anti-Caspase-8 (human), mAb antibody (C15)

Specifications / Handling

More Information
Product Details
Synonyms	Apoptotic Cysteine Protease; Apoptotic Protease Mch-5; CAP4; FADD-homologous ICE/ced-3-like Protease
Product Type	Monoclonal Antibody
Properties
Clone	C15
Isotype	Mouse IgG2b
Source/Host	Purified from concentrated hybridoma tissue culture supernatant.
Immunogen/Antigen	Recombinant human caspase-8 (aa 181-478).
Application	Western Blot: (1μg/ml) Immunoprecipitation Immunocytochemistry
Crossreactivity	Human
Specificity	Recognizes the p18 subunit of human caspase-8.
Purity	≥95% (SDS-PAGE)
Purity Detail	Protein G-affinity purified.
Concentration	1mg/ml (Lot dependent 0.5 mg/ml)
Formulation	Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.
Isotype Negative Control	Mouse IgG2b Isotype Control
Shipping and Handling
Shipping	BLUE ICE
Short Term Storage	+4°C
Long Term Storage	-20°C
Handling Advice	After opening, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles.
Use/Stability	Stable for at least 1 year after receipt when stored at -20°C.
Documents
MSDS	Download PDF
Product Specification Sheet
Datasheet	Download PDF

Product-specific References

Description

Procaspase-8 belongs to the family of caspases. Binding of FasL to Fas leads to formation of a receptor complex at the cellular membrane, which was named DISC. The DISC consists of oligomerized receptors, the DD-containing adaptor molecule FADD, procaspase-8, procaspase-10 and c-FLIP. The DISC structure provides a platform for the oligomerization of procaspase-8 that allows two procaspase-8 homodimers to be in the close proximity leading to the initial activation of procaspase-8. At the first cleavage step, the N-terminal p43/p41 and the C-terminal p30 cleavage products are generated. Importantly, these cleavage products already possess catalytic activity. At the second cleavage step, p43/p41 and p30 are processed to p10 and p18, respectively, which leads to the generation of the active caspase-8 heterotetramer (p18/p10)2.

Product References

FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b: C. Scaffidi, et al.; J. Biol. Chem. 272, 26953 (1997)
Bcl-xL Acts Downstream of Caspase-8 Activation by the CD95 Death-inducing Signaling Complex: J.P. Medema, et al.; J. Biol. Chem. 273, 3388 (1998)
Two CD95 (APO-1/Fas) signaling pathways: C. Scaffidi, et al.; EMBO J. 17, 1675 (1998)
Liposomal ET-18-OCH3 Induces Cytochrome c-Mediated Apoptosis Independently of CD95 (APO-1/Fas) Signaling: O. Cuvillier, et al. Blood 94, 3583 (1999)
FADD/MORT1 and Caspase-8 Are Recruited to TRAIL Receptors 1 and 2 and Are Essential for Apoptosis Mediated by TRAIL Receptor 2: M.R. Sprick, et al.; Immunity 12, 599 (2000)
Involvement of caspases and of mitochondria in Fas ligation-induced eosinophil apoptosis: modulation by interleukin-5 and interferon-gamma: S. Letuve, et al.; J. Leukoc. Biol. 70, 767 (2001)
Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8: M.R. Sprick, et al.; EMBO J. 21, 4520 (2002)
Proteasome inhibition results in TRAIL sensitization of primary keratinocytes by removing the resistance-mediating block of effector caspase maturation: M. Leverkus, et al.; Mol. Cell. Biol. 23, 777 (2003)
Lack of Proapoptotic Activity of Soluble CD95 Ligand Is Due to Its Failure to Induce CD95 Oligomers: S. Jang, et al.; J. Int. Cyt. Res. 23, 441 (2003)
Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice: S.T. Eichhorst, et al.; Nature Med. 10, 602 (2004)
Caspase-2 is activated at the CD95 death-inducing signaling complex in the course of CD95-induced apoptosis: I.N. Lavrik, et al.; Blood 108, 559 (2006)
The c-FLIP-NH2 terminus (p22-FLIP) induces NF-kappaB activation: A. Golks, et al.; J. Exp. Med. 203, 1295 (2006)
The role of CAP3 in CD95 signaling: new insights into the mechanism of procaspase-8 activation: A. Golks, et al.; Cell Death Diff. 13, 489 (2006)
Retinoic acid induces caspase-8 transcription via phospho-CREB and increases apoptotic responses to death stimuli in neuroblastoma cells: M. Jiang, et al.; Biochim. Biophys. Acta 1783, 1055 (2008)
CD95 Stimulation Results in the Formation of a Novel Death Effector Domain Protein-containing Complex: I.N. Lavrik, et al.; J. Biol. Chem. 283, 26401 (2008)
Critical Role for Caspase-8 in Epidermal Growth Factor Signaling: D. Finaly, et al.; Cancer Res. 69, 5023 (2009)
A New C-terminal Cleavage Product of Procaspase-8, p30, Defines an Alternative Pathway of Procaspase-8 Activation: J.C. Hoffmann, et al.; Mol. Cell Biol. 29, 4431 (2009)
2D-gel Electrophoresis As a Tool to Investigate the Composition of CD95 DISC: D. Riess & I. Lavrik; Acta Naturae 2, 96 (2010)
Novel HTS Strategy Identifies TRAIL-Sensitizing Compounds Acting Specifically Through the Caspase-8 Apoptotic Axis: D. Finlay, et al.; PLoS One 5, e13375 (2010)
Stoichiometry of the CD95 Death-Inducing Signaling Complex: Experimental and Modeling Evidence for a Death Effector Domain Chain Model: K. Schleich, et al.; Mol. Cell 47, 1 (2012)
Caspase-8 Acts in a Non-enzymatic Role as a Scaffold for Assembly of a Pro-inflammatory “FADDosome” Complex upon TRAIL Stimulation: C.M. Henry & S.J. Martin; Mol. Cell 65, 715 (2017)
Systemic network analysis identifies XIAP and IκBα as potential drug targets in TRAIL resistant BRAF mutated melanoma: G. Del Mistro, et al.; NPJ Syst. Biol. Appl. 4, 39 (2018)
TRAIL receptors serve as stress-associated molecular patterns to promote ER-stress-induced inflammation: G.P. Sullivan, et al.; Dev. Cell. 52, 714 (2020)
Focal adhesion kinase plays a dual role in TRAIL resistance and metastatic outgrowth of malignant melanoma: G. Del Mistro, et al.; Cell Death Dis. 13, 54 (2022)
Human ZBP1 induces cell death-independent inflammatory signaling via RIPK3 and RIPK1: R. Peng, et al.; EMBO Rep. e55839 (2022)
cFLIPL acts as a suppressor of TRAIL- and Fas-initiated inflammation by inhibiting assembly of caspase-8/FADD/RIPK1 NF-kB-activating complexes: P. Davidovich, et al.; Cell Rep. 42, 113476 (2023)

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anti-Caspase-8 (human), mAb (C15)