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50 µg

Ref. AG-20B-0057-C050

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Neuf 230.00 H.T.


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Détails Produit

Product description: Monoclonal Antibody. Recognizes the p18 subunit of human caspase-8. Isotype: Mouse IgG2b. Clone: C15. Applications: ICC, IP, WB. Liquid. In PBS containing 10% glycerol and 0.02% sodium azide. 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.

Alternate Names/Synonyms: Apoptotic Cysteine Protease; Apoptotic Protease Mch-5; CAP4; FADD-homologous ICE/ced-3-like Protease

Product Type: Monoclonal Antibody

Clone: C15

Isotype: Mouse IgG2b

Immunogen: Recombinant human caspase-8 (aa 181-478).

Applications: ICC, IP, WB

Species Crossreactivity: Human

Specificity: Recognizes the p18 subunit of human caspase-8.

Purity: >95% (SDS-PAGE)

Concentration: 0.5 mg/ml

Formulation: Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.

Short Term Storage: +4°C

Long Term Storage: -20°C

Shipping: BLUE ICE

Use & Stability: Stable for at least 1 year after receipt when stored at -20°C.

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Literature 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)