The CFLAR (CASP8 and FADD-like apoptosis regulator) protein, also known as c-FLIP, is a key regulator of apoptosis and necroptosis, playing dual roles in cell survival and death signaling. It shares structural homology with caspase-8 but lacks proteolytic activity due to critical amino acid substitutions. CFLAR exists in multiple splice variants (e.g., FLIP-L, FLIP-S), which interact with death receptors (e.g., Fas, TRAIL-R) and adaptor proteins like FADD to modulate caspase-8 activation in the death-inducing signaling complex (DISC).
CFLAR antibodies are essential tools for studying its complex regulatory functions. They enable detection of protein expression levels, localization, and isoform-specific interactions in various pathological contexts, including cancer, autoimmune disorders, and neurodegenerative diseases. Commercially available antibodies are typically validated for applications like Western blotting, immunohistochemistry, and flow cytometry, often using knockout cell lines as specificity controls.
Research using CFLAR antibodies has revealed its context-dependent roles: FLIP-L generally inhibits apoptosis by limiting caspase-8 activation, while FLIP-S may promote necroptosis under certain conditions. Dysregulation of CFLAR expression correlates with therapy resistance in cancers and inflammatory diseases, making it a potential therapeutic target. These antibodies also facilitate investigations into combination therapies that modulate CFLAR to overcome treatment resistance. Proper validation remains crucial due to CFLAR's structural similarity to other death effector domain (DED)-containing proteins.