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| Alternative Name : |
Methionine-R-sulfoxide reductase B1, MsrB1, Selenoprotein X, SelX, SEPX1, SELR, SELX, HSPC270, MGC3344. |
| Amount : |
10 µg |
Source : Escherichia Coli.
SEPX1 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 136 amino acids (1-116 a.a.) and having a molecular mass of 14.8kDa. In bacteria, the selenocystein (Sec/U) element is positioned directly following the UGA codon within the reading frame for the selenoprotein so we mutated Sec-95 to Cys. The SEPX1 is purified by proprietary chromatographic techniques.
Methionine sulfoxide reductase B1 (SEPX1 or MSRB1), is a selenoprotein that contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that usually signals translation termination. SEPX1 is a member of the methionine sulfoxide reductase B (MsrB) family, and is expressed in an assortment of adult and fetal tissues. MSRs (Methionine sulfoxide reductases) catalyze the reduction of free and protein-bound methionine sulfoxides to corresponding methionines. The oxidation of methionine by ROS creates a diastereomeric mixture of methionine-S-sulfoxide (Met-S-SO) and methionine-R-sulfoxide (Met-R-SO). Two separate enzyme families evolved for reduction of these sulfoxides, with methionine-S-sulfoxide reductase (MsrA) being stereospecific for Met-S-SO and methionine-R-sulfoxide reductase (MsrB) for Met-R-SO.
