Human recombinant caspase 2-3-7
Ontology highlight
ABSTRACT:
INSTRUMENT(S): instrument model
ORGANISM(S): Homo Sapiens (human)
SUBMITTER: 
Magdalena Wejda
PROVIDER: PRD000557 | Pride | 2012-08-15
REPOSITORIES: Pride
Publications
Degradomics reveals that cleavage specificity profiles of caspase-2 and effector caspases are alike.
Wejda Magdalena M Impens Francis F Takahashi Nozomi N Van Damme Petra P Gevaert Kris K Vandenabeele Peter P
The Journal of biological chemistry 20120723 41
Caspase-2 is considered an initiator caspase because its long prodomain contains a CARD domain that allows its recruitment and activation in several complexes by homotypic death domain-fold interactions. Because little is known about the function and specificity of caspase-2 and its physiological substrates, we compared the cleavage specificity profile of recombinant human caspase-2 with those of caspase-3 and -7 by analyzing cell lysates using N-terminal COmbined FRActional DIagonal Chromatogra ...[more]
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