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1000 results found for “epimerase”
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Name :
Treponema TmpA 45kDaDescription:
Treponema pallidum TmpA, 45kDa Recombinant
Product # :
TRP-251Price :
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Shipped at Room temp
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Description
Recombinant Treponema TmpA produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 45kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-10.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Treponema pallidum is a gram-negative spirochaete bacterium and is considered to be metabolically crippled. There are at least four known subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum and T. pallidum endemicum. The helical structure of T. pallidum pallidum allows it to move in a corkscrew motion through viscous mediums such as mucus. Treponema pallidum sub sp. pallidum has one of the smallest bacterial genomes at 1.14 million base pairs (Mb) and has limited metabolic capabilities, reflecting its adaptation through genome reduction to the rich environment of mammalian tissue.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Treponema TmpA although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Treponema TmpA in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
GLK E.Coli, ActiveDescription:
Glucokinase E.coli Recombinant, BioActive
Glucokinase, ECK2384, JW2385.
Product # :
PKA-121Price :
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Description
GLK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (1-321) and having a molecular mass of 37.1kDa.GLK is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GLK protein solution (1mg/ml) contains 0.15M NaCl, 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 70unit/mg obtained by measuring the increase of NADPH in absorbance at 340 nm resulting from the reduction of NADP. One unit will oxidize 1.0 umole of Glucose to D-glucose 6-phosphate per minute in the presence of Beta-NADP at pH 9.0 at 37C.
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Introduction
Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.
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Synonyms
Glucokinase, ECK2384, JW2385.
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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 MGSMTKYALV GDVGGTNARL ALCDIASGEI SQAKTYSGLD YPSLEAVIRV YLEEHKVEVK DGCIAIACPI TGDWVAMTNH TWAFSIAEMK KNLGFSHLEI INDFTAVSMA IPMLKKEHLI QFGGAEPVEG KPIAVYGAGT GLGVAHLVHV DKRWVSLPGE GGHVDFAPNS EEEAIILEIL RAEIGHVSAE RVLSGPGLVN LYRAIVKADN RLPENLKPKD ITERALADSC TDCRRALSLF CVIMGRFGGN LALNLGTFGG VFIAGGIVPR FLEFFKASGF RAAFEDKGRF KEYVHDIPVY LIVHDNPGLL GSGAHLRQTL GHIL
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 :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT should be stored at 4°C between 2-7 days and for future use below -18°C.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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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
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 :
LYPLAL1 HumanDescription:
Lysophospholipase Like I Human Recombinant
Lysophospholipase-like protein 1, LYPLAL1.
Product # :
ENZ-644Price :
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Shipped with Ice Packs
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Description
LYPLAL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.9kDa.LYPLAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The LYPLAL1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Lysophospholipase-like protein 1 (LYPLAL1) is a member of the AB hydrolase 2 family. LYPLAL1 doesn’t exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates as a result of its shallow active site.
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Synonyms
Lysophospholipase-like protein 1, LYPLAL1.
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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 MGSHMAAASG SVLQRCIVSP AGRHSASLIF LHGSGDSGQG LRMWIKQVLN QDLTFQHIKI IYPTAPPRSY TPMKGGISNV WFDRFKITND CPEHLESIDV MCQVLTDLID EEVKSGIKKN RILIGGFSMG GCMAMHLAYR NHQDVAGVFA LSSFLNKASA VYQALQKSNG VLPELFQCHG TADELVLHSW AEETNSMLKS LGVTTKFHSF PNVYHELSKT ELDILKLWIL TKLPGEMEKQ K.
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 :
ACAT2 HumanDescription:
Acetyl-Coenzyme A acetyltransferase 2 Human Recombinant
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
Product # :
ENZ-295Price :
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Description
ACAT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 433 amino acids (1-397 a.a.) and having a molecular mass of 45.4 kDa. The ACAT2 is fused to 36 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ACAT2 Human solution containing 20mM Tris pH-8, 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ACAT2 enzyme participates in lipid metabolism. ACAT2 takes part in lipoprotein assembly, catalyzing cholesterol esterification in mammalian cells. ACAT2 is an integral membrane protein that localizes to the endoplasmic reticulum of human intestinal cells. ACAT2 deficiency contributes to severe mental retardation and hypotonus.
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Synonyms
Acetyl-CoA acetyltransferase cytosolic, Cytosolic acetoacetyl-CoA thiolase, ACAT2, Acetyl CoA transferase-like protein, ACAT-2.
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Physical Appearance
Sterile Filtered clear solution.
