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Thioredoxin Reductase E.Coli Recombinant ( TRXR E.Coli )

DescriptionTRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard

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Data sheet

Formulation TRXR E.Coli solution containing 20mM Tris HCl pH-8, 1mM DTT, and 10% glycerol.
Purity Greater than 90% as determined by SDS-PAGE.
Description TRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated,polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard chromatography.
Protein Background TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.
Expression host Escherichia Coli.
Synonyms TRXB, TRXR, Thioredoxin Reductase.
Reagent Appearance Sterile filtered colorless solution.
Stability Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino acid sequence MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.
Biological Activity Specific activity is 4-5 units/ml, and was measured in a coupled assay with DTNB and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.

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