN AAALLRLRAA ATRAMREHFY NAGYVEVAPP TLVQTQVEGG STLFNLDYFG EQSFLTQSSQ LYLETCIPTL GDVFLHCSVL QGGKISHSST LAEYAHVEAE CPFITLDDLM EKIEELVCDT VDRLLADEEA KKLLEHINPK FQPPERPFLR MEYKDAIKWL QEHNVENEFG NTFTYGEDIA EAAERFMTDT INKPILLNRF PSEIKAFYMQ RDAKDNTLTE SVDLLMPGVG EIVGGSMRIW KFDELSKAFK NVEIDPKPYY WYLDQRLYGT CPHGGYGLGL ERFICWLTNT NHIRDVCLYP RFVGRCVP.

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.

Description:

Membrane Metalloendopeptidase Human Recombinant, Active

Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.

Product # :

ENZ-1116

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Description

MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.

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Introduction
Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.
Synonyms
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH

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.

Description:

Hydroxysteroid (17-beta) Dehydrogenase 8 Human Recombinant

E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.

Product # :

ENZ-108

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Description

HSD17B8 Human Recombinant 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 29.1kDa.HSD17B8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

HSD17B8 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 150mM NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
E2 17-beta-dehydrogenase 8 (HSD17B8) is a member of the short-chain dehydrogenases/reductases (SDR) family. In mice, the HSD17B8 protein is a 17-beta-hydroxysteroid dehydrogenase which can regulate the concentration of biologically active estrogens and androgens. HSD17B8 is preferentially an oxidative enzyme and inactivates E2, testosterone, and DHT. However, the HSD17B8 enzyme has some reductive activity and can synthesize E2 from E1. HSD17B8 may have a role in biosynthesis of fatty acids in mitochondria.
Synonyms
E2 17-beta-dehydrogenase 8, 17-beta-hydroxysteroid dehydrogenase 8, 17-beta-HSD 8, 3-oxoacyl-[acyl-carrier-protein] reductase, Protein Ke6, Ke-6, Really interesting new gene 2 protein, Testosterone 17-beta-dehydrogenase 8, HSD17B8, FABGL, HKE6, RING2, KE6, FABG, H2-KE6, SDR30C1, D6S2245E, dJ1033B10.9.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MASQLQNRLR SALALVTGAG SGIGRAVSVR LAGEGATVAA CDLDRAAAQE TVRLLGGPGS KEGPPRGNHA AFQADVSEAR AARCLLEQVQ ACFSRPPSVV VSCAGITQDE FLLHMSEDDW DKVIAVNLKG TFLVTQAAAQ ALVSNGCRGS IINISSIVGK VGNVGQTNYA ASKAGVIGLT QTAARELGRH GIRCNSVLPG FIATPMTQKV PQKVVDKITE MIPMGHLGDP EDVADVVAFL ASEDSGYITG TSVEVTGGLF M.

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.

Description:

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-735

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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.

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

Description:

ElaC Ribonuclease Z 1 Human Recombinant

ElaC Ribonuclease Z 1, D29, ElaC Homolog Protein 1, TRNA 3 Endonuclease 1, TRNA Z (Short Form), Ribonuclease Z 1, Deleted In Ma29, EC 3.1.26.11, TRNase Z 1, RNaseZ(S), RNase Z 1, Zinc Phosphodiesterase ELAC Protein 1, TRNA 3 Processing Endoribonuclease, ElaC (E. Coli) Homolog 1, ElaC Homolog 1 (E. Coli), ElaC Homolog 1, TRNase ZS, ELAC1.

Product # :

ENZ-883

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Description

ELAC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a) and having a molecular mass of 42.4 kDa.ELAC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ELAC1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
ElaC Ribonuclease Z 1, also known as ELAC1 is a member of the RNase Z family. Zinc phosphodiesterase, which shows some tRNA 3'-processing endonuclease activity. In addition, ELAC1 is implicated in tRNA maturation, by removing a 3'-trailer from precursor tRNA.
Synonyms
ElaC Ribonuclease Z 1, D29, ElaC Homolog Protein 1, TRNA 3 Endonuclease 1, TRNA Z (Short Form), Ribonuclease Z 1, Deleted In Ma29, EC 3.1.26.11, TRNase Z 1, RNaseZ(S), RNase Z 1, Zinc Phosphodiesterase ELAC Protein 1, TRNA 3 Processing Endoribonuclease, ElaC (E. Coli) Homolog 1, ElaC Homolog 1 (E. Coli), ElaC Homolog 1, TRNase ZS, ELAC1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSMDVTF LGTGAAYPSP TRGASAVVLR CEGECWLFDC GEGTQTQLMK SQLKAGRITK IFITHLHGDH FFGLPGLLCT ISLQSGSMVS KQPIEIYGPV GLRDFIWRTM ELSHTELVFH YVVHELVPTA DQCPAEELKE FAHVNRADSP PKEEQGRTIL LDSEENSYLL FDDEQFVVKA FRLFHRIPSF GFSVVEKKRP GKLNAQKLKD LGVPPGPAYG KLKNGISVVL ENGVTISPQD VLKKPIVGRK ICILGDCSGV VGDGGVKLCF EADLLIHEAT LDDAQMDKAK EHGHSTPQMA ATFAKLCRAK RLVLTHFSQR YKPVALAREG ETDGIAELKK QAESVLDLQE VTLAEDFMVI SIPIKK

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.

