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1000 results found for “deaminase”
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Name :
tPA Human, Sf9Description:
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-1011Price :
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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.
More Info
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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.
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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
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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Name :
AK5 HumanDescription:
Adenylate Kinase 5 Human Recombinant
Adenylate kinase isoenzyme 5, AK 5, ATP-AMP transphosphorylase 5, AK5, AK6.
Product # :
PKA-011Price :
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Description
AK5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 586 amino acids (1-562 a.a.) and having a molecular mass of 65.9kDa.AK5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
AK5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Adenylate kinase isoenzyme 5 (AK5) belongs to the adenylate kinase family, which is involved in regulating the adenine nucleotide composition within a cell by catalyzing the reversible transfer of phosphate groups among adenine nucleotides. AK5 is related to the UMP/CMP kinase of several species. AK5 is located in the cytosol and expressed exclusively in the brain.
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Synonyms
Adenylate kinase isoenzyme 5, AK 5, ATP-AMP transphosphorylase 5, AK5, AK6.
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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 MGSHMNTNDA KEYMARREIP QLFESLLNGL MCSKPEDPVE YLESCLQKVK ELGGCDKVKW DTFVSQEKKT LPPLNGGQSR RSFLRNVMPG NSNFPYRRYD RLPPIHQFSI ESDTDLSETA ELIEEYEVFD PTRPRPKIIL VIGGPGSGKG TQSLKIAERY GFQYISVGEL LRKKIHSTSS NRKWSLIAKI ITTGELAPQE TTITEIKQKL MQIPDEEGIV IDGFPRDVAQ ALSFEDQICT PDLVVFLACA NQRLKERLLK RAEQQGRPDD NVKATQRRLM NFKQNAAPLV KYFQEKGLIM TFDADRDEDE VFYDISMAVD NKLFPNKEAA AGSSDLDPSM ILDTGEIIDT GSDYEDQGDD QLNVFGEDTM GGFMEDLRKC KIIFIIGGPG SGKGTQCEKL VEKYGFTHLS TGELLREELA SESERSKLIR DIMERGDLVP SGIVLELLKE AMVASLGDTR GFLIDGYPRE VKQGEEFGRR IGDPQLVICM DCSADTMTNR LLQRSRSSLP VDDTTKTIAK RLEAYYRASI PVIAYYETKT QLHKINAEGT PEDVFLQLCT AIDSIF.
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 :
CA13 HumanDescription:
Carbonic Anhydrase XIII Human Recombinant
Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.
Product # :
ENZ-902Price :
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Shipped with Ice Packs
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Description
CA13 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids (1-262a.a) and having a molecular mass of 31.8kDa.CA13 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CA13 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4),10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze 1.0 pmole of 4-nitrophenyl acetate to 4-nitrophenol per minute at pH 7.5 at 37C.More Info
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Introduction
Carbonic Anhydrase XIII, also known as CA13 is a member of the alpha-carbonic anhydrase family, which catalyzes the rapid interconversion of carbon dioxide and water tobicarbonate and protons, a reversible reaction which occurs relatively slowly in the absence of catalyst. Furthermore, the active siteof nearly all carbonic anhydrases contains a zinc ion; they have been classified as metalloenzymes. At least fivedistinct CA families (?, ?, ?, ? and ?) have been found. These families have no significant a.a sequence resemblance and in just about allcases are considered to be an example of convergent evolution. The ?-CAs have been demonstrated in humans.
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Synonyms
Carbonic Anhydrase XIII, Carbonate Dehydratase XIII, EC 4.2.1.1, CA-XIII, Carbonic, Anhydrase 13, CAXIII.
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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 SSGLVPRGSP MGSMSRLSWG YREHNGPIHW KEFFPIADGD QQSPIEIKTK EVKYDSSLRP LSIKYDPSSA KIISNSGHSF NVDFDDTENK SVLRGGPLTG SYRLRQVHLH WGSADDHGSE HIVDGVSYAA ELHVVHWNSD KYPSFVEAAH EPDGLAVLGV FLQIGEPNSQ LQKITDTLDS IKEKGKQTRF TNFDLLSLLP PSWDYWTYPG SLTVPPLLES VTWIVLKQPI NISSQQLAKF RSLLCTAEGE AAAFLVSNHR PPQPLKGRKV RASFH.
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 :
PGP Human, ActiveDescription:
Phosphoglycolate Phosphatase Human Recombinant, Active
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
Product # :
ENZ-1044Price :
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Description
PGP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 345 amino acids (1-321a.a) and having a molecular mass of 36.5kDa.PGP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PGP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT..
