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1000 results found for “epimerase”
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Name :
TDG HumanDescription:
Thymine-DNA Glycosylase Human Recombinant
Thymine-DNA Glycosylase, G/T Mismatch-Specific Thymine DNA Glycosylase, EC 3.2.2.29.
Product # :
ENZ-649Price :
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Description
TDG Human Recombinant produced in E. coli is a single polypeptide chain containing 433 amino acids (1-410) and having a molecular mass of 48.4 kDa.TDG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TDG solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
Thymine-DNA glycosylase (TDG) is a member of the TDG/mug DNA glycosylase family.
TDG is a nuclear protein that fixes G/T mismatches to G/C pairs by hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired thymin. In addition, TDG removes uracil and 5-bromouracil from mispairings with guanine. The TDG enzyme has an essential role in cellular defense against genetic mutation triggered by the spontaneous deamination of 5-methylcytosine and cytosine. -
Synonyms
Thymine-DNA Glycosylase, G/T Mismatch-Specific Thymine DNA Glycosylase, EC 3.2.2.29.
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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 MGSMEAENAG SYSLQQAQAF YTFPFQQLMA EAPNMAVVNE QQMPEEVPAP APAQEPVQEA PKGRKRKPRT TEPKQPVEPK KPVESKKSGK SAKSKEKQEK ITDTFKVKRK VDRFNGVSEA ELLTKTLPDI LTFNLDIVII GINPGLMAAY KGHHYPGPGN HFWKCLFMSG LSEVQLNHMD DHTLPGKYGI GFTNMVERTT PGSKDLSSKE FREGGRILVQ KLQKYQPRIA VFNGKCIYEI FSKEVFGVKV KNLEFGLQPH KIPDTETLCY GMPSSSARCA QFPRAQDKVH YYIKLKDLRD QLKGIERNMD VQEVQYTFDL QLAQEDAKKM AVKEEKYDPG YEAAYGGAYG ENPCSSEPCG FSSNGLIESV ELRGESAFSG IPNGQWMTQS FTDQIPSFSN HCGTQEQEEE SHA.
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 :
ProMatrilysinDescription:
ProMatrix Metalloproteinase-7 Recombinant
Product # :
ENZ-272Price :
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Description
Matrix metalloproteinase-7 (MMP-7) also known as matrilysin and PUMP (EC 3.4.24.23) cleaves a number of substrates including collagen types IV and X, elastin, fibronectin, gelatin, laminin and proteoglycans. MMP-7 is closely related to the stromelysin family members but is encoded by a different gene. MMP-7 is the smallest of all the MMPs consisting of a pro-peptide domain and a catalytic domain. It lacks the hemopexin-like domain common to other members of the MMPs. MMP-7 is secreted as a 28 kDa proenzyme and can be activated in vitro by organomercurials and trypsin and in vivo by MMP-3 to a 18 kDa active MMP-7 enzyme. Once activated, MMP-7 can activate pro-MMP-1 and pro-MMP-9 but not pro-MMP-2. MMP-7 is widely expressed having been reported in elevated levels in cycling endometrium as well as in colorectal cancers and adenomas, hepatocellular carcinomas, rectal carcinomas, and approximately 50% of gliomas.
Source
Escherichia Coli.
Formulation
The protein contains the following additives 25mM Tris-HCl (pH 7.5),150mM NaCl, 5mM CaCl2, 0.01% Brij-35 and 0.02% NaN3.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity was found to be 1400 IU/mg.More Info
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Physical Appearance
Sterile clear liquid 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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Unit Definition
One unit is defined as the digestion of 1 µg Azocoll/min at 37°C.
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 :
ECHS1 HumanDescription:
Enoyl CoA Hydratase, Short chain, 1, Mitochondrial Human Recombinant
Enoyl-CoA hydratase 1, SCEH.
Product # :
ENZ-556Price :
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Description
ECHS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (28-290 a.a.) and having a molecular mass of 30.6kDa.ECHS1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ECHS1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH-8), 1mM DTT,0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
ECHS1 is part of the hydratase/isomerase superfamily. ECHS1 is localized in the mitochondrial matrix and Expressed in muscle, liver and fibroblasts, with low expression in kidney and spleen, ECHS1 exists as a homohexamer that takes part in the second phase of the mitochondrial fatty acid β-oxidation pathway.
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Synonyms
Enoyl-CoA hydratase 1, SCEH.
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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 MASGANFEYI IAEKRGKNNT VGLIQLNRPK ALNALCDGLI DELNQALKIF EEDPAVGAIV LTGGDKAFAA GADIKEMQNL SFQDCYSSKF LKHWDHLTQV KKPVIAAVNG YAFGGGCELA MMCDIIYAGE KAQFAQPEIL IGTIPGAGGT QRLTRAVGKS LAMEMVLTGD RISAQDAKQA GLVSKICPVE TLVEEAIQCA EKIASNSKIV VAMAKESVNA AFEMTLTEGS KLEKKLFYST FATDDRKEGM TAFVEKRKAN FKDQ.
