In human Viral FLICE-inhibitory proteins (v-FLIPs) is identified as c-FLIP. It is composed of two death effector domains which have structural resemblance with the N-terminal half of caspase-8 and a caspase-like domain. It exist as multiple splice variants: FLIP α, β, γ and δ. Along with splice variants, it has two endogenous forms of the protein − c-FLIP_long and c-FLIP_short.

FLIP antibody was raised against a 19 amino acid peptide near the carboxy terminus of human FLIP.
The immunogen is located within amino acids 180 - 230 of FLIP.

Anti-FLIPγ/δ, C-Terminal antibody is suitable for microarray and western blot at a dilution of 1:1,000 using HeLa, Jurkat, THP-1, A431, K562, and NIH-3T3 cell lysates.

C-FLIP plays an important role in apoptosis signaling pathways. It acts as proapoptotic molecule or as an anti-apoptotic molecule. It has been reported that c-FLIP can interact with both FADD and caspase-8. It prevents caspase-8 recruitment and processing through DED-DED (Death Effector Domain) interaction followed by CD95-induced apoptosis.

Solution in 0.01 M phosphate buffered saline containing 0.02% sodium azide.

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