Caspase-7/MCH-3 Mouse, Unlabeled, Clone: 51, BD
Mouse Monoclonal Antibody
Manufacturer: BD Biosciences 610812
Apoptosis is induced by cysteine proteases which include Ced-3 of C.elegans, Caspase-3 (also known as CPP32, Yama, or apopain), and DCP-1 of Drosophila.. Multiple signals, such as activation of Fas and granzyme B, activate Caspase-3 which, in turn, cleaves substrates. Some substrates of Caspase-3 are PARP, MCH-3, MCH-2, U1-associated 70kDa protein, and SREBPs. Caspase-7/MCH-3 is a putative cysteine protease cloned from human Jurkat T lymphocytes. This protein shows significant homology to mammalian interleukin-1β -converting enzyme (ICE), Caspase-3, and the Caenorhabditis elegans protein Ced3. All three of these proteins are cytoplasmic cysteine proteases that induce apoptosis when overexpressed in different cell types. This apoptosis can be inhibited by coexpression of Bcl-2. Similar to ICE and Caspase-3, Caspase-7 is a proenzyme that is proteolytically cleaved into p20 and p12 subunits that form the active Caspase-7 heterodimeric complex. Similarity to ICE and Caspase-3, as well as its high levels observed in lymphocytes, suggests that Caspase-7 plays an important role in immunologic apoptosis.
Immunofluorescence, Immunoprecipitation, Western Blotting
|Immunofluorescence, Western Blot|
|Human MCH-3 aa. 4-126|
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