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3,000 units/mg, and is defined as the amount of enzyme that hydrolyze 1.0 nmole of p-nitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
More Info
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Introduction
Phosphoglycolate phosphatase (PGP) is discovered in all tissues including red cells, lymphocytes and cultured fibroblasts (at protein level). PGP is most active in skeletal muscle and cardiac muscle. The catalytic activity of PGP is 2-phosphoglycolate + H2O = glycolate + phosphate. Diseases associated with PGP include tardive dyskinesia and polycystic kidney disease.
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Synonyms
Glycerol-3-phosphate phosphatase, G3PP, Aspartate-based ubiquitous Mg(2+)-dependent phosphatase, AUM, Phosphoglycolate phosphatase, PGP.
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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 MGSHMAAAEA GGDDARCVRL SAERAQALLA DVDTLLFDCD GVLWRGETAV PGAPEALRAL RARGKRLGFI TNNSSKTRAA YAEKLRRLGF GGPAGPGASL EVFGTAYCTA LYLRQRLAGA PAPKAYVLGS PALAAELEAV GVASVGVGPE PLQGEGPGDW LHAPLEPDVR AVVVGFDPHF SYMKLTKALR YLQQPGCLLV GTNMDNRLPL ENGRFIAGTG CLVRAVEMAA QRQADIIGKP SRFIFDCVSQ EYGINPERTV MVGDRLDTDI LLGATCGLKT ILTLTGVSTL GDVKNNQESD CVSKKKMVPD FYVDSIADLL PALQG.
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 :
FUT3 HumanDescription:
Fucosyltransferase 3 Human Recombinant
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
Product # :
ENZ-745Price :
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Description
FUT3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (35-361 a.a) and having a molecular mass of 40.6kDa.FUT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FUT3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Fucosyltransferase 3 (FUT3) catalyzes alpha-1, 3 and alpha-1, 4 glycosidic linkages which take part in the expression of Vim-2, Lewis A, Lewis B, sialyl Lewis X and Lewis X/SSEA-1 antigens. FUT3 takes part in blood group Lewis determination; Lewis-positive (Le+) individuals have an active enzyme while Lewis-negative (Le-) individuals have an inactive enzyme. FUT3 also operates on the corresponding 1, 4-galactosyl derivative, creating1, 3-L-fucosyl links.
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Synonyms
Galactoside 3(4)-L-fucosyltransferase, Blood group Lewis alpha-4-fucosyltransferase, Lewis FT, Fucosyltransferase 3, Fucosyltransferase III, FucT-III, FUT3, FT3B, LE, CD174, Les.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSRVSRDDA TGSPRAPSGS SRQDTTPTRP TLLILLWTWP FHIPVALSRC SEMVPGTADC HITADRKVYP QADTVIVHHW DIMSNPKSRL PPSPRPQGQR WIWFNLEPPP NCQHLEALDR YFNLTMSYRS DSDIFTPYGW LEPWSGQPAH PPLNLSAKTE LVAWAVSNWK PDSARVRYYQ SLQAHLKVDV YGRSHKPLPK GTMMETLSRY KFYLAFENSL HPDYITEKLW RNALEAWAVP VVLGPSRSNY ERFLPPDAFI HVDDFQSPKD LARYLQELDK DHARYLSYFR WRETLRPRSF SWALDFCKAC WKLQQESRYQ TVRSIAAWFT.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
LDHB HumanDescription:
Lactate Dehydrogenase B Human Recombinant
Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.
Product # :
ENZ-967Price :
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Description
LDHB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 334 amino acids (1-334) and having a molecular mass of 36.6kDa.
Source
Escherichia Coli.
Formulation
The LDHB solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is >300 units/mg, in which 1 unit will convert 1.0 umole of pyruvate to L-lactate and beta-NAD per min at pH 7.5 at 37°.
More Info
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Introduction
LDHB is part of the lactate dehydrogenase family. LDHB is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concomitant interconversion of NADH and NAD+. LDHB catalyzes the oxidation of hydroxybutyrate, and frequently called Hydroxybutyrate Dehydrogenase (HBD). The LDH family consists of three members, LDH-A, LDH-B and LDH-C. LDHs function as powerful markers for germ cell tumors.
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Synonyms
Lactate Dehydrogenase B, Renal Carcinoma Antigen NY-REN-46, LDH Heart Subunit, EC 1.1.1.27, LDH-B, LDH-H, Epididymis Secretory Protein Li 281, Testicular Secretory Protein Li 25, Lactate Dehydrogenase H Chain, HEL-S-281, EC 1.1.1 , LDHBD, TRG-5.
