Home  >  Products  >  MSRA, Recombinant, Human, aa24-235, His-Tag (Methionine Sulfoxide Reductase A, Peptide Methionine Sulfoxide Reductase, Peptide-methionine (S)-S-oxide Reductase, Peptide Met(O) Reductase, Protein-methionine-S-oxide Reductase, PMSR)

MSRA, Recombinant, Human, aa24-235, His-Tag (Methionine Sulfoxide Reductase A, Peptide Methionine Sulfoxide Reductase, Peptide-methionine (S)-S-oxide Reductase, Peptide Met(O) Reductase, Protein-methionine-S-oxide Reductase, PMSR)

Cat no: 045444


Supplier: United States Biological
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MSRA (methionine sulfoxide reductase A ) belongs to the MsrA Met sulfoxide reductase family. This enzyme has an important function as a repair enzyme for proteins that have been inactivated by oxidation. It catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. In enzymology, a MSRA is an enzyme that catalyzes the chemical reaction. The 3 substrates of this enzyme are peptide-L-methionine, thioredoxin disulfide, and H2O, whereas its two products are peptide-L-methionine (R)-S-oxide and thioredoxin. Source: Recombinant corresponding to aa24-235 from human MSRA, fused to His-tag at N-terminus, expressed in E.coli. Molecular Weight: ~26.2kD (237aa) confirmed by MALDI-TOF AA Sequence: MGSSHHHHHH SSGLVPRGSH MGSHMGNSAS NIVSPQEALP GRKEQTPVAA KHHVNGNRTV EPFPEGTQMA VFGMGCFWGA ERKFWVLKGV YSTQVGFAGG YTSNPTYKEV CSEKTGHAEV VRVVYQPEHM SFEELLKVFW ENHDPTQGMR QGNDHGTQYR SAIYPTSAKQ MEAALSSKEN YQKVLSEHGF GPITTDIREG QTFYYAEDYH QQYLSKNPNG YCGLGGTGVS CPVGIKK Storage and Stability: May be stored at 4 degrees C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Aliquots are stable for 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Catalogue number: 045444
Size: 100ug
Form: Supplied as a liquid in 20mM Tris-HCl, pH 8.0, 1mM DTT, 50mM sodium chloride, 10% glycerol.
Purity: ~90% (SDS-PAGE)
References: 1. Boschi-Muller S, et al. (2005) Biochim. Biophys. Acta. 1703 (2): 231-8. 2. Hansel A., et al. (2005) Biochim. Biophys. Acta 1703:239-247.

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