CASP8 Proteins

CASP8 (Caspase 8) is a Protein Coding gene. Diseases associated with CASP8 include Caspase 8 Deficiency and Hepatocellular Carcinoma. Among its related pathways are Apoptosis and survival Caspase cascade and CDK-mediated phosphorylation and removal of Cdc6. Gene Ontology (GO) annotations related to this gene include protein heterodimerization activity. An important paralog of this gene is CASP10.

The following recombinant CASP8 proteins are manufactured in house under a complete QC system by CUSABIO. They are expressed by Yeast, E.coli, Baculovirus, Mammalian cell, In Vivo Biotinylation in E.coli. Highlights of these recombinant CASP8 proteins as follow:
High purity, Low endotoxin, Multiple Tags, Animal-free, Wide applications (Cell assay, Protein-protein interaction, Drug-related studies, Enzymatic activity in vitro, Protein structure analysis, etc.)
In addition, various options on sizes, excellent technical support, and recombinant CASP8 proteins custom service will be also offered.

CASP8 Proteins Catalog

CASP8 Proteins for Mus musculus (Mouse)

CASP8 Proteins for Homo sapiens (Human)

CASP8 Background

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 [1]. 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 [2]. 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 [10]. 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 [3]. 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) [4]. 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 [5]. Caspase-3 and caspase-6 can facilitate the transition of pro-caspase-8 to be an active dimer form via proteolysis [6][7]. 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 [8]. 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 [9].

[1] H.R. Stennicke, G.S. et al. Properties of the caspases [J]. Biochim. Biophys. Acta, 1387 (1998), pp. 17-31.
[2] 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
[3] 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.
[4] 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.
[5] 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.
[6] 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.
[7] 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.
[8] 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.[9] 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).
[10] 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.


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