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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
MATLKEKLIA PVAEEEATVP NNKITVVGVG QVGMACAISI LGKSLADELA LVDVLEDKLK GEMMDLQHGS LFLQTPKIVA DKDYSVTANS KIVVVTAGVR QQEGESRLNL VQRNVNVFKF IIPQIVKYSP DCIIIVVSNP VDILTYVTWK LSGLPKHRVI GSGCNLDSAR FRYLMAEKLG IHPSSCHGWI LGEHGDSSVA VWSGVNVAGV SLQELNPEMG TDNDSENWKE VHKMVVESAY EVIKLKGYTN WAIGLSVADL IESMLKNLSR IHPVSTMVKG MYGIENEVFL SLPCILNARG LTSVINQKLK DDEVAQLKKS ADTLWDIQKD LKDL.
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 :
GNPNAT1 HumanDescription:
Glucosamine-Phosphate N-Acetyltransferase 1 Human Recombinant
Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.
Product # :
ENZ-037Price :
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Description
GNPNAT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (1-184a.a.) and having a molecular mass of 23.1KDa.GNPNAT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GNPNAT1 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.1M NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
GNPNAT1 is a member of the GNA1 subfamily of the larger acetyltransferase family of proteins. GNPNAT1 is limited to the Golgi apparatus and the endosome. GNPNAT1 is vital for UDPGlcNAc biosynthesis pathway. GNPNAT1 catalyzes the synthesis of GlcNAc6P from AcCoA and GlcN6P, a step in the UDP-GlcNAc6P formation pathway.
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Synonyms
Gpnat1, GNPNAT, GNA1, EC 2.3.1.4, FLJ10607, Glucosamine-Phosphate N-Acetyltransferase 1, Phosphoglucosamine acetylase, Phosphoglucosamine transacetylase, Glucosamine 6-Phosphate N-Acetyltransferase.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKPDETP MFDPSLLKEV DWSQNTATFS PAISPTHPGE GLVLRPLCTA DLNRGFFKVL GQLTETGVVS PEQFMKSFEH MKKSGDYYVT VVEDVTLGQI VATATLIIEH KFIHSCAKRG RVEDVVVSDE CRGKQLGKLL LSTLTLLSKK LNCYKITLEC
LPQNVGFYKK FGYTVSEENY MCRRFLK
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 :
WWOX HumanDescription:
WW Domain Containing Oxidoreductase Human Recombinant
FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.
Product # :
ENZ-422Price :
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Description
WWOX Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 254 amino acids (1-234 a.a.) and having a molecular mass of 28.3 kDa.The WWOX is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The WWOX solution (1mg/ml) contains 20mM Tris pH-8, & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
WWOX is a proapoptotic protein and a tumor suppressor protein. WWOX is found in all eukaryotes and involved in the regulation of a broad range of cellular functions such as protein degradation, transcription, and RNA splicing. WWOX functions synergistically with TP53/p53 to control genotoxic stress-induced cell death. WWOX takes part in tumor necrosis factor (TNF)-mediated cell death. Loss of WWOX expression is associated with pancreatobiliary cancers. Reduced expression levels of WWOX protein is associated with the pathogenesis of basal-like differentiation in breast cancer. Loss of WWOX expression is associated with extrahepatic cholangiocarcinoma. WWOX gene alteration is an early genetic alteration contributes to oral carcinogenesis. WWOX induces apoptosis and inhibits human hepatocellular carcinoma cell growth through a mechanism enhanced by JNK inhibition.
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Synonyms
FOR, WOX1, FRA16D, HHCMA56, PRO0128, SDR41C1, D16S432E, WWOX, WW domain-containing oxidoreductase, Fragile site FRA16D oxidoreductase.
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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 MAALRYAGLD DTDSEDELPP GWEERTTKDG WVYYANHTEE KTQWEHPKTG KRKRVAGDLP YGWEQETDEN GQVFFVDHIN KRTTYLDPRL AFTVDDNPTK PTTRQRYDGS TTAMEILQGR DFTGKVVVVT GANSGIGFET AKSFALHGAH VILACRNMAR ASEAVSRILE EWQQGAATTV YCAAVPELEG LGGMYFNNCC RCMPSPEAQS EETARTLWAL SERLIQERLG SQSG.
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 :
PCMT1 HumanDescription:
Protein-L-Isoaspartate O-Methyltransferase Human Recombinant
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
Product # :
ENZ-522Price :
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Description
PCMT1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 263 amino acids (1-227 a.a.) and having a molecular mass of 28.8 kDa. The PCMT1 is fused to a 36 amino acids His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PCMT1 Human solution containing 20mM Tris-HCl pH-8, 0.1M NaCl, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PCMT1 enzyme catalyses the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. PCMT1 is involved in the repair and/or degradation of damaged proteins.
