|Calculated MW||55391 Da|
|Application & Usage||Western blotting (0.5-4 µg/ml). The immunoaffinity purified antibody detects the full length (55 kDa), intermediate cleavage fragments (26-31 kDa) and cleaved large fragment (18 kDa) of caspase-8.|
|Other Names||CASP8 , MGC78473 , CASP-8, MACH, procaspase-8, MCH5, ALPS2B, FLICE, CAP4, EC 126.96.36.199|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit anti-caspase-8 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Caspase-8 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||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.|
|Tissue Location||Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle|
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Provided below are standard protocols that you may find useful for product applications.
Caspase family of cysteine proteases has been shown to play a key role in apoptosis. Caspase-8 is a 55 kDa cytosolic protein that is synthesized as an inactive pro-enzyme. Activation of caspase-8 involves a two-step proteolysis: the cleavage of caspase-8 to generate a 43 and a 12 kDa fragment which is further processed to 10 kDa. The p43 is then cleaved to yield p26 and the release of the active site containing p18.
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