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 :
QPCT HumanDescription:
Glutaminyl-Peptide Cyclotransferase Human Recombinant
Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.
Product # :
ENZ-912Price :
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Description
QPCT produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 339 amino acids (29-361a.a.) and having a molecular mass of 38.7kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). QPCT is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
QPCT 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
Glutaminyl-Peptide Cyclotransferase, also known as QPCT is a member of the glutaminyl-peptide cyclotransferase family. QPCT is responsible for the biosynthesis of pyroglutamyl peptides. Furthermore, QPCT is partial against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length following the second residue. QPCT catalyzes N-terminal pyroglutamate formation, also in vitro, it catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid.
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Synonyms
Glutaminyl-Peptide Cyclotransferase, Glutaminyl Cyclase, QC, Glutaminyl-TRNA Cyclotransferase, Glutamyl Cyclase, EC 2.3.2.5, SQC, EC, GCT, Glutaminyl-peptide cyclotransferase.
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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
VSPSASAWPE EKNYHQPAIL NSSALRQIAE GTSISEMWQN DLQPLLIERY PGSPGSYAAR QHIMQRIQRL QADWVLEIDT FLSQTPYGYR SFSNIISTLN PTAKRHLVLA CHYDSKYFSH WNNRVFVGAT DSAVPCAMML ELARALDKKL LSLKTVSDSK PDLSLQLIFF DGEEAFLHWS PQDSLYGSRH LAAKMASTPH PPGARGTSQL HGMDLLVLLD LIGAPNPTFP NFFPNSARWF ERLQAIEHEL HELGLLKDHS LEGRYFQNYS YGGVIQDDHI PFLRRGVPVL HLIPSPFPEV WHTMDDNEEN LDESTIDNLN KILQVFVLEY LHLHHHHHH.
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 :
MME Human, ActiveDescription:
Membrane Metalloendopeptidase Human Recombinant, Active
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
Product # :
ENZ-1116Price :
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Description
MME Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 708 amino acids (52-750 aa) and having a molecular mass of 80.9kDa.MME is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The MME solution (1mg/ml) contains 10% Glycerol, 20 mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 5,000 pmol/min/ug. One unit will convert 1.0 pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to MCA- Pro-Leu-OH per minute, at pH 8.8 at 25C˚.
More Info
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Introduction
Neutral endopeptidase (NEP) is an enzyme located in the cell membrane (bound to it) that is able to dissolve biologically active proteins and is expressed on the surface of lymphoid progenitors, human podocytes, syncytiotrophoblastic cells, and many other epithelial cells including polymorphonuclear leukocytes.
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Synonyms
Membrane Metalloendopeptidase, Common Acute Lymphocytic Leukemia Antigen, Neutral Endopeptidase 24.11, Skin Fibroblast Elastase, Neutral Endopeptidase, Atriopeptidase, Enkephalinase, EC 3.4.24.11, Neprilysin, CALLA, NEP, SFE,Membrane Metallo-Endopeptidase (Neutral Endopeptidase, Enkephalinase, CALLA, CD10), Membrane Metallo-Endopeptidase Variant 1, Membrane Metallo-Endopeptidase Variant 2, Neprilysin-390, Neprilysin-411, CD10 Antigen, EC 3.4.24, CMT2T, SCA43, CD10, EPN, MME.
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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
ADPYDDGICK SSDCIKSAAR LIQNMDATTE PCTDFFKYAC GGWLKRNVIP ETSSRYGNFD ILRDELEVVL KDVLQEPKTE DIVAVQKAKA LYRSCINESA IDSRGGEPLL KLLPDIYGWP VATENWEQKY GASWTAEKAI AQLNSKYGKK VLINLFVGTD DKNSVNHVIH IDQPRLGLPS RDYYECTGIY KEACTAYVDF MISVARLIRQ EERLPIDENQ LALEMNKVME LEKEIANATA KPEDRNDPML LYNKMTLAQI QNNFSLEING KPFSWLNFTN EIMSTVNISIT NEEDVVVYAP EYLTKLKPI LTKYSARDLQ NLMSWRFIMD LVSSLSRTYK ESRNAFRKAL YGTTSETATW RRCANYVNGN MENAVGRLYV EAAFAGESKH VVEDLIAQIR EVFIQTLDDL TWMDAETKKR AEEKALAIKE RIGYPDDIVS NDNKLNNEYL ELNYKEDEYF ENIIQNLKFS QSKQLKKLRE KVDKDEWISG AAVVNAFYSS GRNQIVFPAG ILQPPFFSAQ QSNSLNYGGI GMVIGHEITH GFDDNGRNFN KDGDLVDWWT QQSASNFKEQ SQCMVYQYGN FSWDLAGGQH LNGINTLGEN IADNGGLGQA YRAYQNYIKK NGEEKLLPGL DLNHKQLFFL NFAQVWCGTY RPEYAVNSIK TDVHSPGNFR IIGTLQNSAE FSEAFHCRKN SYMNPEKKCR VWHHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
MAT2A HumanDescription:
Methionine Adenosyltransferase II Alpha Human Recombinant
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
Product # :
ENZ-320Price :
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Description
MAT2A Human Recombinant fused with His tag (20 a.a.) at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 45.8 kDa.The MAT2A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAT2A solution (1mg/ml) contains 20mM Tris pH-8 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
MAT2A is an important enzyme in cellular metabolism and catalyzes the formation of S-adenosylmethionine (SAMe) from L-methionine and ATP. MAT2A is expressed in extrahepatic tissues. In liver, MAT2A expression associates with growth, dedifferentiation, and cancer. NF-kappa B and AP-1 are necessary for basal MAT2A expression in HepG2 cells and mediate the increase in MAT2A expression in response to TNF-alpha. Up-regulation of MAT2A provides growth improvement and s-adenosylmethionine and methylthioadenosine thus can block mitogenic signaling in colon cancer cells. Lower expression of both MAT2A and MAT2beta and interfere with leptin signaling in liver cancer cells.