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Synonyms
EC 2.1.1.77, PIMT, PCMT1, Protein-beta-aspartate methyltransferase, Protein L-isoaspartyl/D-aspartyl methyltransferase, L-isoaspartyl protein carboxyl methyltransferase.
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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
RGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMAWK SGGASHSELI HNLRKNGIIK TDKVFEVMLA TDRSHYAKCN PYMDSPQSIG FQATISAPHM HAYALELLFD QLHEGAKALD VGSGSGILTA CFARMVGCTG KVIGIDHIKE LVDDSINNVR KDDPTLLSSG RVQLVVGDGR MGYAEEAPYD AIHVGAAAPV VPQALIDQLK PGGRLILPVG PAGGNQMLEQ YDKLQDGSIK MKPLMGVIYV PLTDKEKQWS RWK.
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 :
GLB1 E.ColiDescription:
Galactosidase-Beta 1 E.coli Recombinant
lacZ, beta-gal, β-gal.
Product # :
ENZ-041Price :
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Description
The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.
Source
Escherichia Coli.
Formulation
Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol
Purity
Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.
More Info
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Introduction
Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.
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Synonyms
lacZ, beta-gal, β-gal.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Protein should be stored for Short Term at 4°C and for long term at -20°C.
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Purification Method
Purified by proprietary chromatographic technique.
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 :
GLO1 HumanDescription:
Glyoxalase-I Human Recombinant
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
Product # :
ENZ-398Price :
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Description
Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
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Synonyms
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
UPP1 E.coliDescription:
Uridine Phosphorylase E.coli Recombinant
UPASE, UDRPASE, UPP, UDP.
Product # :
ENZ-258Price :
Quantity :
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Description
UPP1 E.Coli Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 273 amino acids (1-253) and having a molecular mass of 29.3 kDa. UPP1 is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UPP1 solution (1mg/ml) contains 20 mM Tris-HCl buffer (pH 8.0), 1mM DTT, 50mM NaCl and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UPP1 catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate which are used as carbon and energy sources or in the release of pyrimidine bases for nucleotide synthesis. UPP1 is part of the family of glycosyltransferases, specifically the pentosyltransferases. Pyrimidine nucleoside phosphorylases add ribose or deoxyribose to pyrimidine bases to form nucleosides that can be incorporated into RNA or DNA.
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Synonyms
UPASE, UDRPASE, UPP, UDP.
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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 MSKSDVFHLG LTKNDLQGAT LAIVPGDPDR VEKIAALMDK PVKLASHREF TTWRAELDGK PVIVCSTGIG GPSTSIAVEE LAQLGIRTFL RIGTTGAIQP HINVGDVLVT TASVRLDGAS LHFAPLEFPA VADFECTTAL VEAAKSIGAT THVGVTASSD TFYPGQERYD TYSGRVVRHF KGSMEEWQAM GVMNYEMESA TLLTMCASQG LRAGMVAGVI VNRTQQEIPN AETMKQTESH AVKIVVEAAR RLL.
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 :
UROD HumanDescription:
Uroporphyrinogen Decarboxylase Human Recombinant
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
Product # :
ENZ-536Price :
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Description
UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).
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Synonyms
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
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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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.
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 :
ENTPD3 Human, sf9 BioactiveDescription:
Ectonucleoside Triphosphate Diphosphohydrolase 3 Human Recombinant, sf9 Bioactive
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
Product # :
ENZ-1020Price :
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Description
ENTPD3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 451 amino acids (44-485a.a.) and having a molecular mass of 50.7kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).ENTPD3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ENTPD3 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.
Biological Activity
Specific activity is > 250,000 pmol/min/ug, and is defined as the amount of enzyme that hydrolyze ATP per minute at pH 7.5 at 37C.More Info
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Introduction
Ectonucleoside Triphosphate Diphosphohydrolase 3, also known as ENTPD3, which owns a threefold preference for the hydrolysis of ATP over ADP is similar to E-type nucleotidases (NTPases). ENTPD3 is a protein coding gene which contains four apyrase-conserved areas which is characteristic of NTPases.
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Synonyms
Ectonucleoside Triphosphate Diphosphohydrolase 3, Ecto-ATP Diphosphohydrolase 3, CD39 Antigen-Like 3, Ecto-ATPDase 3, Ecto-Apyrase 3, Ecto-ATPase 3, EC 3.6.1.5, NTPDase 3, CD39L3, HB6, NTPDase-3, EC 3.6.1, Ectonucleoside triphosphate diphosphohydrolase 3, NTPDase 3, CD39 antigen-like 3, Ecto-ATP diphosphohydrolase 3, Ecto-ATPDase 3, Ecto-ATPase 3, Ecto-apyrase 3, HB6.
