| Product Name | mug, 1-168aa |
|---|---|
| Description | G/U mismatch-specific DNA glycosylase, xanthine DNA glycosylase, also known as mug, 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. 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. Recombinant E.coli mug protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | G/U mismatch-specific DNA glycosylase, xanthine DNA glycosylase, dug, ECK3058, JW3040, ygjF |
| Host | E. coli |
| Molecular Weight | 33.8kDa (298aa) confirmed by MALDI-TOF |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSMVEDILA PGLRVVFCGI NPGLSSAGTG FPFAHPANRF WKVIYQAGFT DRQLKPQEAQ HLLDYRCGVT KLVDRPTVQA NEVSKQELHA GGRKLIEKIE DYQPQALAIL GKQAYEQGFS QRGAQWGKQT LTIGSTQIWV LPNPSGLSRV SLEKLVEAYR ELDQALVVRG R |
| Tag | His-tag |
| Reactivity | E. coli |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH 8.0) containing 0.1M NaCl, 30% glycerol, 1mM DTT |
| Concentration | 0.5 mg/ml (determined by Bradford assay) |
| Purity | > 90% by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -2°C or -7°C. Avoid repeated freezing and thawing cycles. |
| References | Lee HW., et al. (2010) J Biol Chem. 285(53):41483-90 Gallinari P., et al. (1996) Nature. 383(6602):735-8. |
| Background | G/U mismatch-specific DNA glycosylase, xanthine DNA glycosylase, also known as mug, 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. 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. Recombinant E.coli mug protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Supplier | ARP |
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