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Synonyms
MATA2, MATII, SAMS2, MAT-2A, S-adenosylmethionine synthetase isoform type-2, AdoMet synthetase 2, Methionine adenosyltransferase 2, Methionine adenosyltransferase II, MAT2A, AMS2.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY.
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 :
FKBP1A MouseDescription:
FK506 Binding Protein 1A Mouse Recombinant
Peptidyl-prolyl cis-trans isomerase FKBP1A, PPIase FKBP1A, 12 kDa FK506-binding protein, 12 kDa FKBP, FKBP-12, Calstabin-1, FK506-binding protein 1A, FKBP-1A, Immunophilin FKBP12, Rotamase, Fkbp1, FKBP1A.
Product # :
ENZ-871Price :
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Description
FKBP1A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (1-108 a.a) and having a molecular mass of 14.4kDa.FKBP1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FKBP1A solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FKBP1A is a 12kDa protein initially discovered on an immune cells on the basis of its capability to bind as well as mediate the intracellular effect of the immunosuppressant FK506. FKBP1A is also known to mediate the action of Rapamycin-immunosuppressive agent. FKBP1A is part of the family of immunophilins, which have in common high affinity for immunosuppressant drugs and a peptidyl-prolyl cis-trans isomerase (PPIase). Activity which participates in folding of proline-containing protein. In the absence of immunosuppressive ligands, FKBP1A is involved in intracellular calcium regulation by associating with 3 types of Ca2+ release channel complexes: skeletal ryanodine receptors, cardiac ryanodine receptors and the inositol 1,4,5-triphosphate receptor. FKBP1A also interact with TGF-beta type I receptor exerting an inhibitory effect on the TGF-beta signaling pathway. FKBP12 plays a role in modulation of ryanodine receptor isoform-1 (ryr-1), a component of the calcium release channel of skeletal muscle sarcoplasmic reticulum. FKBP1A increase the folding of proteins and catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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Synonyms
Peptidyl-prolyl cis-trans isomerase FKBP1A, PPIase FKBP1A, 12 kDa FK506-binding protein, 12 kDa FKBP, FKBP-12, Calstabin-1, FK506-binding protein 1A, FKBP-1A, Immunophilin FKBP12, Rotamase, Fkbp1, FKBP1A.
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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 MGSHMGVQVE TISPGDGRTF PKRGQTCVVH YTGMLEDGKK FDSSRDRNKP FKFTLGKQEV IRGWEEGVAQ MSVGQRAKLI ISSDYAYGAT GHPGIIPPHA TLVFDVELLK LE
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 :
HARS Human, Sf9Description:
Histidyl-tRNA Synthetase Human Recombinant, Sf9
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1.
Product # :
ENZ-335Price :
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Description
Histidyl-tRNA Synthetase Human Recombinant produced in baculovirus is a single, glycosylated, polypeptide chain having a molecular mass of 58.3 kDa.The Histidyl-tRNA Synthetase is fused to 6x His Tag and purified by proprietary chromatographic techniques.
Source
Sf9 Insect Cells.
Formulation
The protein solution contains 20mM HEPES, 250mM sodium chloride 0.1% and 20% Glycerol, (pH 7.5).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Aminoacyl-tRNA synthetases are a class of enzymes that charge tRNAs with their cognate amino acids. The protein encoded by this gene is a cytoplasmic enzyme which belongs to the class II family of aminoacyl-tRNA synthetases. The enzyme is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. The gene is located in a head-to-head orientation with HARSL on chromosome five, where the homologous genes share a bidirectional promoter. The gene product is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
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Synonyms
Histidyl-tRNA synthetase, EC 6.1.1.21, Histidine-tRNA ligase, HisRS, HRS, FLJ20491, JO-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Histidyl-tRNA Synthetase although stable at 4°C for 3 weeks, should be stored below -18°C.Please prevent freeze-thaw cycles.
