Caspase-10 Recombinant Rabbit monoclonal Antibody IgG
Fig1: Western blot analysis of Caspase-10 on K562 cells lysates using anti-Caspase-10 antibody at 1/1,000 dilution.
Fig2: Immunohistochemical analysis of paraffin-embedded human liver cancer tissue using anti-Caspase-10 antibody. Counter stained with hematoxylin.
Fig3: Immunohistochemical analysis of paraffin-embedded human kidney tissue using anti-Caspase-10 antibody. Counter stained with hematoxylin.
Host Species; Species ReactivityRabbit; Human
Application SummaryWB, IHC, IP, FC
Purification; FormulationProA affinity purified; 1*TBS (pH7.4), 1%BSA, 40%Glycerol. Preservative: 0.05% Sodium Azide.; Liquid form.
ALTnamesCaspase-10, Apoptotic protease Mch-4, FAS-associated death domain protein interleukin-1B-converting enzyme 2, ICE-like apoptotic protease 4
BackgroundCaspase-10, also designated Mch4, is recruited to the native TRAIL and CD9 death-inducing signaling complexes (DISCs) by the FADD/Mort1 adaptor protein complex. Caspase-10 requires the assembly of the FADD and DISC complexes for its recruitment and cleavage-induced activation during CD95-induced apoptosis of activated T cells. The N-terminus of caspase-10 contains FADD-like death effector domains further indicating that it associates with FADD to induce apoptosis. Caspase-10 is not required for apoptosis induction and when overexpressed, cannot reverse defects in apoptosis induction caused by caspase-8 deficiency. Granzyme B cleaves procaspase-10 at an IXXD-A processing sequence to produce mature caspase-10. Mutations in the caspase-10 gene in the prodomain, p17 large protease subunit and p12 small protease subunit have been linked to a number of non-Hodgkin lymphomas in humans.(ET1701-53)