CASP8 Antibodies for Homo sapiens (Human)
|Code||Product Name||Species Reactivity||Application|
|CSB-PA18109A0Rb||Human||ELISA, WB, IHC, IF|
|CSB-PA001234||Human,Mouse,Rat||WB, IHC, ELISA|
|CSB-PA060299||Human,Rat||WB, IHC, ELISA|
|CSB-PA181094ZA01HU||Homo sapiens||ELISA, WB (ensure identification of antigen)|
CASP8 Proteins for Mus musculus (Mouse)
In Vivo Biotinylation in E.coli
CASP8 Proteins for Homo sapiens (Human)
In Vivo Biotinylation in E.coli
CASP8 ELISA Kit for Homo sapiens (Human)
|Code||Product Name||Sample Types||Sensitivity|
|CSB-E13636h||serum, plasma, cell lysates||7.81 pg/ml|
Caspase-8, encoded by gene CASP8, is a member of the cysteine proteases that specifically cleave substrates at sites located after aspartic acid residues in target amino acid sequences . Like all caspases, caspase‐8 is synthesized as an inactive monomer procaspase. Caspase-8 activation requires not only proteolytic processing but also the dimerization process . Caspase-8 carries a large N-terminal prodomain with a DED (death effector domain) followed by the catalytic domain containing a large and small subunit separated by a linker region . Ligation of Fas by Fas Ligand initiates recruitment of caspase-8 to the membrane-bound DISC (death-inducing signaling complex) via the adaptor protein FADD (FAS-associated death domain) through their death effector domain (DED), respectively . The DISC is formed at the cytoplasmic tail of the engaged DR that also includes the adapter protein FAS-associated death domain (FADD) or TNFR-associated death domain (TRADD) . Recruitment of caspase-8 monomers results in dimerization and activation. Caspase-8 activation also occurs through a feedback loop derived from the intrinsic apoptotic pathway . Caspase-3 and caspase-6 can facilitate the transition of pro-caspase-8 to be an active dimer form via proteolysis . As an initiator caspase, active caspase-8 is released to the cytosol and cleaves downstream effector caspases. In some cell types, caspase-8 cleaves the BH3-only protein Bid to promote MOMP that ultimately induces cytochrome c leakage, caspase-9 activation, and subsequent apoptosis . Activated caspase‐9 further stimulates further downstream caspases, including caspase‐8. Melanie Fritsch et al. uncovered that caspase-8 represents the molecular switch that controls apoptosis, necroptosis, and pyroptosis, and prevents tissue damage during embryonic development and adulthood .
 H.R. Stennicke, G.S. et al. Properties of the caspases [J]. Biochim. Biophys. Acta, 1387 (1998), pp. 17-31.
 A. Oberst, C. Pop, A.G. et al. Inducible dimerization and inducible cleavage reveal a requirement for both processes in caspase-8 activation [J]. J. Biol. Chem., 285 (2010), pp. 16632-16642
 F.C. Kischkel, S. Hellbardt, et al. Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor [J]. EMBO J., 14 (1995), pp. 5579-5588.
 Boldin MP, Goncharov TM, et al. Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death [J]. Cell. 1996 Jun 14; 85(6):803-15.
 T. Kuwana, J.J. Smith, et al. Apoptosis induction by caspase-8 is amplified through the mitochondrial release of cytochrome c [J]. J. Biol. Chem., 273 (1998), pp. 16589-16594.
 V. Cowling, J. Downward Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain [J]. Cell Death Differ., 9 (2002), pp. 1046-1056.
 D. Sohn, K. Schulze-Osthoff, et al. Caspase-8 can be activated by interchain proteolysis without receptor-triggered dimerization during drug-induced apoptosis [J]. J. Biol. Chem., 280 (2005), pp. 5267-5273.
 Luo X, Budihardjo I, et al. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors [J]. Cell. 1998 Aug 21; 94(4):481-90. Melanie Fritsch, Saskia D. Günther, et al. Caspase-8 is the molecular switch for apoptosis, necroptosis and pyroptosis [J]. Nature volume 575, pages683-687(2019).
 Fuentes-Prior P, Salvesen GS The protein structures that shape caspase activity, specificity, activation and inhibition [J]. Biochem J. 2004 Dec 1; 384(Pt 2):201-32.