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Applications
Western Blot: Strongly reactive with human anti Histidyl-tRNA Synthetase antisera.
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Protein content
Protein quantitation was carried out by using 0.25 - 2.0 mg/ml Bradford assay vs. BSA.
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 :
Lysozyme HumanDescription:
Lysozyme Human Recombinant
EC 3.2.1.17, LYZ, Lysozyme.
Product # :
ENZ-1159Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.
Source
Oryza sativa (rice).
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Purity as determined by SDS-PAGE is greater than 90%.
Biological Activity
1.6x105 U/mg.
More Info
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Introduction
Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
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Synonyms
EC 3.2.1.17, LYZ, Lysozyme.
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Physical Appearance
Sterile Filtered lyophilized (freeze-dried) off white powder.
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Stability
Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.
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 :
NDUFAF2 HumanDescription:
NADH Dehydrogenase 1 Alpha Subcomplex, Assembly Factor 2 Human Recombinant
Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.
Product # :
ENZ-150Price :
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Shipped with Ice Packs
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Description
NDUFAF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a.) and having a molecular mass of 22kDa.NDUFAF2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NDUFAF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 20% glycerol and 200mM NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Mimitin (NDUFAF2) is a member of the complex I NDUFA12 subunit family.NADH dehydrogenase is an enzyme located in the inner mitochondrial membrane, which catalyzes the transfer of electrons from NADH to coenzyme Q (CoQ). NDUFAF2 is the "entry enzyme" of oxidative phosphorylation in the mitochondria. Mimitin protein functions as a molecular chaperone for mitochondrial complex I assembly.
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Synonyms
Mimitin mitochondrial, B17.2-like, B17.2L, Myc-induced mitochondrial protein, MMTN, NADH dehydrogenase [ubiquinone] 1 alpha subcomplex assembly factor 2, NDUFA12-like protein, NDUFAF2, NDUFA12L, mimitin.
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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 MGWSQDLFRA LWRSLSREVK EHVGTDQFGN KYYYIPQYKN WRGQTIREKR IVEAANKKEV DYEAGDIPTE WEAWIRRTRK TPPTMEEILK NEKHREEIKI KSQDFYEKEK LLSKETSEEL LPPPVQTQIK GHASAPYFGK EEPSVAPSST GKTFQPGSWM PRDGKSHNQ.
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 :
BHMT2 HumanDescription:
Betaine-Homocysteine Methyltransferase 2 Human Recombinant
BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.
Product # :
ENZ-798Price :
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Description
BHMT2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 386 amino acids (1-363 a.a.) and having a molecular mass of 42.7kDa. BHMT2 is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
BHMT2 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Betaine-Homocysteine Methyltransferase 2 (BHMT2) is involved in the regulation of homocysteine metabolism. Homocysteine is a sulfur-containing amino acid which has a key role in methylation reactions. Transfer of the methyl group from betaine to homocysteine generates methionine, which donates the methyl group to methylate DNA, proteins, lipids, and other intracellular metabolites. BHMT2 is one of two methyl transferases which can catalyze the transfer of the methyl group from betaine to homocysteine. BHMT2 converts homocysteine to methionine using S-methylmethionine (SMM) as a methyl donor. Homocysteine metabolism anomalies are implicated in disorders varying from vascular disease to neural tube birth defects such as spina bifida.
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Synonyms
BHMT2, Betaine--Homocysteine S-Methyltransferase 2, SMM-Hcy Methyltransferase, Betaine-Homocysteine Methyltransferase 2, S-Methylmethionine--Homocysteine S-Methyltransferase BHMT2, EC 2.1.1.10, EC 2.1.1.5.
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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
MGSSHHHHHH SSGLVPRGSH MGSMAPAGRP GAKKGILERL ESGEVVIGDG SFLITLEKRG YVKAGLWTPE AVIEHPDAVR QLHMEFLRAG SNVMQTFTFS ASEDNMESKW EDVNAAACDL AREVAGKGDA LVAGGICQTS IYKYQKDEAR IKKLFRQQLE VFAWKNVDFL IAEYFEHVEE AVWAVEVLKE SDRPVAVTMC IGPEGDMHDI TPGECAVRLV KAGASIVGVN CRFGPDTSLK TMELMKEGLE WAGLKAHLMV QPLGFHAPDC GKEGFVDLPE YPFGLESRVA TRWDIQKYAR EAYNLGVRYI GGCCGFEPYH IRAIAEELAP ERGFLPPASE KHGSWGSGLD MHTKPWIRAR ARREYWENLL PASGRPFCPS LSKPDF.
