RIPK3 is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, which contains a C-terminal domain unique from other RIP family members. RIPK3 is predominantly localized to the cytoplasm, and specifically, are colocalized in the mitochondrion which can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. RIPK3 is a component of the tumor necrosis factor (TNF) receptor-I signaling complex, and can induce apoptosis and weakly activate the NF-kappaB transcription factor and caspase-8 prevents RIPK3-dependent necrosis without inducing apoptosis by functioning in a proteolytically active complex with CFLAR and that this complex is required for the protective function. Recombinant full-length human RIPK3 was expressed by baculovirus in Sf9 insect cells using an N-terminal GST tag.

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