Caspase 9, aa299-318, IN2, Blocking Peptide (ICE-LAP6, Mch6, Apaf 3)

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. A novel member in the caspase family was recently identified and designated ICE-LAP6, Mch6, and Apaf-3 (1-3). Caspase-9 and Apaf-1 bind to each other, which leads to caspase-9 activation (3). Caspase-9 is also activated by granzyme B and CPP32 (1,2). Activated caspase-9 cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis (3). Caspase-9 play a central role in cell death induced by a wide variety of apoptosis activators including TNFa, TRAIL, anti-CD-95, FADD, and TRADD (4). Caspase-9 is expressed in a variety of human tissues (1,2). \n\nAmino acids 299 to 318 of human caspase-9 (1-3).

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SPECIFICATIONS

Catalog Number

C2088-14P

Size

50ug

Form

Supplied as a lyophilized powder.

Purity

Purified 60-70%

References

1. Duan H, Orth K, Chinnaiyan AM, Poirier GG, Froelich CJ, He WW, Dixit VM. ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated by the cytotoxic T cell protease granzyme B. J Biol Chem 1996;271:16720-4 \n\n2. Srinivasula SM, Fernandes-Alnemri T, Zangrilli J, Robertson N, Armstrong RC, Wang L, Trapani JA, Tomaselli KJ, Litwack G, Alnemri ES. The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic mediator CPP32. J Biol Chem 1996;271:27099-106\n\n3. Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997;91:479-89\n\n4. Pan G, O'Rourke K, Dixit VM. Caspase-9, Bcl-XL, and Apaf-1 form a ternary complex. J Biol Chem 1998;273:5841-5.\n