| Catalog# |
C152 |
| Source |
E.coli |
| Description |
Recombinant E. coli G/U Mismatch-Specific DNA Glycosylase/Mug is produced with our E.coli expression system. The target protein is expressed with sequence (Met1-Arg168) of E.coli Mug. |
| 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. |
| Endotoxin |
Less than 0.1 ng/µg (1 IEU/µg) |
| Amino Acid Sequence |
MVEDILAPGLRVVFCGINPGLSSAGTGFPFAHPANRFWKVIYQAGFTDRQLKPQEAQHLLDYRCG VTKLVDRPTVQANEVSKQELHAGGRKLIEKIEDYQPQALAILGKQAYEQGFSQRGAQWGKQTLTI GSTQIWVLPNPSGLSRVSLEKLVEAYRELDQALVVRGRLEHHHHHH
|
| Background |
E. coli Mismatch Uracil DNA Glycosylase (Mug protein) 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. It is required for DNA damage lesion repair in stationary-phase cells. |