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 :
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 :
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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.
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Name :
ENPP1 MouseDescription:
Ectonucleotide Pyrophosphatase Mouse Recombinant
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.
Product # :
ENZ-1193Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
ENPP1 Mouse Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain containing 828 amino acids (Lys85-Glu906) and having a molecular mass of 95.2kDa. ENPP1 Mouse is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
The filtered (0.4µm) concentrated protein solution was lyophilized with PBS, PH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1, E-NPP 1, Membrane component chromosome 6 surface marker 1, Phosphodiesterase I/nucleotide pyrophosphatase 1, Plasma-cell membrane glycoprotein PC-1, ENPP1, M6S1, NPPS, PC1, PDNP1, NPP1, PC-1, PCA1, ARHR2, COLED.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.
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Amino Acid Sequence
KEVKSCKGRC FERTFSNCRC DAACVSLGNC CLDFQETCVE PTHIWTCNKF RCGEKRLSRF VCSCADDCKT HNDCCINYSS VCQDKKSWVE ETCESIDTPE CPAEFESPPT LLFSLDGFRA EYLHTWGGLL PVISKLKNCG TYTKNMRPMY PTKTFPNHYS IVTGLYPESH GIIDNKMYDP KMNASFSLKS KEKFNPLWYK GQPIWVTANH QEVKSGTYFW PGSDVEIDGI LPDIYKVYNG SVPFEERILA VLEWLQLPSH ERPHFYTLYL EEPDSSGHSH GPVSSEVIKA LQKVDRLVGM LMDGLKDLGL DKCLNLILIS DHGMEQGSCK KYVYLNKYLG DVNNVKVVYG PAARLRPTDV PETYYSFNYE ALAKNLSCRE PNQHFRPYLK PFLPKRLHFA KSDRIEPLTF YLDPQWQLAL NPSERKYCGS GFHGSDNLFS NMQALFIGYG PAFKHGAEVD SFENIEVYNL MCDLLGLIPA PNNGSHGSLN HLLKKPIYNP SHPKEEGFLS QCPIKSTSND LGCTCDPWIV PIKDFEKQLN LTTEDVDDIY HMTVPYGRPR ILLKQHHVCL LQQQQFLTGY SLDLLMPLWA SYTFLRNDQF SRDDFSNCLY QDLRIPLSPV HKCSYYKSNS KLSYGFLTPP RLNRVSNHIY SEALLTSNIV PMYQSFQVIW HYLHDTLLQR YAHERNGINV VSGPVFDFDY DGRYDSLEIL KQNSRVIRSQ EILIPTHFFI VLTSCKQLSE TPLECSALES SAYILPHRPD NIESCTHGKR ESSWVEELLT LHRARVTDVE LITGLSFYQD RQESVSELLR LKTHLPIFSQ EDHHHHHH.
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Background
Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is an enzyme with multifaceted roles in cellular metabolism, bone mineralization, and insulin signaling. Research utilizing mouse models has been pivotal in elucidating the complex biology of ENPP1 and its implications for various physiological processes and disease states. This study aims to provide a comprehensive exploration of ENPP1 in mouse physiology, shedding light on its diverse functions and potential applications in understanding metabolic health and disease mechanisms.
The primary objective of this research is to elucidate the impact of ENPP1 in mouse models on metabolic health. In vivo experiments using genetically modified mice with altered ENPP1 expression or activity will be conducted to investigate how ENPP1 influences glucose homeostasis, insulin sensitivity, and lipid metabolism. Understanding these mechanisms is fundamental for deciphering the role of ENPP1 in metabolic diseases such as diabetes and obesity.
The second objective is to assess the clinical relevance of ENPP1 in mouse models of bone health. Mouse models of skeletal disorders will be employed to explore how ENPP1 affects bone mineralization, density, and remodeling. These investigations may provide valuable insights into potential therapeutic strategies targeting ENPP1 in bone-related diseases.
The third objective is to explore the broader implications of ENPP1 in mouse physiology, including its effects on vascular health, inflammation, and tissue repair. Research will investigate its roles in vascular calcification, inflammation resolution, and tissue regeneration. Understanding the multifaceted properties of ENPP1 in mouse models may open new avenues for therapeutic interventions in various metabolic and chronic disease contexts.
By delving into the diverse functions of ENPP1 in mouse physiology, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for metabolic diseases, bone disorders, and other conditions influenced by ENPP1.
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 HumanDescription:
Cyclophilin-B Human Recombinant
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
Product # :
ENZ-313Price :
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Description
Cyclophilin-B Human Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 192 amino acids (26-216) and having a molecular mass of 21.2 kDa. PPIB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
1 mg/ml solution containing 20mM Tris-HCl 8.0, 20mM NaCl, 0.5mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.More Info
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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
Peptidylprolyl isomerase B, PPIase, Rotamase, S-cyclophilin, PPIB, cyclophilin-like protein, peptidyl-prolyl cis-trans isomerase B, Cyclophilin B, SCYLP, CYPB, CYP-S1, MGC2224, MGC14109.
