Caspase 8 (CASP8) belongs to the cysteine aspartic acid protease (caspase) family of enzymes. Caspases that activate in sequence play an essential role in the execution phase of cell Apoptosis.
Caspases function as inactive proenzymes that comprise a pro-domain, a massive protease subunit, as well as a smaller subunit of protease.
Caspase 8 is implicated in the death of cells programmed caused by Fas and other apoptotic stimuli. Caspase 8 binds to the death effector domain (DED) of FADD via an identical DED domain that is present in the pro-form Caspase 8 protein. You can know more about Caspase-8/CASP8 Antibody online.
Image Source: Google
Caspase-8 Antibody (8CSP03) comes in both the unconjugated anti-caspase-8 version and also several conjugated forms of anti-caspase-8 antibody. These include HRP, agarose, PE, and numerous Alexa Fluor(r) conjugates.
Caspase-8 binds with adaptor molecule FADD creating an aggregate known as the death-inducing signaling complex (DISC) that activates caspase-8. This active protein gets then released from the complex and stimulates downstream Apoptotic Proteases.
Caspase-8, a heterodimer composed of 2 subunits (p18 as well as p10) It is expressed in a wide range of however it is found with the highest concentrations in peripheral blood cells (PBLs) as well as thymus, the spleen, and liver.
There are defects in CASP8 that encodes for caspase-8, which can result in CASP8D (caspase-8 deficiencies) that is characterized by splenomegaly as well as CD95-induced apoptosis of PBLs.
It can result in immunodeficiency due to problems with T lymphocytes and NK cells as well as activated B lymphocytes.