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Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. Additionally we are shipping APEX2 Antibodies (53) and APEX2 Kits (2) and many more products for this protein.
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APE2 associates with Chk1 (show CHEK1 Proteins); a serine residue (S86) in the Chk1 (show CHEK1 Proteins)-binding motif of APE2 is essential for Chk1 (show CHEK1 Proteins) phosphorylation, indicating a Claspin-like but distinct role for APE2 in ATR-Chk1 (show CHEK1 Proteins) signaling.
Determinants in nuclease (show DCLRE1C Proteins) specificity of Ape1 (show APEX1 Proteins) and Ape2, human homologues of Escherichia coli exonuclease (show EXO1 Proteins) III
Ape2 exhibits strong 3'-5' exonuclease and 3'-phosphodiesterase activities and has only a very weak AP-endonuclease activity.
Ape2 may be involved in repair of oxidative DNA damage and PCNA (show PCNA Proteins)-dependent repair synthesis.
expression of Apex 2 in chondrocytes appears to be associated with the degeneration of articular cartilage in osteoarthritis.
Results indicate a role for apurinic/apyrimidinic endonuclease (APE (show RPLP0 Proteins)) 2 (Apex2) in the protection of germinal center (GC) cells from activation-induced cytidine deaminase (show AICDA Proteins) (AID)-independent damage.
data provide new insight into error-prone repair of AID-induced lesions, which we propose is facilitated by down-regulation of APE1 (show APEX1 Proteins) and up-regulation of APE2 expression in germinal center B cells.
Extensive analysis of bone marrow hematopoiesis in APE2-deficient mice finds inhibition of the pro-B to pre-B lymphocyte (show AKAP17A Proteins) transition, due to a p53 (show TP53 Proteins)-dependent DNA damage response, independent from its ubiquitous and essential homolog APE1 (show APEX1 Proteins).
APEX2 is required for proper cell cycle progression of proliferating lymphocytes.
Both APE1 (show APEX1 Proteins) and APE2 function in antibody switch recomibination, resulting in double stranded breaks necesary for this recombination.
The present study clearly demonstrates that APEX2-null lymphocytes have a higher frequency of DNA breaks, indicating that APEX2 may play an important role(s) during their generation and/or repair.
Apex2 is required for efficient somatic hypermutation of immunoglobulin genes.
Apurinic/apyrimidinic (AP) sites occur frequently in DNA molecules by spontaneous hydrolysis, by DNA damaging agents or by DNA glycosylases that remove specific abnormal bases. AP sites are pre-mutagenic lesions that can prevent normal DNA replication so the cell contains systems to identify and repair such sites. Class II AP endonucleases cleave the phosphodiester backbone 5' to the AP site. This gene encodes a protein shown to have a weak class II AP endonuclease activity. Most of the encoded protein is located in the nucleus but some is also present in mitochondria. This protein may play an important role in both nuclear and mitochondrial base excision repair. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene.
DNA-(apurinic or apyrimidinic site) lyase 2
, APEX nuclease (apurinic/apyrimidinic endonuclease) 2
, DNA-(apurinic or apyrimidinic site) lyase 2-like
, AP endonuclease 2
, AP endonuclease XTH2
, apurinic/apyrimidinic endonuclease-like 2
, APEX nuclease 2
, apurinic-apyrimidinic endonuclease 2