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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
MLLPGPSAAD EKKKGPKVTV KVYFDLRIGD EDVGRVIFGL FGKTVPKTVD NFVALATGEKGFGYKNSKFH RVIKDFMIQG GDFTRGDGTG GKSIYGERFP DENFKLKHYG PGWVSMANAGKDTNGSQFFI TTVKTAWLDG KHVVFGKVLE GMEVVRKVES TKTDSRDKPL KDVIIADCGK IEVEKPFAIA KE.
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 :
GPT Human, ActiveDescription:
Glutamic-Pyruvate Transaminase Human Recombinant, Active
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
Product # :
ENZ-280Price :
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Description
Alanine Aminotransferase Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 495a.a and having a molecular mass of 54,479 Dalton. The amino acid sequence is the same as that of native form of human liver ALT.The ALT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was dialyzed against 40mM sodium acetate buffer (pH 5.5), 1mM DTT,1mM EDTA, 5mM 2-oxoglutarate and 0.1mM pyridoxal-5'-phosphate.
Purity
Greater than 95.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The specific activity was found to be 839 U/mg.
More Info
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Introduction
Alanine transaminase or ALT is a transaminaseenzyme.
ALT is found in serumand in various bodily tissues, but is most commonly associated with the liver; It catalyzes the transfer of an aminogroup from alanineto a-ketoglutarate, the products of this reversible transaminationreaction being pyruvateand glutamatealanine+ a-ketoglutarate= pyruvate+ glutamate
It is commonly measured clinically as a part of a diagnostic liver function test, to determine liver health. It is also called serum glutamate pyruvate transaminase (SGPT) or alanine aminotransferase (ALAT). Diagnostically, it is almost always measured in units/litre (U/L). -
Synonyms
Alanine aminotransferase 1, ALT1, EC 2.6.1.2, Glutamate pyruvate transaminase 1, GPT 1, Glutamic--alanine transaminase 1, Glutamic--pyruvic transaminase 1, GPT, AAT1, GPT1.
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Physical Appearance
Sterile liquid formulation.
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Stability
AAT1 although stable at 10°C for 5 days, should be stored below -18°C.Please prevent freeze-thaw cycles.
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 :
EMAP II HumanDescription:
Endothelial-Monocyte Activating Polypeptide II Human Recombinant
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
Product # :
CYT-607Price :
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Shipped at Room temp
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Description
EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.
Purity
Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.More Info
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Introduction
EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.
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Synonyms
AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized EMAP-II although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EMAP-II should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized EMAP-II in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
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Background
What is the molecular weight/Mw of EMAP II HUMAN Protein?
EMAP II HUMAN Protein has a total Mw of 18.3kDa.
What is the source or expression system of EMAP II HUMAN Protein?
Escherichia Coli.
What is the Purity of EMAP II HUMAN Protein?
EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of EMAP II HUMAN Protein?
Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.
What is the amino acid sequence of EMAP II HUMAN Protein?
SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.
What applications can EMAP II HUMAN Protein be used in?
EMAP II HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EMAP II HUMAN Protein?
The endotoxin level is minimal, EMAP II HUMAN Protein was purified using conventional chromatography techniques
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ENO2 MouseDescription:
Enolase-2 Mouse Recombinant
AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.
Product # :
ENZ-1028Price :
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Description
ENO2 Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 49.7kDa.ENO2 is fused to a 23 amino acid His-tag at N-terminus& purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ENO2 solution (1mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000 pmol/min/µg, and was obtained by measuring the decrease of NAD in absorbance at 340nm resulting from NADH at pH 6.5 at 37°C.More Info
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Introduction
Neuron-specificenolase also caled NSE is a glycolytic isoenzyme which is situated in central and peripheral neurons and neuroendocrine cells. Enolase-2 is released into the CSF when neural tissue is injured. Neoplasms derived from neural or neuroendocrine tissue release Enolase-2 into the blood. Enolase-2 is a useful substance that has been detected in patients with certain tumors, such as neuroblastoma, small cell lung cancer, medullary thyroid cancer, carcinoid tumors, pancreatic endocrine tumors, and melanoma. ENO2 is 1 of the 3 enolase isoenzymes found in mammals. ENO2 isoenzyme, is found in mature neurons and cells of neuronal origin. An exchange from alpha enolase to gamma enolase occurs in neural tissue during development in rats and primates.
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Synonyms
AI837106, D6Ertd375e, Eno-2, NSE, 2-phospho-D-glycerate hydro-lyase, Enolase 2, Neural enolase, Neuron-specific enolase.
