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This protein is ubiquitous and highly conserved. Additionally we are shipping MSRA Antibodies (50) and MSRA Kits (11) and many more products for this protein.
Showing 10 out of 68 products:
Escherichia coli (E. coli) MSRA Protein expressed in Escherichia coli (E. coli) - ABIN667438
Kuschel, Hansel, Schönherr, Weissbach, Brot, Hoshi, Heinemann: Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). in FEBS letters 1999
Show all 2 references for ABIN667438
Human MSRA Protein expressed in Escherichia coli (E. coli) - ABIN1098294
Hansel, Heinemann, Hoshi: Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. in Biochimica et biophysica acta 2005
Show all 2 references for ABIN1098294
Results suggest that lower MsrA (show MSR1 Proteins) activity modifies Amyloid-beta solubility properties and causes mitochondrial dysfunction in a mouse model of Alzheimer's disease.
MsrA (show MSR1 Proteins) acts as a negative regulator of vascular smooth muscle cell proliferation and neointimal hyperplasia after vascular injury through control of the Ras/Raf (show RAF1 Proteins)/ERK1 (show MAPK3 Proteins)/ERK2 (show MAPK1 Proteins) signaling pathway.
ARD1 (show ARD1A Proteins) has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA (show MSR1 Proteins).
These results suggest that COMT (show COMT Proteins) activity may be reduced by methionine oxidation, and point to Msr (show MSR1 Proteins) as a key molecular determinant for the modulation of COMT (show COMT Proteins) activity in the brain.
The MsrA (show MSR1 Proteins) and protein oxidation play a role in the regulation of glucose homeostasis.
MsrA (show MSR1 Proteins) protects the kidney against I/R injury, and that this protection is associated with reduced oxidative stress and inflammatory responses.
MsrA (show MSR1 Proteins) overexpression in MsrA (show MSR1 Proteins)-depleted cells led to the reduction of increased HO-1 (show HMOX1 Proteins) expression, and suppressed nuclear accumulation of Nrf2 (show NFE2L2 Proteins).
Mammalian and yeast Msra (show MSR1 Proteins) reduced free methionine sulfoxide much more efficiently than Msrb (show MSRB2 Proteins).
Data show that glutaredoxin (show GRX1 Proteins) acts as a reductant for methionine sulfoxide reductases A and B (MsrA (show MSR1 Proteins) and MsrB (show MSRB2 Proteins)) with or without resolving cysteine.
Characterization and solution structure of mouse myristoylated methionine sulfoxide reductase A.
this study we have identified, for the first time, compounds structurally related to the natural products fusaricidins that markedly activate recombinant bovine and human MsrA and human MsrB (show MSRB2 Proteins).
The association of MsrA haplotypes with executive functions indicated that MsrA is associated with executive function defects in bipolar I disorder patients.
Silencing the expression of the main Msr elements-MsrA, MsrB1, or MsrB2 exacerbates sensitivity toward oxidative stress.
ARD1 (show TRIM23 Proteins) has a crucial role in the cellular response to oxidative stress as a bona fide regulator of MSRA.
The functional MSRA rs10903323 G/A polymorphism is associated with coronary artery disease development.
We hypothesize that the activity of MsrA can be employed as a marker for the isolation of stem and progenitor cell subpopulations for cell therapy applications.
The MSRA rs10903323 G/A variant allele is associated with Rheumatoid Arthritis development, especially among male patients, older patients, C-Reactive Protein (show CRP Proteins)-positive patients, and anti-cyclic citrullinated peptide negative patients.
The MSRA rs10903323 gene polymorphism may be implicated in the increased risk to develop cardiovascular events, in particular ischaemic heart disease, observed in rheumatoid arthritis patients.
Mammalian and yeast MSRA reduced free methionine sulfoxide much more efficiently than MSRB (show MSRB2 Proteins).
Data show that glutaredoxin (show GRX1 Proteins) acts as a reductant for methionine sulfoxide reductases A and B (MsrA and MsrB (show MSRB2 Proteins)) with or without resolving cysteine.
The results indicate that thionein (T), which is formed when the zinc is removed from zinc-containing metallothionein (show MT Proteins) (Zn-MT), can function as a reducing system for the Msr (show MTRR Proteins) proteins because of its high content of cysteine residues.
This protein is ubiquitous and highly conserved. It carries out the enzymatic reduction of methionine sulfoxide to methionine. Human and animal studies have shown the highest levels of expression in kidney and nervous tissue. Its proposed function is the repair of oxidative damage to proteins to restore biological activity. Three transcript variants encoding different isoforms have been found for this gene.
, mitochondrial peptide methionine sulfoxide reductase
, peptide Met(O) reductase
, peptide methionine sulfoxide reductase
, peptide-methionine (S)-S-oxide reductase
, protein-methionine-S-oxide reductase
, cytosolic methionine-S-sulfoxide reductase
, peptide met (O) reductase