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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 KDRWGSMNAG SDPVVIVSAA RTIIGSFNGA LAAVPVQDLG STVIKEVLKR ATVAPEDVSE
VIFGHVLAAG CGQNPVRQAS VGAGIPYSVP AWSCQMICGS GLKAVCLAVQ SIGIGDSSIV VAGGMENMSK APHLAYLRTG VKIGEMPLTD SILCDGLTDA FHNCHMGITA ENVAKKWQVS REDQDKVAVL SQNRTENAQK AGHFDKEIVP VLVSTRKGLI EVKTDEFPRH GSNIEAMSKL KPYFLTDGTG TVTPANASGI NDGAAAVVLM KKSEADKRGL TPLARIVSWS QVGVEPSIMG IGPIPAIKQA VTKAGWSLED VDIFEINEAF AAVSAAIVKE LGLNPEKVNI EGGAIALGHP LGASGCRILV TLLHTLERMG RSRGVAALCI GGGMGIAMCV QR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ACY1 HumanDescription:
Aminoacylase-1 Human Recombinant
N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.
Product # :
ENZ-296Price :
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Description
ACY1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-408 a.a.) and having a molecular mass of 48kDa. The ACY1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACY1 solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and ACY1 is the first member of a new family of zinc-binding enzymes.
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Synonyms
N-acyl-L-amino-acid amidohydrolase, ACY-1, ACY1D, ACYLASE, ACY1,EC 3.5.1.143.
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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 MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCVSIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ
RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMNLTLEP EIMPAATDNR YIRAVGVPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSDS.
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 :
GOT2 Human, ActiveDescription:
Glutamic-Oxaloacetic Transaminase 2 Human Recombinant, Active
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
Product # :
ENZ-998Price :
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Shipped with Ice Packs
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Description
GOT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 60 units/mg, and is defined as the amount of enzyme that convert 1umole of α-ketoglutarate to L-Glutamate per minute at pH 8.0 at 25C.More Info
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Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.
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Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
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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 MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.
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 :
B3GNT2 HumanDescription:
Beta-1,3-N-Acetylglucosaminyltransferase 2 Human Recombinant
B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.
Product # :
ENZ-973Price :
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Description
B3GNT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 375 amino acids (29-397a.a.) and having a molecular mass of 43.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). B3GNT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
B3GNT2 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Beta-1,3-N-Acetylglucosaminyltransferase 2 (B3GNT2) is a part of the beta-1,3-N-acetylglucosaminyltransferase family which takes part in the synthesis of poly-N-acetyllactosamine. B3GNT2 is a type II transmembrane protein which prefers the substrate of lacto-N-neotetraose. B3GNT2 catalyzes the initiation and elongation of poly-N-acetyllactosamine chains and comprises the main polylactosamine synthase.
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Synonyms
B3GNT2, B3GN-T2, B3GNT, B3GNT-2, B3GNT1, BETA3GNT, BGnT-2, BGNT2, N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2, Beta-1,3-N-acetylglucosaminyltransferase 1, BGnT-1, Beta-1,3-Gn-T1, Beta3Gn-T1, Beta-1,3-galactosyltransferase 7, Beta-1,3-GalTase 7, Beta3Gal-T7, Beta3GalT7, b3Gal-T7, Beta-3-Gx-T7, beta-GlcNAc beta-1,3-galactosyltransferase 7, betaGal beta-1,3-N-acetylglucosaminyltransferase 2, BGnT-2, Beta-1,3-Gn-T2, Beta-1,3-N-acetylglucosaminyltransferase 2, Beta3Gn-T2, beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7.
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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
ADPKSSSQEK NGKGEVIIPK EKFWKISTPP EAYWNREQEK LNRQYNPILS MLTNQTGEAG RLSNISHLNY CEPDLRVTSV VTGFNNLPDR FKDFLLYLRC RNYSLLIDQP DKCAKKPFLL LAIKSLTPHF ARRQAIRESW GQESNAGNQT VVRVFLLGQT PPEDNHPDLS DMLKFESEKH QDILMWNYRD TFFNLSLKEV LFLRWVSTSC PDTEFVFKGD DDVFVNTHHI LNYLNSLSKT KAKDLFIGDV IHNAGPHRDK KLKYYIPEVV YSGLYPPYAG GGGFLYSGHL ALRLYHITDQ VHLYPIDDVY TGMCLQKLGL VPEKHKGFRT FDIEEKNKNN ICSYVDLMLV HSRKPQEMID IWSQLQSAHL KCHHHHHH.
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 :
GPI AntibodyDescription:
Glucose-6-Phosphate Isomerase, Mouse Anti Human
Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.
