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E. coli Mismatch Uracil DNA Glycosylase (Mug protein), also known as G/U mismatch-specific DNA glycosylase, is an 18 kDa constitutively expressed protein which belongs to the TDG/mug DNA glycosylase family. It has been proposed that the Mug protein excises 3,N4-ethenocytosine and removes the uracil base from mismatches in the order of U:G>U:A, although the biological role remains unclear. Uracil bases in DNA can arise from deamination of cytosine giving rise to increased spontaneous mutations. The enzyme Uracil-N-Glycosylase removes uracil from the DNA leaving an AP site. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar-phosphate backbone of the DNA and the mispaired base. The complementary strand guanine functions in substrate recognition. Required for DNA damage lesion repair in stationary-phase cells.
| Source | E. coli |
| Names | G/U Mismatch-Specific DNA Glycosylase, Double-Strand-Specific Uracil Glycosylase, Mismatch-Specific Uracil DNA-Glycosylase, MUG, mug, ygjF |
| Accession # | P0A9H1 |
| Formulation | Supplied as a 0.2 μM filtered solution of 20mM Tris-HCl, 2.5mM β-ME, 1mM PMSF, 50% Glycerol, pH 8.0 |
| Shipping | The product is shipped on dry ice/ice packs. |
| Storage | Store at < -20°C, stable for 6 months after receipt. Please minimize freeze-thaw cycles. |
| Purity | Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE. |
| Amino Acid Sequence | MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQLKPQEAQHLLDYRCG VTKLVDRPTVQANEVSKQELHAGGRKLIEKIEDYQPQALAILGKQAYEQGFSQRGAQWGKQTLTI GSTQIWVLPNPSGLSRVSLEKLVEAYRELDQALVVRGRLEHHHHHH |