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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
ADLQIHKQEV LPPGLKYGIV LDAGSSRTTV YVYQWPAEKE NNTGVVSQTF KCSVKGSGIS SYGNNPQDVP RAFEECMQKV KGQVPSHLHG STPIHLGATA GMRLLRLQNE TAANEVLESI QSYFKSQPFD FRGAQIISGQ EEGVYGWITA NYLMGNFLEK NLWHMWVHPH GVETTGALDL GGASTQISFV AGEKMDLNTS DIMQVSLYGY VYTLYTHSFQ CYGRNEAEKK FLAMLLQNSP TKNHLTNPCY PRDYSISFTM GHVFDSLCTV DQRPESYNPN DVITFEGTGD PSLCKEKVAS IFDFKACHDQ ETCSFDGVYQ PKIKGPFVAF AGFYYTASAL NLSGSFSLDT FNSSTWNFCS QNWSQLPLLL PKFDEVYARS YCFSANYIYH LFVNGYKFTE ETWPQIHFEK EVGNSSIAWS LGYMLSLTNQ IPAESPLIRL PIEPPHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
DUT Pyrococcus FruriosusDescription:
Thermostable dUTPase Pyrococcus Fruriosus Recombinant
Thermostable dUTPase, dUTPase.
Product # :
ENZ-281Price :
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Source
Escherichia Coli.
Formulation
dUTPase is supplied in 20mM Tris-HCl (pH 8.2), 1mM DTT, 0.1mM EDTA, 100mM KCl, 0.1% Nonidet P40, 0.1% Tween 20 and 50% glycerol at a concentration of 1000U/µl of the enzyme.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Synonyms
Thermostable dUTPase, dUTPase.
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Physical Appearance
Sterile filtered liquid formulation.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Unit Definition
One unit of enzyme catalyzes hadrylazation of 10 nanomoles of dUTP to dUMP in one hour at 85 Centigrade.
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Specific Activity
10³U/ug.
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 :
HDAC8 MouseDescription:
Histone Deacetylase 8 Mouse Recombinant
Histone deacetylase 8, HD8, Hdac8.
Product # :
ENZ-1026Price :
Quantity :
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Description
HDAC8 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 383 amino acids (1-377 a.a.) and having a molecular mass of 42.5kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).HDAC8 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
HDAC8 protein solution (0.25mg/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
Histone deacetylase 8 (HDAC8) is a member of the class 1 of the histone deacetylase/acuc/apha family. HDAC8 is biologically involved in skull morphogenesis and metabolic control of the ERR-alpha/PGC1-alpha transcriptional complex. Histones play a key role in transcriptional regulation, cell cycle progression, and developmental events. Histone acetylation/deacetylation modifies chromosome structure and affects transcription factor access to DNA.
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Synonyms
Histone deacetylase 8, HD8, Hdac8.
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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
MEMPEEPANS GHSLPPVYIY SPEYVSICDS LVKVPKRASM VHSLIEAYAL HKQMRIVKPK VASMEEMATF HTDAYLQHLQ KVSQEGDEDH PDSIEYGLGY DCPATEGIFD YAAAIGGGTI TAAQCLIDGK CKVAINWSGG WHHAKKDEAS GFCYLNDAVL GILRLRRKFD RILYVDLDLH HGDGVEDAFS FTSKVMTVSL HKFSPGFFPG TGDMSDVGLG KGRYYSVNVP IQDGIQDEKY YHICESVLKE VYQAFNPKAV VLQLGADTIA GDPMCSFNMT PVGIGKCLKY VLQWQLATLI LGGGGYNLAN TARCWTYLTG VILGKTLSSE IPDHEFFTAY GPDYVLEITP SCRPDRNEPH RIQQILNYIK GNLKHVVHHH HHH.
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 :
PYGL HumanDescription:
Phosphorylase, Glycogen, Liver Human Recombinant
GSD6, Glycogen phosphorylase, liver form.
Product # :
ENZ-675Price :
Quantity :
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Description
PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.
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Synonyms
GSD6, Glycogen phosphorylase, liver form.
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Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.
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 :
ACE2 RatDescription:
Angiotensin Converting Enzyme 2 Rat Recombinant
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
Product # :
ENZ-1124Price :
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Description
ACE2 Rat produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 731 amino acids (18-740 aa) and having a molecular mass of 84.7kDa. ACE2 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The ACE2 solution contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 150 pmol/min/ug, and is defined as the amount of enzyme that hydrolysis 1.0 pmole of McaYVADAPK(Dnp)-OH per minute at pH 7.5, at 25C.