Product # :
ANT-613Price :
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Shipped with Ice Packs
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Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a neurotrophic factor for spinal and sensory neurons.
Defects in the GPI gene cause the nonspherocytic hemolytic anemia and a severe enzyme deficiency can be linked to hydrops fetalis, immediate neonatal death and neurological impairment.
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Synonyms
Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human GPI mAb, clone PAT22G2AT, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human GPI protein 1-558 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG2a heavy chain and k light chain.
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Clone
PAT22G2AT.
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Applications
The antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
GPI antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
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 :
CYB5R2 HumanDescription:
Cytochrome B5 Reductase 2 Human Recombinant
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.
Product # :
ENZ-799Price :
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Description
CYB5R2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a.) and having a molecular mass of 33.8kDa. CYB5R2 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
CYB5R2 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Cytochrome b5 reductase 2 (CYB5R2) is involved in desaturation and elongation of fatty acids, cholesterol biosynthesis, drug metabolism, and, in erythrocyte, methemoglobin reduction. CYB5R2 is responsible for NADH-dependent lucigenin chemiluminescence in spermatozoa by reducing both lucigenin and 2-[4-iodophenyl]-3-[4-nitrophenyl]-5-[2,4-disulfophenyl]-2H tetrazolium monosodium salt (WST-1).
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Synonyms
CYB5R2, Cytochrome B5 Reductase 2, EC 1.6.2.2, B5R.2, Cytochrome B5 Reductase B5R.2, NADH-Cytochrome B5 Reductase 2, b5R.2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNSRRRE PITLQDPEAK YPLPLIEKEK ISHNTRRFRF GLPSPDHVLG LPVGNYVQLL AKIDNELVVR AYTPVSSDDD RGFVDLIIKI YFKNVHPQYP EGGKMTQYLE NMKIGETIFF RGPRGRLFYH GPGNLGIRPD QTSEPKKTLA DHLGMIAGGT GITPMLQLIR HITKDPSDRT RMSLIFANQT EEDILVRKEL EEIARTHPDQ FNLWYTLDRP PIGWKYSSGF VTADMIKEHL PPPAKSTLIL VCGPPPLIQT AAHPNLEKLG YTQDMIFTY.
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 :
PGD HumanDescription:
Phosphogluconate Dehydrogenase Human Recombinant
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
Product # :
ENZ-501Price :
Quantity :
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Shipped with Ice Packs
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Description
PGD Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 503 amino acids (1-483 a.a.) and having a molecular mass of 55.3 kDa. The PGD is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PGD solution contains 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
6PGD is the second dehydrogenase in the pentose phosphate shunt. Pentose is neccesary for nucleic acid biosynthesis. The pentose phosphate cycle is a major source of NADPH 6PGD deficiency is usually asymptomatic, and the inheritance of this disorder is autosomal dominant. PGD deficiency raises the erythrocyte pyruvate kinase levels of activity and decreases glutathione synthetase, resulting in hemolysis.
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Synonyms
EC 1.1.1.44, 6PGD, PGDH, 6-phosphogluconate dehydrogenase decarboxylating, PGD.
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Physical Appearance
Sterile Filtered clear colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAQADIALIG LAVMGQNLIL NMNDHGFVVC AFNRTVSKVD DFLANEAKGT KVVGAQSLKE MVSKLKKPRR IILLVKAGQA VDDFIEKLVP LLDTGDIIID GGNSEYRDTT RRCRDLKAKG ILFVGSGVSG GEEGARYGPS LMPGGNKEAW PHIKTIFQGI AAKVGTGEPC CDWVGDEGAG HFVKMVHNGI EYGDMQLICE AYHLMKDVLG MAQDEMAQAF EDWNKTELDS FLIEITANIL KFQDTDGKHL LPKIRDSAGQ KGTGKWTAIS ALEYGVPVTL IGEAVFARCL SSLKDERIQA SKKLKGPQKF QFDGDKKSFL EDIRKALYAS KIISYAQGFM LLRQAATEFG WTLNYGGIAL MWRGGCIIRS VFLGKIKDAF DRNPELQNLL LDDFFKSAVE NCQDSWRRAV STGVQAGIPM PCFTTALSFY DGYRHEMLPA SLIQAQRDYF GAHTYELLAK PGQFIHTNWT GHGGTVSSSS YNA.
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 :
GGCT HumanDescription:
Gamma-Glutamylcyclotransferase Human Recombinant
Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.
