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Recombinant E. coli G/U Mismatch-Specific DNA Glycosylase/Mug

Recombinant E. coli G/U Mismatch-Specific DNA Glycosylase/Mug Recombinant E. coli G/U Mismatch-Specific DNA Glycosylase/Mug

Instruction Manual!

Product name: Recombinant E. coli G/U Mismatch-Specific DNA Glycosylase/Mug
Source:E.coli
Purity:Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 2.5mM β-ME, 1mM PMSF, 50% Glycerol, pH 8.0.
Applications:Applications:SDS-PAGE; WB; ELISA; IP.
Storage:Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:100ug/50ug/200ug/1mg/1g
Source E.coli
Description Recombinant E.coli Mug is produced by our E.coli expression system and the target gene encoding Met1-Arg168 is expressed with a 6His tag at the C-terminus.
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 TrisHCl, 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 reducing SDS-PAGE.
Endotoxin Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
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.

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