More Info
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Introduction
Angiotensin converting enzyme 2 or ACE-2 is an enzyme that is located in the cell membranes in different organs such as kidney, intestines, lungs, heart & arteries. ACE2 acts as an entry receptor of SARS coronaviruses & SARS-CoV-2.The coronavirus spike (S) glycoprotein is a class I viral fusion antigen bound to the external envelope of the virion that has a role in a crucial part in viral infection by identifying host cell receptors and starting fusion of the viral and cellular membranes. Couple of main domains in coronavirus S1 have been identified, the N-terminal domain and C-terminal domain. One or the other and/or both S1 domains acts as a receptor-binding domain. SARS-CoV + MERS-CoV equally use C-domain to attach their receptors.ACE2 is a type I transmembrane antigen with an extracellular N-terminal domain having the catalytic site and an intracellular C-terminal tail. ACE2 has a signal peptide, a transmembrane domain & a single metalloproteinase active site holds an HEXXH zinc-binding domain. ACE-2 takes part as a mono-carboxypeptidase which degrades Ang I to produce the nonapeptide Ang 1–9 and Ang II to create the heptapeptide Ang 1–7.
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Synonyms
ACE2, 2010305L05Rik, Angiotensin I Converting Enzyme, Angiotensin I Converting, Enzyme (Peptidyl-Dipeptidase A), Angiotensin-Converting Enzyme Homolog, Angiotensin-Converting Enzyme, ACE-Related Carboxypeptidase, Metalloprotease MPROT15, Peptidyl-Dipeptidase A, ACEH, EC 3.4.17.23, EC 3.4.17.
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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
QSLIEEKAES FLNKFNQEAE DLSYQSSLAS WNYNTNITEE NAQKMNEAAA KWSAFYEEQS KIAQNFSLQE IQNATIKRQL KALQQSGSSA LSPDKNKQLN TILNTMSTIY STGKVCNSMN PQECFLLEPG LDEIMATSTD YNRRLWAWEG WRAEVGKQLR PLYEEYVVLK NEMARANNYE DYGDYWRGDY EAEGVEGYNY NRNQLIEDVE NTFKEIKPLY EQLHAYVRTK LMEVYPSYIS PTGCLPAHLL GDMWGRFWTN LYPLTTPFLQ KPNIDVTDAM VNQSWDAERI FKEAEKFFVS VGLPQMTPGF WTNSMLTEPG DDRKVVCHPT AWDLGHGDFR IKMCTKVTMD NFLTAHHEMG HIQYDMAYAK QPFLLRNGAN EGFHEAVGEI MSLSAATPKH LKSIGLLPSN FQEDNETEIN FLLKQALTIV GTLPFTYMLE KWRWMVFQDK IPREQWTKKW WEMKREIVGV VEPLPHDETY CDPASLFHVS NDYSFIRYYT RTIYQFQFQE ALCQAAKHDG PLHKCDISNS TEAGQKLLNM LSLGNSGPWT LALENVVGSR NMDVKPLLNY FQPLFVWLKE QNRNSTVGWS TDWSPYADQS IKVRISLKSA LGKNAYEWTD NEMYLFRSSV AYAMREYFSR EKNQTVPFGE ADVWVSDLKP RVSFNFFVTS PKNVSDIIPR SEVEEAIRMS RGRINDIFGL NDNSLEFLGI YPTLKPPYEP PVTLEHHHHH 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 :
PDIA4 HumanDescription:
Protein Disulfide Isomerase A4 Human Recombinant
Endoplasmic reticulum resident protein 72, ERP70, ERP72.
Product # :
ENZ-246Price :
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Description
PDIA4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 646 amino acids (21-645 a.a.) and having a molecular weight of 72.9kDa. The PDIA4 is fused to 21a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PDIA4 1mg/ml protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
PDIA4 is an endoplasmic reticulum luminal protein that is a stress protein as well as a member of the protein disulfide isomerase family of proteins. PDIA4 participates in the catalysis of protein-S-S-bond rearrangement. PDIA4 and PDIA3 function as proteases, protein disulfide isomerases, phospholipases or an arrangement of these.
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Synonyms
Endoplasmic reticulum resident protein 72, ERP70, ERP72.