Product # :
ENZ-062Price :
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Description
GGCT produced in E.Coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (1-188a.a.) and having a molecular mass of 23.2kDa.GGCT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GGCT protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
GGCT is a member of the family of transferases, specifically the aminoacyltransferases. GGCT protein catalyzes the formation of 5-oxoproline from gamma-glutamyl dipeptides and takes an important part in glutathione homeostasis. GGCT induces release of cytochrome c from mitochondria with resultant induction of apoptosis.
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Synonyms
Gamma-Glutamylcyclotransferase, CRF21, C7orf24, MGC3077, Cytochrome c-releasing factor 21, GCTG, Ggc, Chromosome 7 open reading frame 24, FLJ11717, EC 2.3.2.4.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSHMANSGCKDVT GPDEESFLYF AYGSNLLTER IHLRNPSAAF FCVARLQDFK LDFGNSQGKT SQTWHGGIAT IFQSPGDEVW GVVWKMNKSN LNSLDEQEGV KSGMYVVIEV KVATQEGKEI TCRSYLMTNY ESAPPSPQYK KIICMGAKEN GLPLEYQEKL KAIEPNDYTG KVSEEIEDII KKGETQTL
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 :
CTRB1 HumanDescription:
Chymotrypsinogen-B1, Human Recombinant
Product # :
ENZ-1016Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human CTRB1 expressed in E.coli containing 245 amino acids having a Mw of 27kDa is purified by standard chromatography techniques.
Source
E.coli
Formulation
The Human CTRB1 was lyophilized without any additives.
Purity
Greater than 95% as determined by HPLC.
Biological Activity
1100 units/mg protein.
One unit is defined as the amount of enzyme that will hydrolyze 1.0 μmole of N-alpha-acetyl-L-tyrosine ethyl ester (ATEE) per min at pH 7.0 at 25°C.More Info
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Introduction
Chymotrypsinogen-B1 (CTRB1) belongs to the serine protease family of enzymes and forms a main precursor of the pancreatic proteolytic enzymes. CTRB1 is located next to a related chymotrypsinogen gene. CTRB1 is a protein coding gene which encodes different isoforms which may undergo similar processing to generate the mature protein.
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Physical Appearance
Sterile Filtered lyophilized powder.
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Stability
Recombinant Human CTRB1 although stable at room temp for 1 week, should be stored desiccated below -18°C. 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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Solubility
It is recommended to reconstitute the lyophilized Human CTRB1 in 1ml 50mM HAc which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
CG VPAIHPVLSG LSRIVNGEDA VPGSWPWQVS LQDKTGFHFC GGSLISEDWV VTAAHCGVRT SDVVVAGEFD QGSDEENIQV LKIAKVFKNP KFSILTVNND ITLLKLATPA RFSQTVSAVC LPSADDDFPAGTLCATTGWG KTKYNANKTP DKLQQAALPL LSNAECKKSW GRRITDVMIC AGASGVSSCM GDSGGPLVCQ KDGAWTLVGI VSWGSDTCST SSPGVYARVTKLIPWVQKIL AAN.
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 :
PDIA3 HumanDescription:
Protein Disulfide Isomerase A3 Human Recombinant
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
Product # :
ENZ-474Price :
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Description
PDIA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 518 amino acids (25-505 a.a.) and having a molecular wieght of 58.5 kDa. The PDIA3 is fused to 37 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDIA3 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PDIA3 is an enzyme that belongs to the endoplasmic reticulum and interacts with lectin chaperones calreticulin and calnexin to modulate folding of newly synthesized glycoproteins. PDIA3 has protein disulfide isomerase activity. Complexes of lectins and PDIA3 mediate protein folding by promoting formation of disulfide bonds in their glycoprotein substrates. PDIA3 is expressed in the lumbar spinal cord from rats submitted to peripheral lesion during neonatal period. PDIA3 interacts with thiazide-sensitive sodium-chloride cotransporter in the kidney and is induced by glucose deprivation. PDIA3 is part of the major histocompatibility complex (MHC) class I peptide-loading complex (TAP1), which is important for formation of the final antigen conformation and export from the endoplasmic reticulum to the cell surface.
