Cleaved Drosophila Dcp-1 (Asp215) Antibody #9578
- WB
- IF
Supporting Data
| REACTIVITY | Dm |
| SENSITIVITY | Endogenous |
| MW (kDa) | 22 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- Dm-D. melanogaster
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:800 |
Storage
Protocol
Specificity / Sensitivity
Cleaved Drosophila Dcp-1 (Asp215) Antibody recognizes endogenous levels of the large 22 kDa fragment of cleaved Dcp-1. This antibody does not recognize full length Dcp-1. The antibody also detects a non-specific, apoptotic-related band at 50 kDa by western blot.
Species Reactivity:
D. melanogaster
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to amino-terminal residues adjacent to Asp215 of Drosophila Dcp-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
Cell death in the fruit fly Drosophila melanogaster is regulated by many of the same stimuli as mammalian cell death (1). The Drosophila genome contains seven caspase genes; three encode initiator caspases, and four encode effector caspases (reviewed in (2)). The Drosophila effector caspase, death caspase-1 (Dcp-1), is a critical executioner of apoptosis. It is involved in the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly (ADP-ribose) polymerase (PARP). The activation of Dcp-1 requires proteolytic processing of its inactive zymogen into active p22 and p13 fragments (3). Comparison of the in vivo activity between DrICE and Dcp-1 has shown that DrICE is a more effective inducer of apoptosis than Dcp-1, which instead plays a role in determining the rate of cell death (4).
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