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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 MVAGAEGPDE DSSNRENAIE DEEEEEEEDD DEEEDDLEVK EENGVLVLND ANFDNFVADK DTVLLEFYAP WCGHCKQFAP EYEKIANILK DKDPPIPVAK IDATSASVLA SRFDVSGYPT IKILKKGQAV DYEGSRTQEE IVAKVREVSQ PDWTPPPEVT LVLTKENFDE VVNDADIILV EFYAPWCGHC KKLAPEYEKA AKELSKRSPP IPLAKVDATA ETDLAKRFDV SGYPTLKIFR KGRPYDYNGP REKYGIVDYM IEQSGPPSKE ILTLKQVQEF LKDGDDVIII GVFKGESDPA YQQYQDAANN LREDYKFHHT FSTEIAKFLK VSQGQLVVMQ PEKFQSKYEP RSHMMDVQGS TQDSAIKDFV LKYALPLVGH RKVSNDAKRY TRRPLVVVYY SVDFSFDYRA ATQFWRSKVL EVAKDFPEYT
FAIADEEDYA GEVKDLGLSE SGEDVNAAIL DESGKKFAME PEEFDSDTLR EFVTAFKKGK LKPVIKSQPV PKNNKGPVKV VVGKTFDSIV MDPKKDVLIE FYAPWCGHCK QLEPVYNSLA KKYKGQKGLV IAKMDATAND VPSDRYKVEG FPTIYFAPSG DKKNPVKFEG GDRDLEHLSK FIEEHATKLS RTKEEL.
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 :
KEL MouseDescription:
Kell Metallo-Endopeptidase Mouse Recombinant
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
Product # :
ENZ-1158Price :
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Description
KEL Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 674 amino acids (49-713 aa) and having a molecular mass of 76.3kDa.KEL is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The KEL solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Kell blood group glycoprotein homolog or KEL, is an enzyme, part of the zinc endopeptidase of the neprilysin (NEP) group of proteins. KEL has a crucial part in the production of the potent bioactive ET-3, which also includes enzymes that are endothelin convertingenzymes (PEX, XCE, DINE &various NEP-like proteins). KEL uses a single disulfide bond to XK, a gated membranal transporter. The Kell antigen system that includes two proteins, is very crucial among blood group systems.
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Synonyms
kell blood group antigen, kell blood group glycoprotein, Kell blood group, Kell blood group glycoprotein homolog, KEL, Kell, CD238 antigen, CD238, ECE3, Kell blood group-metalloendopeptidase, Kell blood group-metalloendopeptidase.
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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
ADPIFRNCGP CPCETPVCME LLDHYLASGN RSVAPCTDFF SFACEKANGT SDSFQALTEE NKSRLWRLLE APGSWHLGSG EEKAFQFYNS CMDTDAIEAS GSGPLIQIIE ELGGWNITGN WTSLDFNQNL RLLMSQYGHF PFFRAYLRPH PAPPHTPIIQ IDQPEFDILL QQEQEQKVYA QILREYVTYL NRLGTLLGSN PQEAQQHASW SIVFTSRLFQ FLRPQQQQQA QDKLFHVVTI DELQEMAPAI DWLSCLQAIF TPMSLNSSQT LVVHDLDYLR NMSQLVEEGL LNHRESIQSY MILGLVDTLS PALDTKFQEA RRELIQELRK LKERPPLPAY PRWMKCVEQT GAFFEPTLAA LFVREAFGPS IQSAAMELFA EIKDAVIIRL KKLSWISEET QKEALNKLAQ LQVEMGAPKR AVKPDIATQE YNDIQLGPSF LQSFLSCVRS LRARNVQSFL QPFPYHRWQK SPWEVNAYYS ISDHMVVFPA GLLQPPFFHP GYPRAVNFGA AGSIMAHELL HIFYQLLLPG GCPACDTHVL QEALLCLERH YAAFPLPSIS SFNGSHTLLE NAADIGGVAI AFQAYSKRIV EHTGELTLPN LDLSPYQLFF RSYAQVMCRG LSSQDPQDPH SPPSLRVHGP LSNTPDFAKH FHCPRGTLLN PSARCKLWHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TSEN15 HumanDescription:
tRNA Splicing Endonuclease 15 Human Recombinant
tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.
Product # :
PRO-144Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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- More Info
Description
TSEN15 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 191 amino acids (1-171 a.a.) and having a molecular mass of 20.9kDa. The TSEN15 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TSEN15 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
tRNA-splicing endonuclease subunit Sen15 (TSEN15) is a member of the SEN15 family. tRNA splicing is an essential process required for cell growth and division. TSEN15 is a subunit of the tRNA splicing endonuclease. TSEN15 cleaves pre-tRNA at the 5' and 3' splice sites to release the intron.
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Synonyms
tRNA-splicing endonuclease subunit Sen15, SEN15 homolog, HsSEN15, tRNA-intron endonuclease Sen15, TSEN15, C1orf19, SEN15.
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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 MEERGDSEPT PGCSGLGPDG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM ELDIGDATHV YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE GLQTVVPTPI TASLSHNRIR EILKASRKLQ GDPDLPMSFT LAIVESDSTI VYYKLTDGFM LPDPQNISLR R.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SENP8 HumanDescription:
Sentrin Specific Peptidase Family Member 8 Human Recombinant
SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2 (NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8.
