MSRA Antibody (N-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9UJ68 |
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Clone Names | 80902036 |
Gene ID | 4482 |
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Other Names | Mitochondrial peptide methionine sulfoxide reductase, Peptide-methionine (S)-S-oxide reductase, Peptide Met(O) reductase, Protein-methionine-S-oxide reductase, PMSR, MSRA |
Target/Specificity | The synthetic peptide sequence used to generate the antibody AP7321a was selected from the N-term region of human MSRA. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | MSRA |
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Function | Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. |
Cellular Location | [Isoform 1]: Mitochondrion. [Isoform 3]: Cytoplasm. Nucleus. |
Tissue Location | Ubiquitous. Highest expression in adult kidney and cerebellum, followed by liver, heart ventricles, bone marrow and hippocampus |
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Provided below are standard protocols that you may find useful for product applications.
Background
MSRA is ubiquitous and highly conserved. This protein 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. The protein's proposed function is the repair of oxidative damage to proteins to restore biological activity.
References
Pascual,I., Larrayoz,I.M. Genomics 93 (1), 62-71 (2009)Schallreuter,K.U., Rubsam,K. J. Invest. Dermatol. 128 (4), 808-815 (2008)Picot,C.R., Perichon,M. FEBS Lett. 558 (1-3), 74-78 (2004)Vougier,S., Mary,J. Biochem. J. 373 (PT 2), 531-537 (2003)
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