APE-1 antibodies are immunoreagents designed to detect APE-1, a 35–37 kDa protein with dual enzymatic activities:
DNA Repair: APE-1’s C-terminal domain processes apurinic/apyrimidinic (AP) sites via base excision repair (BER) .
Redox Regulation: The N-terminal domain activates transcription factors (e.g., NF-κB, HIF-1α) by reducing cysteine residues, modulating immune and inflammatory responses .
Commercial APE-1 antibodies (e.g., clones 13B8E5C2, E5Y2C) are validated for applications including Western blot (WB), immunohistochemistry (IHC), and immunofluorescence (IF) .
The table below summarizes widely used APE-1 antibodies:
Cancer Detection: Serum APE-1 autoantibodies (APE1-AAbs) are elevated in non-small cell lung cancer (NSCLC) patients and correlate with chemotherapy response .
Therapeutic Predictor: APE1-AAbs levels decrease post-chemotherapy in responsive NSCLC patients, highlighting their utility in monitoring treatment efficacy .
DNA Repair Inhibition: Small-molecule inhibitors (e.g., NO.0449-0145) block APE1’s endonuclease activity, inducing apoptosis and overcoming drug resistance in NSCLC .
Telomere Stability: APE1 stabilizes telomeric DNA by interacting with TRF2 and POT1; its depletion causes telomere shortening and genomic instability .
Nuclear Role: APE1 antibodies detect nuclear staining in normal tissues (e.g., liver, placenta) and cancers (e.g., osteosarcoma) .
Cytoplasmic Role: In neurons and hepatocytes, APE1 exhibits cytoplasmic localization, suggesting redox signaling roles outside the nucleus .
A 37 kDa band is consistently observed in HeLa, HepG2, and 293T lysates, aligning with APE1’s predicted molecular weight .
Knockout controls (e.g., APEX1-null HAP1 cells) confirm antibody specificity .
APE1 inhibitors are under investigation for cancer therapy due to their dual targeting of DNA repair and redox pathways: