|Application ||WB, E|
|Calculated MW||58951 Da|
|Antigen Region||164-192 aa|
|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||This CASP10 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 164-192 amino acids from the Central region of human CASP10.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CASP10 Antibody (Center) is for research use only and 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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