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Synonyms
ERp57, ERp60, ERp61, GRP57, GRP58, HsT17083, P58, PI-PLC, ER60, Protein disulfide-isomerase A3, Disulfide isomerase ER-60, Endoplasmic reticulum resident protein 60, ER protein 60, 58 kDa microsomal protein, Endoplasmic reticulum resident protein 57, ER protein 57, 58 kDa glucose-regulated protein, PDIA3.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMSDV LELTDDNFES RISDTGSAGL MLVEFFAPWC GHCKRLAPEY EAAATRLKGI VPLAKVDCTA NTNTCNKYGV SGYPTLKIFR DGEEAGAYDG PRTADGIVSH LKKQAGPASV PLRTEEEFKK FISDKDASIV GFFDDSFSEA HSEFLKAASN LRDNYRFAHT NVESLVNEYD DNGEGIILFR PSHLTNKFED KTVAYTEQKM TSGKIKKFIQ ENIFGICPHM TEDNKDLIQG KDLLIAYYDV DYEKNAKGSN YWRNRVMMVA KKFLDAGHKL NFAVASRKTF SHELSDFGLE STAGEIPVVA IRTAKGEKFV MQEEFSRDGK ALERFLQDYF DGNLKRYLKS EPIPESNDGP VKVVVAENFD EIVNNENKDV LIEFYAPWCG HCKNLEPKYK ELGEKLSKDP NIVIAKMDAT ANDVPSPYEV RGFPTIYFSP ANKKLNPKKY EGGRELSDFI SYLQREATNP PVIQEEKPKK KKKAQEDL.
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 :
AKR1C4 Human, HisDescription:
Aldo-Keto Reductase Family 1 Member C4 Human Recombinant, His Tag
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
Product # :
ENZ-145Price :
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Shipped with Ice Packs
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Description
AKR1C4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323) and having a molecular mass of 39.2 kDa.The AKR1C4 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AKR1C4 protein 1mg/ml is supplied in 20mM Tris-HCl, pH-8, 0.1M NaCl, 1mM DTT and 20% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 700 pmol/min/ug, and is defined as the amount of enzyme that catalyze the oxidation of 1.0 pmole 1-Acenaphthenol in the presence of NADP per minute at pH 8.8 at 25°C.More Info
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Introduction
AKR1C4 is a member of the aldo/keto reductase superfamily that has over 40 known enzymes and proteins. AKR1C4 enables the conversion of aldehydes and ketones to their corresponding alcohols by using NADH and/or NADPH as cofactors. AKR1C4 takes part in the bioreduction of chlordecone, a toxic organochlorine pesticide, to chlordecone alcohol in liver.
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Synonyms
Aldo-keto reductase family 1 member C4 (chlordecone reductase 3-alpha hydroxysteroid dehydrogenase type I dihydrodiol dehydrogenase 4), 3-alpha-hydroxysteroid dehydrogenase type I, MGC22581, HAKRA, 3 alpha-hydroxysteroid dehydrogenase/dihydrodiol dehydrogenase 4, CDR, DD4, CHDR, 3-alpha-HSD1, C11.
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Physical Appearance
AKR1C4 is supplied as a sterile filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDPKYQRVEL NDGHFMPVLG FGTYAPPEVP RNRAVEVTKL AIEAGFRHID SAYLYNNEEQ VGLAIRSKIA DGSVKREDIF YTSKLWCTFF QPQMVQPALE SSLKKLQLDY VDLYLLHFPM ALKPGETPLP KDENGKVIFD TVDLSATWEV MEKCKDAGLA
KSIGVSNFNC RQLEMILNKP GLKYKPVCNQ VECHPYLNQS KLLDFCKSKD IVLVAHSALG TQRHKLWVDP NSPVLLEDPV LCALAKKHKR TPALIALRYQ LQRGVVVLAK SYNEQRIREN IQVFEFQLTS EDMKVLDGLN RNYRYVVMDF LMDHPDYPFS DEY.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TPST2 Human, sf9Description:
Tyrosylprotein Sulfotransferase 2, sf9 Human Recombinant
Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.
Product # :
ENZ-949Price :
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Description
TPST2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 361 amino acids (26-377 a.a.) and having a molecular mass of 40.4kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). TPST2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
TPST2 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Tyrosylprotein Sulfotransferase 2 (TPST2) is a member of the protein sulfotransferase family. TPST2 is a widely expressed protein, which catalyzes the O-sulfation of tyrosine residues within acidic regions of proteins. The TPST2 protein is a type II integral membrane protein located in the Golgi body.
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Synonyms
Tyrosylprotein Sulfotransferase 2, EC 2.8.2.20, TPST-2, Transport And Golgi Organization 13 Homolog B (Drosophila), Transport And Golgi Organization 13 Homolog B, Protein-Tyrosine Sulfotransferase 2, Tyrosylprotein Phosphotransferase 2, Tyrosylprotein Sulfotransferase-2, TANGO13B.
