Death-associated protein 5 (DAP-5) (also known as p97 and NAT1) is a member of the eukaryotic translation initiation factor 4G (elF4G) family. DAP-5 is ubiquitously expressed and is highly conserved among species. In response to activated FAS or p53, caspase cleaves DAP-5 at position 790 to yield a C-terminal truncated protein which is capable of forming complexes with eIF4A and eIF3. DAP-5 has homology to the carboxy-terminal portion of eIF4G, but lacks the N-terminal region of eIF4G, which is responsible for association with the CAP binding protein eIF4E. By forming translationally inactive complexes with eIF4A and eIF3, but not with eIF4E, DAP-5 functions as a general repressor of translation. During apotosis, the caspase-activated DAP-5 can mediate CAP-independent translation at least from its own internal ribosome entry site, thus resulting in a positive feedback loop responsible for the continuous translation of DAP-5. DAP-5 is also required for cellular differentiation, as it controls specific gene expression pathways.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
DAP-5 (N65) polyclonal antibody detects endogenous levels of DAP-5 protein.
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