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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 MGSMSIEKIW AREILDSRGN PTVEVDLYTA KGLFRAAVPS GASTGIYEAL ELRDGDKQRY LGKGVLKAVD HINSRIAPAL ISSGISVVEQ EKLDNLMLEL DGTENKSKFG ANAILGVSLA VCKAGAAERD LPLYRHIAQL AGNSDLILPV PAFNVINGGS HAGNKLAMQE FMILPVGAES FRDAMRLGAE VYHTLKGVIK DKYGKDATNV GDEGGFAPNI LENSEALELV KEAIDKAGYT EKMVIGMDVA ASEFYRDGKY DLDFKSPADP SRYITGDQLG ALYQDFVRNY PVVSIEDPFD QDDWAAWSKF TANVGIQIVG DDLTVTNPKR IERAVEEKAC NCLLLKVNQI GSVTEAIQAC KLAQENGWGV MVSHRSGETE DTFIADLVVG LCTGQIKTGA PCRSERLAKY NQLMRIEEEL GDEARFAGHN FRNPSVL.
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 :
IYD HumanDescription:
Iodotyrosine Deiodinase Human Recombinant
Iodotyrosine dehalogenase 1, IYD-1, Iodotyrosine Deiodinase, IYD, C6orf71, DEHAL1, iodotyrosine dehalogenase 1 isoform 3, dJ422F24.1, TDH4.
Product # :
ENZ-779Price :
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Description
IYD Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 214 amino acids (24-214 a.a) and having a molecular mass of 25.1kDa.IYD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IYD protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
IYD is an enzyme that catalyzes the oxidative NADPH-dependent deiodination of both mono- and diiodotyrosine although acts more efficiently on monoiodotyrosine. The N-terminus of Iodotyrosine Deiodinase , also known as IYD, plays a role as a membrane anchor. IYD acts during the hydrolysis of thyroglobulin to liberate iodide, which then reenter the hormone-producing pathways.
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Synonyms
Iodotyrosine dehalogenase 1, IYD-1, Iodotyrosine Deiodinase, IYD, C6orf71, DEHAL1, iodotyrosine dehalogenase 1 isoform 3, dJ422F24.1, TDH4.
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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 MGSDRSMEKK KGEPRTRAEA RPWVDEDLKD SSDLHQAEED ADEWQESEEN VEHIPFSHNH YPEKEMVKRS QEFYELLNKR RSVRFISNEQ VPMEVIDNVI RTAGTAPSGA HTEPWTFVVV KDPDVKHKIR KIIEEEEEIN YMKRMGHRWV TDLKKLRTNW IKEYLDTAPI LILIFKQVHG FAANGKKKVH YYNE.
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 :
CHST10 HumanDescription:
Carbohydrate Sulfotransferase 10 Human Recombinant
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
Product # :
ENZ-894Price :
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Description
CHST10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 350 amino acids (28-356 a.a) and having a molecular mass of 41.2kDa.CHST10 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CHST10 protein solution (0.5mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
Carbohydrate Sulfotransferase 10, also known as CHST10 is a member of the sulfotransferase 2 family. CHST10 was first recognized as a sulfotransferase which acts on the human natural killer-1 (HNK-1) glycan. Furthermore, CHST10 is a carbohydrate involved in neurodevelopment as well as synaptic plasticity.
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Synonyms
Carbohydrate Sulfotransferase 10, HNK1ST, HNK-1 Sulfotransferase,HuHNK-1ST, HNK-1ST, EC 2.8.2.-, EC 2.8.2, CHST10.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTFKDPDVYS AKQEFLFLTT MPEVRKLPEE KHIPEELKPT GKELPDSQLV QPLVYMERLE LIRNVCRDDA LKNLSHTPVS KFVLDRIFVC DKHKILFCQT PKVGNTQWKK VLIVLNGAFS SIEEIPENVV HDHEKNGLPR LSSFSDAEIQ KRLKTYFKFF IVRDPFERLI SAFKDKFVHN PRFEPWYRHE IAPGIIRKYR RNRTETRGIQ FEDFVRYLGD PNHRWLDLQF GDHIIHWVTY VELCAPCEIM YSVIGHHETL EDDAPYILKE AGIDHLVSYP TIPPGITVYN RTKVEHYFLG ISKRDIRRLY ARFEGDFKLF GYQKPDFLLN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Cyclophilin D HumanDescription:
Cyclophilin-D Human Recombinant
Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.
Product # :
ENZ-940Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Cyclophilin-D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 178 amino acids and having a molecular mass of 18.9kDa.The Cyclophilin-D is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Cyclophilin-D 0.2µm filtered solution containing PBS pH7.4, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.
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Synonyms
Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.
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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
CSKGSGDPSS SSSSGNPLVY LDVDANGKPL GRVVLELKAD VVPKTAENFR ALCTGEKGFG YKGSTFHRVI PSFMCQAGDF TNHNGTGGKS IYGSRFPDEN FTLKHVGPGV LSMANAGPNT NGSQFFICTI KTDWLDGKHV VFGHVKEGMD VVKKIESFGS KSGRTSKKIV ITDCGQLS.
