Anti-APEX2 Antibody Picoband® Fluoro488 Conjugated

APEX2, also called apurinic/apyrimidinic endonuclease like-2, is a member of the apurinic/apyrimidinic (AP) family of endonucleases that initiate the repair of AP sites formed by spontaneous hydrolysis of the N-glycosylic bond, mutagen-induced base release, or damaged-base excision by a DNA repair glycosylase. RT-PCR detected APEX2 expression in HeLa cells, Jurkat cells, and human kidney, brain and fetal brain tissue. The APEX2 gene is mapped to chromosome Xp11.21. APEX2 participates in both nuclear and mitochondrial base excision repair (BER) and it can play a role in processing 3-prime-damaged termini or 3-prime-mismatched nucleotides. Additionally, APEX2 displayed weaker AP site-specific and 3-prime nuclease activities compared to APEX1.

DNA- (apurinic or apyrimidinic site) lyase 2;3.1.-.-;4.2.99.18; AP endonuclease XTH2; APEX nuclease 2; APEX nuclease-like 2; Apurinic-apyrimidinic endonuclease 2; AP endonuclease 2; APEX2; APE2, APEXL2, XTH2

Function as a weak apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Displays also double-stranded DNA 3'-5' exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5' exonuclease activity on 3'-recessed heteroduplex DNA and is able to remove mismatched nucleotides preferentially. Shows fairly strong 3'-phosphodiesterase activity involved in the removal of 3'-damaged termini formed in DNA by oxidative agents. In the nucleus functions in the PCNA-dependent BER pathway. Required for somatic hypermutation (SHM) and DNA cleavage step of class switch recombination (CSR) of immunoglobulin genes. Required for proper cell cycle progression during proliferation of peripheral lymphocytes. .

1. Burkovics, P., Szukacsov, V., Unk, I., Haracska, L.Human Ape2 protein has 3-5-prime exonuclease activity that acts preferentially on mismatched base pairs.Nucleic Acids Res. 34: 2508-2515, 2006. 2. Hadi, M. Z., Ginalski, K., Nguyen, L. H., Wilson, D. M., III.Determinants in nuclease specificity of Ape1 and Ape2, human homologues of Escherichia coli exonuclease III.J. Molec. Biol. 316: 853-866, 2002. 3. Tsuchimoto, D., Sakai, Y., Sakumi, K., Nishioka, K., Sasaki, M., Fujiwara, T., Nakabeppu, Y.Human APE2 protein is mostly localized in the nuclei and to some extent in the mitochondria, while nuclear APE2 is partly associated with proliferating cell nuclear antigen.Nucleic Acids Res. 29: 2349-2360, 2001.