Chapter title |
Detecting caspase activity in Drosophila larval imaginal discs.
|
---|---|
Chapter number | 7 |
Book title |
Caspases,Paracaspases, and Metacaspases
|
Published in |
Methods in molecular biology, February 2014
|
DOI | 10.1007/978-1-4939-0357-3_7 |
Pubmed ID | |
Book ISBNs |
978-1-4939-0356-6, 978-1-4939-0357-3
|
Authors |
Fogarty CE, Bergmann A, Caitlin E. Fogarty, Andreas Bergmann, Fogarty, Caitlin E., Bergmann, Andreas |
Abstract |
Caspases are a highly specialized class of cell death proteases. Since they are synthesized as inactive full-length zymogens, activation--at least of effector caspases and to some extent also of initiator caspases-requires a proteolytic cleavage event, generating a large and a small subunit, two of each forming the active caspase. The proteolytic cleavage event generates neo-epitopes at both the C-terminus of the large subunit and the N-terminus of the small subunit. The cleaved Caspase-3 (CC3) antibody was raised against the neo-epitope of the large subunit and thus detects only cleaved, but not full-length, Caspase-3. Although raised against human cleaved Caspase-3, the CC3 antibody cross-reacts in other species and detects cleaved caspases, most notably DrICE and Dcp-1, in Drosophila. This protocol describes the procedure for use of the CC3 antibody to detect caspase activity in larval imaginal discs in Drosophila. |
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