Endonuclease V, E. coli
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.
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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.
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).
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).
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.
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).
2,500 units, 10 U/µl
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