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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. Zusätzlich bieten wir Ihnen APEX2 Antikörper (60) und APEX2 Kits (2) und viele weitere Produktgruppen zu diesem Protein an.
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APE2 associates with Chk1 (zeige CHEK1 Proteine); a serine residue (S86) in the Chk1 (zeige CHEK1 Proteine)-binding motif of APE2 is essential for Chk1 (zeige CHEK1 Proteine) phosphorylation, indicating a Claspin-like but distinct role for APE2 in ATR-Chk1 (zeige CHEK1 Proteine) signaling.
Determinants in nuclease (zeige DCLRE1C Proteine) specificity of Ape1 (zeige APEX1 Proteine) and Ape2, human homologues of Escherichia coli exonuclease (zeige EXO1 Proteine) 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 (zeige PCNA Proteine)-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 (zeige RPLP0 Proteine)) 2 (Apex2) in the protection of germinal center (GC) cells from activation-induced cytidine deaminase (zeige AICDA Proteine) (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 (zeige APEX1 Proteine) 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 (zeige AKAP17A Proteine) transition, due to a p53 (zeige TP53 Proteine)-dependent DNA damage response, independent from its ubiquitous and essential homolog APE1 (zeige APEX1 Proteine).
APEX2 is required for proper cell cycle progression of proliferating lymphocytes.
Both APE1 (zeige APEX1 Proteine) 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