|Other Names||Caspase-10, CASP-10, Apoptotic protease Mch-4, FAS-associated death domain protein interleukin-1B-converting enzyme 2, FLICE2, ICE-like apoptotic protease 4, Caspase-10 subunit p23/17, Caspase-10 subunit p12, CASP10, MCH4|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1326b was selected from the C-term region of human CASP10. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates caspase- 3, -4, -6, -7, -8, and -9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC.|
|Tissue Location||Detectable in most tissues. Lowest expression is seen in brain, kidney, prostate, testis and colon|
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Provided below are standard protocols that you may find useful for product applications.
CASP10 is a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. This protein cleaves and activates caspases 3 and 7, and the protein itself is processed by caspase 8. Mutations in the protein are associated with apoptosis defects seen in type II autoimmune lymphoproliferative syndrome.
Lan,Q., Morton,L.M. Blood 114 (2), 264-267 (2009)Kim,Y.R., Kim,K.M. Hum. Pathol. 40 (6), 868-871 (2009)Lisa-Santamaria,P. Biochim. Biophys. Acta 1793 (3), 561-571 (2009)
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