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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
ADPQQVLECR AVLAGLRSPR GAMRPEQEEL VMVGTNHVEY RYGKAMPLIF VGGVPRSGTT LMRAMLDAHP EVRCGEETRI IPRVLAMRQA WSKSGREKLR LDEAGVTDEV LDAAMQAFIL EVIAKHGEPA RVLCNKDPFT LKSSVYLSRL FPNSKFLLMV RDGRASVHSM ITRKVTIAGF DLSSYRDCLT KWNKAIEVMY AQCMEVGKEK CLPVYYEQLV LHPRRSLKLI LDFLGIAWSD AVLHHEDLIG KPGGVSLSKI ERSTDQVIKP VNLEALSKWT GHIPGDVVRD MAQIAPMLAQ LGYDPYANPP NYGNPDPFVI NNTQRVLKGD YKTPANLKGY FQVNQNSTSS HLGSSHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PDCD6IP HumanDescription:
Programmed Cell Death 6 Interacting Protein Human Recombinant
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
Product # :
PRO-792Price :
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Description
PDCD6IP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 412 amino acids (1-392 a.a.) and having a molecular mass of 45.8 kDa. The PDCD6IP is fused to a 20 amino acid His-tag at N-terminus and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PDCD6IP is a Class E VPS protein which participates in concentration and sorting of cargo proteins of the multivesicular body or incorporation into intralumenal vesicles that are generated by invagination and scission from the limiting membrane of the endosome. PDCD6IP binds to the phospholipid lysobisphosphatidic acid which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. PDCD6IP is an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. PDCD6IP is mandatory for completion of cytokinesis. PDCD6IP takes part in HIV-1 virus budding. PDCD6IP replaces TSG101 in its function of supporting HIV-1 release. PDCD6IP takes part in the regulation of both apoptosis and cell proliferation. PDCD6IP is a cytoplasmic protein that cooperates with apoptosis-associated proteins (ALG-2 and PDCD6) and with the endocytosis-regulator CIN85. Overexpression of PDCD6IP and endophilin
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Synonyms
AIP1, Alix, PDCD6-Interacting Protein, DRIP4, ALG-2 interacting protein 1, Programmed cell death 6-interacting protein, Hp95, PDCD6IP, KIAA1375, MGC17003.
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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 MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LA.
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 :
Flavokinase HumanDescription:
Riboflavin Kinase Human Recombinant
Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.
Product # :
PKA-352Price :
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Description
Flavokinase Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids (1-162 a.a.) and having a molecular mass of 20.5kDa. Flavokinase is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Flavokinase solution containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Flavokinase is a transferases family member, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. Flavokinase is an enzyme that catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), which is an obligatory step in vitamin B2 utilization and flavin cofactor synthesis. It has been proposed that TNF, through the activation of the RFK gene, enhances the incorporation of FAD in NADPH oxidase enzymes, which is a critical step for the assembly and activation of NADPH oxidase.
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Synonyms
Riboflavin kinase, ATP:riboflavin 5'-phosphotransferase, Flavokinase, RFK, RIFK, FLJ11149, RP11-422N19.2.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Flavokinase although stable at 4°C for 1 week, should be stored below -18°C. 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 MPRADCIMRH LPYFCRGQVV RGFGRGSKQL GIPTANFPEQ VVDNLPADIS TGIYYGWASV GSGDVHKMVV SIGWNPYYKN TKKSMETHIM HTFKEDFYGE ILNVAIVGYL RPEKNFDSLE SLISAIQGDI EEAKKRLELP EHLKIKEDNF FQVSKSKIMNGH.
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 :
MMP14 Human, HisDescription:
Matrix Metalloproteinase-14 Human Recombinant, His Tag
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 1.
Product # :
ENZ-1003Price :
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Description
MMP14 Human Recombinant produced in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 527 amino acids (21-538a.a) and having a molecular mass of 59.9kDa (Molecular size on SDS-PAGE will appear at approximately 35-70kDa). MMP14 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
MMP14 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Matrix metalloproteinase-14 (MMP14), is a membrane-anchored zinc-binding endopeptidase which is expressed at the leading edge of different invasive carcinomas and also promotes tumor cell invasion through degradation of the extracellular matrix. MMP14 takes a vital part in extracellular matrix, ECM, remodeling by having the capability to degrade type I collagen, activate pro-MMP-2 and process cell adhesion molecules for instance CD44 and integrin alpha V. MMP14 is a key enzyme in many physiological as well as pathological processes for example angiogenesis & tumor invasion.