Product # :
ENZ-146Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
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Description
SENP8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 232 amino acids (1-212) and having a molecular mass of 26.2 kDa.The SENP8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SENP8 protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.1M NaCl, 1mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SENP8 is a cysteine protease which belongs to the sentrin-specific protease family. SENP8 takes part in processing and deconjugation of the ubiquitin-like protein labeled, neural precursor cell expressed developmentally downregulated 8(NEDD8).
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Synonyms
SUMO/sentrin specific peptidase family member 8, DEN1, NEDP1, Protease cysteine 2
(NEDD8 specific), PRSC2, NEDD8-specific protease 1, HsT17512, Deneddylase-1, NEDD8 specific-protease cysteine 2, Sentrin/SUMO-specific protease SENP8. -
Physical Appearance
SENP8 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 MDPVVLSYMD SLLRQSDVSL LDPPSWLNDH IIGFAFEYFA NSQFHDCSDH VSFISPEVTQ FIKCTSNPAE IAMFLEPLDL PNKRVVFLAI NDNSNQAAGG THWSLLVYLQ DKNSFFHYDS HSRSNSVHAK QVAEKLEAFL GRKGDKLAFV EEKAPAQQNS YDCGMYVICN TEALCQNFFR QQTESLLQLL TPAYITKKRG EWKDLITTLA KK
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SULT2A1 HumanDescription:
Sulfotransferase Family, Cytosolic, 2A, Member 1 Human Recombinant
Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.
Product # :
ENZ-141Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
SULT2A1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (1-285a.a) and having a molecular mass of 35.9kDa.SULT2A1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SULT2A1 protein solution (1mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
SULT2A1 is a member fo the sulfotransferase family. SULT2A1 is primarily expressed in liver and adrenal tissues, and to a lesser extent in kidney. SULT2A1 catalyzes the 3'-phosphoadenosine 5'-phosphosulfate-dependent sulfation of an extensive selection of steroids in human liver and adrenal tissues, and in addition is responsible for a larg number of the sulfation of bile acids in human liver.
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Synonyms
Sulfotransferase family cytosolic 2A dehydroepiandrosterone (DHEA)-preferring member 1, DHEA-ST, STD, HST, ST2, ST2A1, ST2A3, Alcohol/hydroxysteroid sulfotransferase, bile-salt sulfotranasferase 2A1, EC 2.8.2.14.
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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 MSDDFLWFEG IAFPTMGFRS ETLRKVRDEF VIRDEDVIIL TYPKSGTNWL AEILCLMHSK GDAKWIQSVP IWERSPWVES EIGYTALSET ESPRLFSSHL PIQLFPKSFF SSKAKVIYLM RNPRDVLVSG YFFWKNMKFI KKPKSWEEYF EWFCQGTVLY GSWFDHIHGW MPMREEKNFL LLSYEELKQD TGRTIEKICQ FLGKTLEPEE LNLILKNSSF QSMKENKMSN YSLLSVDYVV DKAQLLRKGV SGDWKNHFTV AQAEDFDKLF QEKMADLPRE LFPWE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ITPA HumanDescription:
Inosine Triphosphatase Human Recombinant
EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.
Product # :
ENZ-549Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
- purity
- More Info
Description
ITPA Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 215 amino acids (1-194 a.a.) and having a molecular mass of 23.7 kDa. The ITPA is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ITPA solution (1mg/ml) contains 20mM Tris-HCl pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ITPA enzyme catalyzes the pyrophosphohydrolysis of both ITP (inosine triphosphate) and dITP (deoxyinosine triphosphate) to IMP (inosine monophosphate) and diphosphate. IMP is exercised as a substrate for purine nucleotide pathways. IMP is phosphorylated to ITP, and ITPA mediates the concentration of ITP in the cell by changing ITP back to IMP. Defects in ITPA result in ITPA deficiency which is thought to be inherited and is characterized by an over-accumulation of ITP in erythocytes, leukocytes and fibroblasts.
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Synonyms
EC 3.6.1.19, C20orf37, dJ794I6.3, HLC14-06-P, ITPase, My049, OK/SW-cl.9, Inosine Triphosphatase, ITPA.
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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 MMAASLVGKK IVFVTGNAKK LEEVVQILGD KFPCTLVAQK IDLPEYQGEP DEISIQKCQE AVRQVQGPVL VEDTCLCFNA LGGLPGPYIK WFLEKLKPEG LHQLLAGFED KSAYALCTFA LSTGDPSQPV RLFRGRTSGR IVAPRGCQDF GWDPCFQPDG YEQTYAEMPK AEKNAVSHRF RALLELQEYF GSLAA.
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.