Caspase 8 Rabbit anti-Human, Polyclonal, Bioss

Description

• Caspase 8 (CASP8) is a member of the cysteine-aspartic acid protease (caspase) family
• Sequential activation of caspases play a central role in the execution-phase of cell apoptosis
• Caspases exist as inactive proenzymes composed of a pro-domain, a large protease subunit, and a small protease subunit
• Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits
• Caspase 8 is involved in the programmed cell death induced by Fas and various apoptotic stimuli
• The N-terminal FADD-like death effector domain of Caspase 8 suggests that it may interact with Fas-interacting protein FADD
• Caspase 8 was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases
• Caspase 8 binds to the death effector domain (DED) of FADD through an analogous DED domain present in tandem in the pro-form of the Caspase 8 protein
• Activated Caspase 8 then activates other downstream caspases including Caspase 9, thereby committing the cell to undergo apoptosis
• In addition, Caspase 8 also reacts with Jurkat cells and Tonsil
• Overexpression of Caspase 8 induces apoptosis, which can be blocked by inhibitors specific for the ICE family
• Many alternatively spliced transcript variants encoding different isoforms have been described for Caspase 8, however, not all variants have had their full-length sequences determined.