Białka naprawcze DNA

Uracyl-DNA glikozydaza katalizuje hydrolizę wiązania N-glikozydycznego pomiędzy uracylem a cukrem, pozostawiając miejsce apurynowe w jedno- lub dwuniciowym DNA zawierającym uracyl. Enzym nie wykazuje mierzalnej aktywności wobec krótkich oligonukleotydów (<6 zasad) ani substratów RNA.

2,500 units, 10 U/µl

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.

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).

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).

The MutS DNA mismatch protein recognizes heteroduplex DNAs containing mispaired or unpaired bases.