CASP8 exists as a proenzyme (procaspase-8) and is activated during apoptosis or immune responses. Monoclonal antibodies targeting CASP8 detect both pro-forms (e.g., p55, p53) and cleaved active subunits (p43, p18/p10). These antibodies bind to epitopes on the pro-domain or catalytic subunits, enabling precise detection in experimental systems.
CASP8 antibodies are utilized in diverse experimental workflows:
Protein detection: Procaspase-8 (55–53 kDa) and active subunits (p18/p10, p43) .
Optimal dilutions: 1–5 µg/mL for 1H10 , 1:300–5000 for 4G12 .
Controls: Jurkat cells (FAS-induced apoptosis) or recombinant CASP8 .
CASP8 modulates PD-L1 expression, influencing tumor immune evasion:
Mechanism: CASP8 promotes A20-mediated ubiquitination and degradation of PD-L1, reducing immunosuppression .
Therapeutic relevance:
Death receptor agonists: CASP8 expression predicts sensitivity to conatumumab (anti-DR5 antibody) in Ewing sarcoma (EWS). Overexpression of active CASP8 restores conatumumab efficacy in resistant EWS models .
Isoform-specific effects: Procaspase-8 isoforms (e.g., Caspase-8L) may interfere with apoptosis, impacting treatment outcomes .