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Figure 1: Western blot analysis using anti-caspase-2, mAb (11B4) (Prod. No. AG-20T-0136), detecting caspase-2 expression in cultured mouse and human cell lines. Caspase-2 protein was revealed in lysates from 2x105 mouse and human cell lines by 11B4 and ECL.
Figure 2: Immunoprecipitation using anti-caspase-2, mAb (11B4) (Prod. No. AG-20T-0136), an isotype-matched control antibody or an anti-HA mAb of 35S-labelled 293T cells transfected with mutant caspase-2-HA.
Immunoprecipitation: (1-5μg/ml) Western Blot: (1-2μg/ml) Optimal conditions must be determined individually for each application.
Crossreactivity
Dog Human Monkey Mouse Rat
Specificity
Recognizes an epitope in the p19 subunit of human, mouse, rat, monkey and dog caspase-2. Detects bands of ~51kDa (procaspase-2), ~32kDa and ~18kDa (cleavage products) by Western blot.
Caspase-2 is a Class I caspase with a long prodomain necessary for nuclear localization. Upon activation of the apoptotic pathway, the procaspase is cleaved into smaller fragments. Caspase-2 is the nuclear apoptotic respondent to cellular genotoxic stress or mitotic catastrophe and is involved in the activation cascade of caspases responsible for apoptosis execution. Activation occurs upon recruitment to a complex containing a p53-induced death domain protein, PIDD. This suggests caspase-2 can be a nuclear initiator caspase with a requirement for caspase-9 and caspase-3 activation in downstream apoptotic events. In apoptotic pathways resulting from UV-induced DNA damage, processing of caspase-2 occurs downstream of mitochondrial dysfunction and of caspase-9 and caspase-3 activation, extending a possible role for caspase-2 as a parallel effector caspase.
Product References
Caspase-2 is not required for thymocyte or neuronal apoptosis even though cleavage of caspase-2 is dependent on both Apaf-1 and caspase-9: L.A. O'Reilly, et al.; Cell Death Differ. 9, 832 (2002)
A novel Apaf-1–independent putative caspase-2 activation complex: S.H. Read, et al.; J. Cell Biol. 159, 739 (2002)
A Novel Caspase-2 Complex Containing TRAF2 and RIP1: M. Lamkanfi, et al.; J. Biol. Chem. 280, 6923 (2005)
Death domain assembly mechanism revealed by crystal structure of the oligomeric PIDDosome core complex: H.H. Park, et al.; Cell 128, 533 (2007)
Caspase-2 activation in the absence of PIDDosome formation: C. Manzl, et al.; J. Cell Biol. 185, 291 (2009)
LBH589, a deacetylase inhibitor, induces apoptosis in adult T-cell leukemia/lymphoma cells via activation of a novel RAIDD-caspase-2 pathway: H. Hasegawa, et al.; Leukemia 25, 575 (2011)
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