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The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
MYH (mutY homolog (E. coli )) is a DNA glycosylase mismatch repair enzyme that in conjunction with mutM (OGG1), cleaves adenine residues paired with either oxidized (8-hydroxyguanines) or non-modified guanines in order to correct A/G and A/C mismatches. Repair of most modified and mispaired bases in the genome is initiated by DNA glycosylases, which bind and cleave N-glycosyl bonds to initiate base excision repair. MYH is crucial for the avoidance of mutations resulting from oxidative DNA damage. Multiple N-terminal splice variants of MYH exist in mammalian cells. Increasing levels of MYH in A549 cells exposed to oxygen and infrared radiation leads to improvements in cell survival. Biallelic MYH germ-line mutations predispose humans to colorectal adenomas and carcinomas. MYH is abundant in neurons where mitochondrial genomes exposed to reactive oxygen species (ROS) that damage DNA must maintain integrity over the entire mammalian life span.
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Protein Aliases: A/G-specific adenine DNA glycosylase; Adenine DNA glycosylase; adenine-DNA glycosylase; hMYH; MGC4416; mMYH; MutY homolog; mutY homolog alpha; mutY-like protein; OTTHUMP00000009098; OTTHUMP00000009102; rMYH; RP4-534D1.2; the full-length form type A, 5' region
Gene Aliases: 5730495A01Rik; MUTYH; Mutyha; Mutyhalpha; Mutyhb; Mutyhbeta; Mutyhc; MYH
Molecular Function: DNA glycosylase