Caspase8 Antibody | 79-642

Caspase8 Antibody | 79-642 | Gentaur UK, US & Europe Distribution

Host: Rabbit

Reactivity: Human

Homology: N/A

Immunogen: Caspase8 antibody was raised against a peptide sequence around aa.221~225 (T-L-D-K-V) derived from Human Caspase8.

Research Area: Apoptosis, Cancer

Tested Application: WB

Application: Western Blot: 1:500~1:1000

Specificiy: This antibody detects endogenous level of total Caspase8 protein.

Positive Control 1: N/A

Positive Control 2: N/A

Positive Control 3: N/A

Positive Control 4: N/A

Positive Control 5: N/A

Positive Control 6: N/A

Molecular Weight: 18, 43, 57 kDa

Validation: N/A

Isoform: N/A

Purification: Antibodies were purified by affinity-chromatography using epitope-specific peptide.

Clonality: Polyclonal

Clone: N/A

Isotype: N/A

Conjugate: Unconjugated

Physical State: Liquid

Buffer: Antibody supplied in phosphate buffered saline (without Mg2+ and Ca2+) , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Concentration: 1 mg/mL

Storage Condition: Store antibody at -20˚C for up to one year.

Alternate Name: caspase-8, zgc:92075, NCAM, CASP8, MCH5

User Note: N/A

BACKGROUND: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.