Methionine S-oxide reductase (S-form oxidizing),
peptide-Methionine sulfoxide reductase,
|Related Categories||Cell Biology, Cell Signaling and Neuroscience, Cell Stress, Enzymes, Nitric Oxide and Cell Stress,|
|recombinant||expressed in E. coli|
|form||buffered aqueous solution|
|shipped in||wet ice|
|Gene Information||human ... MSRA(4482)|
The assay is based on the ability of MsrA to reduce methionine sulfoxide, which is measured by monitoring the level of NADPH oxidation in the presence of a thioredoxin-regenerating system.
One unit will cause the oxidation of 1 μmole of NADPH per minute at 37 °C at pH 7.6.
Supplied in a solution of 50 mM Tris, pH 7.6, and 150 mM NaCl.
Methionine (Met) residues of proteins are readily oxidized to methionine sulfoxide (MetO), especially under oxidative stress conditions. Oxidative alteration of Met to R/S-Met(O) sterioisomers is reversed by methionine sulfoxide reductases: MsrA reduces S-MetO and MsrB reduces R-MetO, which may prevent irreversible oxidative protein damage and thus extend an organism′s life span.1,2 A series of proteins have been identified as substrates of MsrA, these include Calmodulin and HIV protease. There is evidence showing a connection between MsrA and Alzheimer′s disease.3
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