Endonuclease VIII, E. coli
Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site).
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Description
Human Recombinant Alkyl Adenine DNA Glycosylase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).
MPG is fused to an 8 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Applications
Single cell gel electrophoresis (Comet Assay)
Alkaline elution
Alkaline unwinding
Source
E. coli
Purity
> 95 % as determined by SDS-PAGE
Storage
-80 Avoid repeated freeze-thaw cycles.
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Endonuclease VIII from E. coli acts as both an N-glycosylase and an AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating an apurinic (AP site).
Endonuclease III (Nth) protein from E. coli acts as both N-glycosylase and a AP-lyase. The N-glycosylase activity releases damaged pyrimidines from double-stranded DNA, generating a basic (AP site).
Endonuclease V, (Endo V) is a 3'-endonuclease involved in DNA repair, which initiates removal of deaminated bases from damaged DNA, including uracil, hypoxanthine, and xanthine.
The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases.
Bovine Serum Albumin (BSA) has many uses as a carrier protein and as a stabilizing agent in enzymatic reactions. MCLAB’s Ultrapure BSA is a "non-acetylated" BSA, pure enough to use when the integrity of DNA or RNA is essential. It has been tested for DNase, RNase, endonuclease, protease, peroxidase, and alkaline phosphatase activity, and assayed for fluorescence background.
Human Recombinant Alkyl Adenine DNA Glycosylase produced in E.Coli is a single, non-glycosylated polypeptide chain containing 306 amino acids (1-298 a.a.) and having a molecular mass of 33.9kDa (Molecular weight on SDS-PAGE will appear higher).
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