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SEPX1 encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. Additionally we are shipping Selenoprotein X, 1 Antibodies (17) and Selenoprotein X, 1 Kits (9) and many more products for this protein.
Showing 10 out of 18 products:
Human SEPX1 Protein expressed in Escherichia coli (E. coli) - ABIN667227
Liang, Fomenko, Hua, Kaya, Gladyshev: Diversity of protein and mRNA forms of mammalian methionine sulfoxide reductase B1 due to intronization and protein processing. in PLoS ONE 2010
Show all 2 references for ABIN667227
Silencing the expression of the main Msr elements-MsrA, MsrB1, or MsrB2 exacerbates sensitivity toward oxidative stress.
MsrB1 protected human lens epithelial cells against the peroxynitrite-induced F-actin disruption
MsrB1 plays important roles in protecting HLE (show ELANE Proteins) cell mitochondria against oxidative damage and inhibits oxidative stress-induced (show SQSTM1 Proteins) apoptosis in diabetic cataracts by scavenging ROS (show ROS1 Proteins).
The results demonstrate that in human lens epithelial cells MsrB1 may play important roles in regulating redox balance and mitigating endoplasmic reticulum stress.
The studies in mouse show that MsrB (show MSRB2 Proteins) is a selenoprotein that exhibits high specificity for reduction of the R forms of free and protein-bound methionine sulfoxide.
study identified the regulatory role of MsrB1 as a Mical antagonist in orchestrating actin dynamics and macrophage function
MsrB1/Trx (show TXN Proteins) complex was studied in attempt to understand MsrB1 reduction mechanism. Using NMR data, molecular mechanics, protein docking & molecular dynamics simulations, found that intermediate MsrB1/Trx (show TXN Proteins) complex is stabilized by interprotein beta-layer.
Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance.
Insights into function, catalytic mechanism, and fold evolution of selenoprotein methionine sulfoxide reductase B1 through structural analysis.
Study characterized unexpected diversity of protein and mRNA forms of mammalian selenoprotein MsrB1.
MsrB1 recovers TRPM6 (show TRPM6 Proteins) channel activity by reducing the oxidation of Met(1755) and could, thereby, function as a modulator of TRPM6 (show TRPM6 Proteins) during oxidative stress.
Data show that methionine sulfoxide reductase (Msr (show MSR1 Proteins))B1, but not MsrA (show MSR1 Proteins), is the major methionine sulfoxide reductase in liver of mice and it is among the proteins that are most easily regulated by dietary selenium.
The chemical shift index for MsrB1 indicates that the beta-sheets are the main element for the protein secondary structure.
This gene encodes a selenoprotein, which contains a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded by the UGA codon that normally signals translation termination. The 3' UTR of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a Sec codon rather than as a stop signal. This protein belongs to the methionine sulfoxide reductase (Msr) protein family which includes repair enzymes that reduce oxidized methionine residues in proteins. The protein encoded by this gene is expressed in a variety of adult and fetal tissues and localizes to the cell nucleus and cytosol.
methionine-R-sulfoxide reductase B1
, methionine-R-sulfoxide reductase B1-A
, selenoprotein X, 1
, selenoprotein X, 1a
, selenoprotein X-A
, selenoprotein R
, selenoprotein X 1
, Methionine-R-sulfoxide reductase B1