The antiserum was produced against synthesized Acetyl-peptide derived from human APE1 around the Acetylation site of Lys7. AA range:1-50

Acetyl-Ref-1 (K7) Polyclonal Antibody detects endogenous levels of Ref-1 protein only when acetylated at K7.The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):RGkKG

APEX1

DNA-(apurinic or apyrimidinic site) lyase

APEX1 ;
APE ;
APE1 ;
APEX ;
APX ;
HAP1 ;
REF1 ;
DNA- ;
apurinic or apyrimidinic site ;
lyase ;
APEX nuclease ;
APEN ;
Apurinic-apyrimidinic endonuclease 1 ;
AP endonuclease 1 ;
APE-1 ;
REF-1 ;
Redox factor-1

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 the major AP endonuclease in human cells. Splice variants have been found for this gene; all encode the same protein. [provided by RefSeq, Jul 2008],

Catalytic activity:The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.,Function:Repairs oxidative DNA damages in vitro. May have a role in protection against cell lethality and suppression of mutations. Removes the blocking groups from the 3'-termini of the DNA strand breaks generated by ionizing radiations and bleomycin.,similarity:Belongs to the DNA repair enzymes AP/exoA family.,subunit:Monomer. Component of the SET complex, which also contains SET, ANP32A, HMGB2 and NME1.,

Nucleus. Nucleus, nucleolus. Nucleus speckle. Endoplasmic reticulum. Cytoplasm. Detected in the cytoplasm of B-cells stimulated to switch (By similarity). Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm. .; [DNA-(apurinic or apyrimidinic site) endonuclease, mitochondrial]: Mitochondrion. The cleaved APEX2 is only detected in mitochondria (By similarity). Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress. .

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