APEX1 (R221) polyclonal antibody

The role of transcription factors in the regulation of gene expression is well established. Although the activity of these factors can be regulated by phosphorylation, evidence has indicated regulation of DNA binding mediated by changes in reduction-oxidation (redox) status. Mutational analysis has identified a single conserved cysteine residue mapping within the DNA binding domains of Fos and Jun. Chemical oxidation or modification of this cysteine residue inhibits the DNA binding activity of Fos and Jun. A similar mode of regulation has been recently proposed for other nuclear transcription factors. Oxidation is reversible by these compounds or by a cellular redox/DNA repair protein identified originally as Ref-1 (redox factor 1) . Ref-1 is identical to a previously characterized DNA repair enzyme designated HAP1, APE or APEX.

AP lyase; APE 1; APE; APE-1; APEN; APEX 1; APEX; APEX nuclease (multifunctional DNA repair enzyme) 1; Apex nuclease 1; Apex nuclease; APEX1; Apurinic endonuclease; Apurinic-apyrimidinic endonuclease 1; Apurinic/apyrimidinic (abasic) endonuclease; Apurinic/apyrimidinic endonuclease 1; Apurinic/apyrimidinic exonuclease; APX; BAP1; Deoxyribonuclease (apurinic or apyrimidinic) ; DNA (apurinic or apyrimidinic site) lyase; DNA- (apurinic or apyrimidinic site) lyase; mit

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE) .

Western blot (WB) analysis of APEX1/Ref-1 (R221) pAb at 1:500 dilution Lane1:HepG2 whole cell lysate (40ug) Lane2:PC3 whole cell lysate (40ug) Lane3:MEF whole cell lysate (40ug) Lane4:C6 whole cell lysate (40ug)