|Application ||WB, E|
|Other Accession||NP_203522, 841|
|Calculated MW||55391 Da|
|Application Notes||Casp-8 antibody can be used for the detection of Caspase-8 by Western blot at 1 μg/mL.|
|Other Names||Caspase-8 Antibody: CAP4, MACH, MCH5, FLICE, ALPS2B, Casp-8, Caspase-8, Apoptotic cysteine protease, CASP-8, caspase 8, apoptosis-related cysteine peptidase|
|Target/Specificity||Caspase-8 antibody was raised against a 15 amino acid synthetic peptide from near the carboxy terminus human caspase-8 isoform E.|
The immunogen is located within the last 50 amino acids of Caspase-8.
|Reconstitution & Storage||Caspase-8 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|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|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Caspase-8 Antibody: Caspases are a family of cysteine proteases that can be divided into the apoptotic and inflammatory caspase subfamilies. Unlike the apoptotic caspases, members of the inflammatory subfamily are generally not involved in cell death but are associated with the immune response to microbial pathogens. The apoptotic subfamily can be further divided into initiator caspases, which are activated in response to death signals, and executioner caspases, which are activated by the initiator caspases and are responsible for cleavage of cellular substrates that ultimately lead to cell death. Caspase-8 is an initiator caspase that was identified as a member of the Fas/APO-1 death-inducing signaling complex. The adaptor molecule FADD couples procaspase-8 to the Fas receptor death domain; subsequent oligomerization promotes procaspase-8 autoactivation. FLIP, a catalytically inactive caspase-8-like molecule inhibits these interactions and thus can inhibit apoptosis. This antibody will only detect isoform E of caspase-8.
Martinon F and Tschopp J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory diseases. Cell 2004; 117:561-74.
Zhivotovsky B and Orrenius S. Caspase-2 function in response to DNA damage. Biochim. Biophys. Res. Comm. 2005; 331:859-67.
Wolf BB and Green DR. Suicidal tendencies: apoptotic cell death by caspase family proteinases. J. Biol. Chem. 1999; 274:20049-52.
Muzio M, Chinnaiyan AM, Kischkel FC, et al. FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex. Cell 1996; 85:817-27.
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