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 :
NUDT10 HumanDescription:
Nudix Type Motif 10 Human Recombinant
Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.
Product # :
ENZ-126Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NUDT10 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (1-164 a.a.) and having a molecular mass of 19.5kDa.NUDT10 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NUDT10 protein solution (0.5mg/ml) 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
NUDT10 belongs to the Nudix hydrolase family of pyrophosphatases. Nudix hydrolases contain a characteristic Nudix domain and are responsible for catalyzing the hydrolysis of nucleoside diphosphate derivatives. NUDT10 functions as a manganese-dependent polyphosphate phosphohydrolase with an optimum pH of 8.5. NUDT10 protein specifically metabolizes diadendosine-polyphosphates and, to a lesser extent, diphosphoinositol polyphosphates.
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Synonyms
Diphosphoinositol polyphosphate phosphohydrolase 3-alpha, DIPP-3-alpha, DIPP3-alpha, hDIPP3alpha, Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-alpha, Nucleoside diphosphate-linked moiety X motif 10, Nudix motif 10, hAps2, NUDT10, APS2, DIPP3A.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
NUDT10 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Amino Acid Sequence
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG AAVREVYEEA GVKGKLGRLL GVFEQNQDPK HRTYVYVLTV TELLEDWEDS VSIGRKREWF KVEDAIKVLQ CHKPVHAEYL EKLKLGGSPT NGNSMAPSSP DSDPLEHHHH HH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
B3GAT3 HumanDescription:
Beta-1,3-Glucuronyltransferase 3 Human Recombinant
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
Product # :
ENZ-711Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
B3GAT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 330 amino acids (29-335 a.a) and having a molecular mass of 36.4kDa. B3GAT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
B3GAT3 protein solution (1mg/ml) containing 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
Beta-1,3-glucuronyltransferase 3 (B3GAT3) is involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. B3GAT3 has a part in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. B3GAT3 shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc.
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Synonyms
Beta-1,3-glucuronyltransferase 3, GLCATI, Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3, Glucuronosyltransferase I, GlcAT-I, GlcUAT-I, B3GAT3, UDP-GlcUA:Gal beta-1,3-Gal-R glucuronyltransferase.
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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 MGSQPCDCLP PLRAAAEQLR QKDLRISQLQ AELRRPPPAP AQPPEPEALP TIYVVTPTYA RLVQKAELVR LSQTLSLVPR LHWLLVEDAE GPTPLVSGLL AASGLLFTHL VVLTPKAQRL REGEPGWVHP RGVEQRNKAL DWLRGRGGAV GGEKDPPPPG TQGVVYFADD DNTYSRELFE EMRWTRGVSV WPVGLVGGLR FEGPQVQDGR VVGFHTAWEP SRPFPVDMAG FAVALPLLLD KPNAQFDSTA PRGHLESSLL SHLVDPKDLE PRAANCTRVL VWHTRTEKPK MKQEEQLQRQ GRGSDPAIEV.
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 :
CBR1 HumanDescription:
Carbonyl Reductase-1 Human Recombinant
CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.
Product # :
ENZ-415Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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Description
Recombinant Human CBR1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 277 amino acids (1-277 a.a) and having a molecular mass of 30 kDa. CBR1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CBR1 protein contains 20mM Tris-HCl buffer pH-8.5, and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
CBR1 is one of numerous monomeric, NADPH-dependent oxidoreductases having ubiquistly specificity for carbonyl compounds. CBR1 is broadly distributed in human tissues. CBR1 metabolizes toxic environmental quinones and pharmacological relevant substrates. CBR1 converts prostaglandin E2 to prostaglandin F2-alpha.
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Synonyms
CBR, hCBR1, SDR21C1, CBR1, Carbonyl reductase [NADPH] 1, NADPH-dependent carbonyl reductase 1, Prostaglandin-E(2) 9-reductase, Prostaglandin 9-ketoreductase, 15-hydroxyprostaglandin dehydrogenase [NADP+], CRN.
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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
MSSGIHVALV TGGNKGIGLA IVRDLCRLFS GDVVLTARDV TRGQAAVQQL QAEGLSPRFH QLDIDDLQSI RALRDFLRKE YGGLDVLVNN AGIAFKVADP TPFHIQAEVT MKTNFFGTRD VCTELLPLIK PQGRVVNVSS IMSVRALKSC SPELQQKFRS ETITEEELVG LMNKFVEDTK KGVHQKEGWP SSAYGVTKIG VTVLSRIHAR KLSEQRKGDK ILLNACCPGW VRTDMAGPKA TKSPEEGAET PVYLALLPPD AEGPHGQFVS EKRVEQW.
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.