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Synonyms
Matrix Metallopeptidase 14, Matrix Metallopeptidase 14 (Membrane-Inserted), Membrane-Type-1 Matrix Metalloproteinase, Membrane Type 1 Metalloprotease, EC 3.4.24.80, MT-MMP 1, MT1-MMP, MMP-14, MMP-X1, MT1MMP, MTMMP1, Matrix Metalloproteinase 14 (Membrane-Inserted), Membrane-Type Matrix Metalloproteinase 1, Matrix Metalloproteinase-14, EC 3.4.24, MT-MMP, WNCHRS, Matrix metalloproteinase-14, Membrane-type matrix metalloproteinase 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
ADLALASLGS AQSSSFSPEA WLQQYGYLPP GDLRTHTQRS PQSLSAAIAA MQKFYGLQVT GKADADTMKA MRRPRCGVPD KFGAEIKANV RRKRYAIQGL KWQHNEITFC IQNYTPKVGE YATYEAIRKA FRVWESATPL RFREVPYAYI REGHEKQADI MIFFAEGFHG DSTPFDGEGG FLAHAYFPGP NIGGDTHFDS AEPWTVRNED LNGNDIFLVA VHELGHALGL EHSSDPSAIM APFYQWMDTE NFVLPDDDRR GIQQLYGGES GFPTKMPPQP RTTSRPSVPD KPKNPTYGPN ICDGNFDTVA MLRGEMFVFK ERWFWRVRNN QVMDGYPMPI GQFWRGLPAS INTAYERKDG KFVFFKGDKH WVFDEASLEP GYPKHIKELG RGLPTDKIDA ALFWMPNGKT YFFRGNKYYR FNEELRAVDS EYPKNIKVWE GIPESPRGSF MGSDEVFTYF YKGNKYWKFN NQKLKVEPGY PKSALRDWMG CPSGGRPDEG TEEETEVIII EVDEEGGGAV SHHHHHH.
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 :
GALNT1 HumanDescription:
Polypeptide N-Acetylgalactosaminyltransferase 1 Human Recombinant
Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1
Product # :
enz-1098Price :
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Description
GALNT1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 528 amino acids (41-559a.a.) and having a molecular mass of 60.4kDa.GALNT1 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GALNT1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The specific activity which is defined as the amount of enzyme that transfer 1.0 pmole of GalNAc from UDP-GalNAc to peptide EA2 per minute at pH 8.0 at 37C is > 300 pmol/min/ug.
More Info
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Introduction
Polypeptide N-Acetylgalactosaminyltransferase 1 (Galnt1) is a part of the UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes. The initial reaction in O-linked oligosaccharide biosynthesis is catalyzed by Glant1, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Moreover, Galnt1 is implicated in the glycosylation of proteins vital for bone formation for instance osteopontin and bone sialoprotein.
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Synonyms
Polypeptide N-acetylgalactosaminyltransferase 1, GALNT1, GALNAC-T1
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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
ADPGLPAGDV LEPVQKPHEG PGEMGKPVVI PKEDQEKMKE MFKINQFNLM ASEMIALNRS
LPDVRLEGCK TKVYPDNLPT TSVVIVFHNE AWSTLLRTVH SVINRSPRHM IEEIVLVDDA
SERDFLKRPL ESYVKKLKVP VHVIRMEQRS GLIRARLKGA AVSKGQVITF LDAHCECTVG
WLEPLLARIK HDRRTVVCPI IDVISDDTFE YMAGSDMTYG GFNWKLNFRW YPVPQREMDR
RKGDRTLPVR TPTMAGGLFS IDRDYFQEIG TYDAGMDIWG GENLEISFRI WQCGGTLEIV
TCSHVGHVFR KATPYTFPGG TGQIINKNNR RLAEVWMDEF KNFFYIISPG VTKVDYGDIS
SRVGLRHKLQ CKPFSWYLEN IYPDSQIPRH YFSLGEIRNV ETNQCLDNMA RKENEKVGIF
NCHGMGGNQV FSYTANKEIR TDDLCLDVSK LNGPVTMLKC HHLKGNQLWE YDPVKLTLQH
VNSNQCLDKA TEEDSQVPSI RDCNGSRSQQ WLLRNVTLPE IFHHHHHH.
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 :
DBH HumanDescription:
DBH Human Recombinant
EC 1.14.17.1, DBM, DBH.
Product # :
ENZ-891Price :
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Description
DBH Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 599 amino acids (40-617 a.a) and having a molecular mass of 67.2kDa.DBH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DBH protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
DBH catalyzes the chemical reaction. DBH is an oxidoreductase which belongs to the copper type II, ascorbate-dependent monooxygenase family, in particular those performing on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated can not be derived from O2 with reduced ascorbate as one donor, as well as incorporation of one ato of oxygen into the other donor.
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Synonyms
EC 1.14.17.1, DBM, DBH.
