Caspase 8, Apoptosis-Related Cysteine Peptidase (CASP8) (full length) antibody

Antigen: Caspase 8, Apoptosis-Related Cysteine Peptidase (CASP8)

Synonyms: CAP4, MACH, MCH5, FLICE, ALPS2B, Casp-8, FLJ17672, MGC78473, Mch5, Caspase-8, MGC92075, caspase-8, zgc:92075, casp8-A, xCaspase-8, CASP8, casp8, DKFZp469A1428

Binding Site: full length

Clonality: Monoclonal (39816)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP)

Catalog no.: ABIN967335

Additional Information

Alternative name: Caspase-8

Immunogen: Human Caspase-8 full-length recombinant protein

Format: Liquid

Isotype: IgG1

Clone: 39816

Description: Caspase-8 (FLICE/MACH-1) is a 55 kDa cytosolic protein with homology to the CD95/Fas-associated signal transducer, FADD/MORT-1, as well as to other caspase (ICE/Ced-3) cysteine proteases. The N-terminal region of caspase-8 contains an amino acid sequence, termed the death domain, that facilitates caspase-8-FADD direct interaction. FADD therefore acts as an adapter molecule, allowing caspase-8 to become recruited to the cytoplasmic region of Fas following receptor activation. Viral proteins (v-FLIPS) which inhibit recruitment and activation of caspase-8 have been isolated. Caspase-8 is produced as a proenzyme (55/50 kDa doublet) which upon receptor aggregation is proteolytically cleaved into smaller subunits of 40/36 (doublet), and 23 kDa. Overexpression of caspase-8 is sufficient to induce apoptosis in certain cell lines (e.g., MCF-7) and this phenotype is blocked by overexpression of the caspase-3 protease inhibitor, CrmA. The antibody recognizes both the proform of human caspase-8 (55/50 kDa doublet) as well as the cleaved forms which migrate at 40/36 (doublet) and 23 kDa in SDS/PAGE. It also immunoprecipitates the full-length human caspase-8. Full-length recombinant human caspase-8 protein was used as immunogen.
Synonyms: FLICE, MACH-1, Mch5

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.

Molecular Weight: 55/50 kDa, 40/36 kDa, 23 kDa

Comments:

Related Products: ABIN967389

Application Details

Application Notes: Applications include western blot analysis (0.125 - 0.5 µg/ml) and immunoprecipitation (4 µg/200 µg cell lysate). Jurkat T cells (ATCC CRL-1573) are suggested as a positive control. Antibodies-online offers several caspase-8 antibodies. A Jurkat model cell system was used to evaluate these antibodies, these results are summarized in the following table. However, actual bands observed could vary according to the cell model system or treatment used.

Concentration: 0.5 mg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at 4°C.

Research Area: Apoptosis/Necrosis

Restrictions: For Research Use only

Images

Western blot analysis of caspase-8. Lysates from control (lanes 1-3) and camptothecin treated Jurkat cells (lanes 4-6) were probed with anti-human caspase-8 (clone 3-1-9, ABIN967335) at the following concentrations: 0.5 (lanes 1,4), 0.25 (lanes 2,5), and 0.125 µg/ml (lanes 3,6). Caspase-8 is identified as 55/50 kDa (proform), 40/36 kDa (cleaved), and 23 kDa (cleaved) bands in treated cells and the 55 kDa band in control cells.

Immunoprecipitation/western blot analysis of caspase-8. Lysates from control (lane 1) or camptothecin-treated Jurkat cells (lane 2) were each immunoprecipitated with anti-human caspase-8 (clone 3-1-9), and western blotted with anti-human caspase-8 (clone 3-1-9). The 55 kDa proform caspase-8 was identified in both control and camptothecin-treated cells.

Publications

Product: Muzio, Chinnaiyan, Kischkel et al.: "FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death--inducing signaling complex." in: Cell, Vol. 85, Issue 6, pp. 817-27, 1996 (PubMed).

Thome, Schneider, Hofmann et al.: "Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors." in: Nature, Vol. 386, Issue 6624, pp. 517-21, 1997 (PubMed).

Cock, Tepper, de Vries et al.: "CD95 (Fas/APO-1) induces ceramide formation and apoptosis in the absence of a functional acid sphingomyelinase." in: The Journal of biological chemistry, Vol. 273, Issue 13, pp. 7560-5, 1998 (PubMed).

Thome, Martinon, Hofmann et al.: "Equine herpesvirus-2 E10 gene product, but not its cellular homologue, activates NF-kappaB transcription factor and c-Jun N-terminal kinase." in: The Journal of biological chemistry, Vol. 274, Issue 15, pp. 9962-8, 1999 (PubMed).

Boesen-de Cock, Tepper, de Vries et al.: "Common regulation of apoptosis signaling induced by CD95 and the DNA-damaging stimuli etoposide and gamma-radiation downstream from caspase-8 activation." in: The Journal of biological chemistry, Vol. 274, Issue 20, pp. 14255-61, 1999 (PubMed).