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Recombinant E. coli Double-Stranded Uracil-DNA Glycosylase His Protein

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SDS-Page: Recombinant E. coli Double-Stranded Uracil-DNA Glycosylase Protein [NBP2-75954] - Recombinant E. coli Double-Stranded Uracil-DNA Glycosylase Protein

Product Details

Summary
Reactivity EcSpecies Glossary
Applications PAGE
Concentration
0.5 mg/ml

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Recombinant E. coli Double-Stranded Uracil-DNA Glycosylase His Protein Summary

Description
A recombinant protein with a N-Terminal His-tag and corresponding to the amino acids 1-168 of E.coli Double-Stranded Uracil-DNA Glycosylase

Source: E.coli

Amino Acid Sequence: MGSSHHHHHH SSGLVPRGSH MGSMVEDILA PGLRVVFCGI NPGLSSAGTG FPFAHPANRF WKVIYQAGFT DRQLKPQEAQ HLLDYRCGVT KLVDRPTVQA NEVSKQELHA GGRKLIEKIE DYQPQALAIL GKQAYEQGFS QRGAQWGKQT LTIGSTQIWV LPNPSGLSRV SLEKLVEAYR ELDQALVVRG R

Source
E. coli
Protein/Peptide Type
Recombinant Protein
Purity
>90%, by SDS-PAGE

Applications/Dilutions

Dilutions
  • SDS-Page
Theoretical MW
21.1 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

Storage
Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.
Buffer
20 mM Tris-HCl buffer (pH 8.0), 0.1 M NaCl, 20% glycerol
Preservative
No Preservative
Concentration
0.5 mg/ml
Purity
>90%, by SDS-PAGE

Alternate Names for Recombinant E. coli Double-Stranded Uracil-DNA Glycosylase His Protein

  • double-strand uracil-DNA glycosylase
  • Double-strand-specific uracil glycosylase
  • dsDNA specific UDG
  • DsUDG
  • EC 3.2.2.28
  • G/U mismatch-specific DNA glycosylase
  • G:T/U mismatch-specific DNA glycosylase
  • Mismatch-specific uracil DNA glycosylase
  • Mug
  • Xanthine DNA glycosylase

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.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

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