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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 MSAPRESPLP YHIPLDPEGS LELSWNVSYT QEAIHFQLLV RRLKAGVLFG MSDRGELENA DLVVLWTDGD TAYFADAWSD QKGQIHLDPQ QDYQLLQVQR TPEGLTLLFK RPFGTCDPKD YLIEDGTVHL VYGILEEPFR SLEAINGSGL QMGLQRVQLL KPNIPEPELP SDACTMEVQA PNIQIPSQET TYWCYIKELP KGFSRHHIIK YEPIVTKGNE ALVHHMEVFQ CAPEMDSVPH FSGPCDSKMK PDRLNYCRHV LAAWALGAKA FYYPEEAGLA FGGPGSSRYL RLEVHYHNPL VIEGRNDSSG IRLYYTAKLR RFNAGIMELG LVYTPVMAIP PRETAFILTG YCTDKCTQLA LPPSGIHIFA SQLHTHLTGR KVVTVLVRDG REWEIVNQDN HYSPHFQEIR MLKKVVSVHP GDVLITSCTY NTEDRELATV GGFGILEEMC VNYVHYYPQT QLELCKSAVD AGFLQKYFHL INRFNNEDVC TCPQASVSQQ FTSVPWNSFN RDVLKALYSF APISMHCNKS SAVRFQGEWN LQPLPKVIST LEEPTPQCPT SQGRSPAGPT VVSIGGGKG
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 :
SORD HumanDescription:
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-1151Price :
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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.
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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.
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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
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.
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Name :
FOLH1 MouseDescription:
Folate Hydrolase 1 Mouse Recombinant
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
Product # :
ENZ-957Price :
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Description
FOLH1 Mouse Recombinant produced in in Sf9 Baculovirus cells is a single, non-glycosylated polypeptide chain containing 717 amino acids (45-752a.a) and having a molecular mass of 80.5kDa (Migrates at 70-100kDa on SDS-PAGE under reducing conditions). FOLH1 is fused to a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The FOLH1 solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Folate Hydrolase 1 (Folh1) is a single pass type 2 membrane protein which is expressed mainly in prostate epithelium. Folh1 which is a part of the peptidase M28 family and M28B subfamily has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase activity. Folh1 can be found in urinary bladder, kidney, testis, ovary, stomach, small intestine colon, and the capillary endothelium of various tumors. Therefore, Folh1 plays a role in directed imaging and therapy of recurrent of metastatic disease.
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Synonyms
Folh1, GCP2, mopsm, Glutamate carboxypeptidase 2, Folate hydrolase 1, Folylpoly-gamma-glutamate carboxypeptidase, FGCP, Glutamate carboxypeptidase II, GCPII, Naalad1.
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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
ADPKPSNEAT GNVSHSGMKK EFLHELKAEN IKKFLYNFTR TPHLAGTQNN FELAKQIHDQ WKEFGLDLVE LSHYDVLLSY PNKTHPNYIS IINEDGNEIF KTSLSEQPPP GYENISDVVP PYSAFSPQGT PEGDLVYVNY ARTEDFFKLE REMKISCSGK IVIARYGKVF RGNMVKNAQL AGAKGMILYS DPADYFVPAV KSYPDGWNLP GGGVQRGNVL NLNGAGDPLT PGYPANEHAY RHELTNAVGL PSIPVHPIGY DDAQKLLEHM GGPAPPDSSW KGGLKVPYNV GPGFAGNFST QKVKMHIHSY TKVTRIYNVI GTLKGALEPD RYVILGGHRD AWVFGGIDPQ SGAAVVHEIV RSFGTLKKKG RRPRRTILFA SWDAEEFGLL GSTEWAEEHS RLLQERGVAY INADSSIEGN YTLRVDCTPL MYSLVYNLTK ELQSPDEGFE GKSLYDSWKE KSPSPEFIGM PRISKLGSGN DFEVFFQRLG IASGRARYTK NWKTNKVSSY PLYHSVYETY ELVVKFYDPT FKYHLTVAQV RGAMVFELAN SIVLPFDCQS YAVALKKYAD TIYNISMKHP QEMKAYMISF DSLFSAVNNF TDVASKFNQR LQELDKSNPI LLRIMNDQLM YLERAFIDPL GLPGRPFYRH IIYAPSSHNK YAGESFPGIY DALFDISSKV NASKAWNEVK RQISIATFTV QAAAETLREV AHHHHHH.
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 :
Cyclophilin B MouseDescription:
Cyclophilin-B Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
Product # :
ENZ-1039Price :
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Description
Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.
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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
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Synonyms
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
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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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
RDKPLKDVII VDSGKIEVEK PFAIAKE.
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.