Catalog Number:

RA15047

Product Type:

Affinity Purified

Immunogen Sequence:

KRTVWGAKQISATSLPTA(C) a.a. 487 - 504 of human Caspase 10/b (FLICE 2)

Host:

Rabbit

Reactivity:

Human, Mouse

Applications:

Western Blot

Description:

This enzyme is a member of a family of evolutionarily conserved cysteine protease proteins known as caspases . Many of these enzymes are part of a proteolytic cascade that plays a central role in cell death by apoptosis. Several caspase-10 splice forms have been identified. Caspase-10a is identical with MCH-4 . Caspase-10b is identical with FLICE-2 . Caspase-10c is a truncated protein that is essentially a prodomain-only form of the caspase. Caspase-10d is a hybrid of the known caspases MCH-4 and FLICE-2 . It is identical to FLICE-2 except for the small (p12) catalytic subunit, which is identical to MCH-4. Caspase-10 requires proteolytic cleavage of its proenzyme form into 2 subunits. These dimerize to form the active enzyme (Fernandes-Alnemri et al). The mature protein cleaves the proenzyme forms of Caspase-3 and Caspase-7 into their mature and biologically active forms. cleaves poly(ADP-ribose) polymerase (PARP) to yield the 85 kD form that promotes cell death by apoptosis . Caspase-10 contains DED domains and FADD domains, which enable it to interact with other proteins containing such domains. The enzyme binds to FADD and to CD95 and the TNF receptor 1. Caspase-10 is one of the initiator caspases involved in signaling through a death receptor protein. Wang et al have identified mutations in the Caspase-10 gene to be responsible for defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Shin et al have reported that approximately 15 percent of non-Hodgkin lymphomas possess a mutated caspase-10 gene and that this may contribute to the pathogenesis of these tumors by mutated caspase-10 having lost its pro-apoptotic function. Expression of mutated caspases derived from the tumours in 293 cells demonstrates that cell death by apoptosis is suppressed (Shin et al).

Reference:

Fernandes-Alnemri T et al In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains. Proceedings of the National Academy of Science (USA) 93(15): 7464-9 (1996)

Shin MS et al Inactivating mutations of CASP10 gene in non-Hodgkin lymphomas. Blood 99: 4094-4099 (2002)

Wang J et al Inherited human caspase 10 mutations underlie defective lymphocyte and dendritic cell apoptosis in autoimmune lymphoproliferative syndrome type II. Cell 98: 47-58 (1999)

Wang J et al Caspase-10 is an initiator caspase in death receptor signaling. Proceedings of the National Academy of Science (USA) 98: 13884-13888 (2001)