Description:

Sorbitol Dehydrogenase Human Recombinant

EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH

Product # :

ENZ-1151

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Description

SORD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 357 amino acids (1-357a.a.) and having a molecular mass of 38.3kDa.SORD is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SORD solution (0.5mg/ml) contains 10% glycerol, 20mM Tris-HCl buffer (pH 8.5) and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity > 15unit/mg. Defined by the amount of enzyme that catalyze the reduction 1.0 umole of D-fructose to D-sorbitol per minute at pH 7.5 at 37˚C.

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Introduction
SORD, also referred to as sorbitol dehydrogenase, belongs to the zinc-containing alcohol dehydrogenase family. It is widely produced. The lens of the eyeand the kidney are the protein highest production areas. Zinc-dependent interconversion of polyols, like sorbitol and xylitol, are enzymatically catalysed to their respective ketoses by SORD.
Synonyms
EC 1.1.1.14, SORD1, SORD, L-iditol 2-dehydrogenase, DHSO, Sorbitol Dehydrogenase,
SDH, (R,R)-butanediol dehydrogenase, L-iditol 2-dehydrogenase, Polyol dehydrogenase, Ribitol dehydrogenase, RDH, Xylitol dehydrogenase, XDH
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MAAAAKPNNL SLVVHGPGDL RLENYPIPEP GPNEVLLRMH SVGICGSDVH YWEYGRIGNF IVKKPMVLGH EASGTVEKVG SSVKHLKPGD RVAIEPGAPR ENDEFCKMGR YNLSPSIFFC ATPPDDGNLC RFYKHNAAFC YKLPDNVTFE EGALIEPLSV GIHACRRGGV TLGHKVLVCG AGPIGMVTLL VAKAMGAAQV VVTDLSATRL SKAKEIGADL VLQISKESPQ EIARKVEGQL GCKPEVTIEC TGAEASIQAG IYATRSGGTL VLVGLGSEMT TVPLLHAAIR EVDIKGVFRY CNTWPVAISM LASKSVNVKP LVTHRFPLEK ALEAFETFKK GLGLKIMLKC DPSDQNP

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.

Description:

Fructose-1,6-Bisphosphatase 1, BioActive Human Recombinant

Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.

Product # :

ENZ-1145

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Description

FBP1 Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 358 amino acids (1-338) and having a molecular mass of 39.0 kDa.FBP1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FBP1 protein solution (1mg/ml) contains 1mM DTT, 10% glycerol and 20mM Tris-HCl buffer (pH 8.0).

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 7,000pmol/min/ug, and is determined by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. 1 unit oxidizes 1.0pmole of fructose 1,6 diphosphate to fructose 6- phosphate and inorganic phosphate per minute at pH 9.5 at 37˚C.

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Introduction
FBP1 or Fructose-1, 6-bisphosphatase 1 is an enzyme, catalyzing the formation of fructose 6-phosphate & inorganic phosphate from fructose 1, 6-bisphosphate. FBP1 is part of the gluconeogenesis regulatory enzymes. Mutations in the enzyme gene can result in metabolic acidosis & hypoglycemia.
Synonyms
Fructose-1,6-bisphosphatase 1, FBPase 1, D-fructose-1,6-bisphosphate 1-phosphohydrolase 1, Liver FBPase, FBP1, FBP.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH 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.

Description:

Tissue Plasminogen Activator Human Recombinant, Sf9

Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.

Product # :

ENZ-1011

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Description

tPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 545 amino acids (24-562 a.a) and having a molecular mass of 61.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).tPA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

tPA protein solution (0.25mg/ml) containing 50mM MES buffer(pH 5.5 ), 40% glycerol, 5mM CaCl2, 1mM DTT and 0.5M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism.
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
QEIHARFRRG ARSYQVICRD EKTQMIYQQH QSWLRPVLRS NRVEYCWCNS GRAQCHSVPV KSCSEPRCFN GGTCQQALYF SDFVCQCPEG FAGKCCEIDT RATCYEDQGI SYRGTWSTAE SGAECTNWNS SALAQKPYSG RRPDAIRLGL GNHNYCRNPD RDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGSAY RGTHSLTESG ASCLPWNSMI LIGKVYTAQN PSAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF PPHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSRCAQES SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP GVYTKVTNYL DWIRDNMRPHHHHHH.

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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