Apoptosis is programmed cell death characterized by nuclear condensation, cell shrinkage, membrane blebbing, and DNA fragmentation. Caspases, a family of cysteine proteases, are the central regulators of apoptosis. Initiator caspases (including caspase-2, -8, -9, -10, -11, and -12) are closely coupled to pro-apoptotic signals. Once activated, initiation caspases cleave and activate downstream effector caspases (including caspase-3, -6, and -7), which in turn execute apoptosis by cleaving targeted cellular proteins.
Western blot analysis of extracts from C6 (rat), NIH/3T3 (mouse), and Jurkat (human) cells, untreated or treated with staurosporine #9953 (1uM, 3 hrs) or etoposide #2200 (25uM, 5hrs) as indicated, using Cleaved Caspase-3 (Asp175) (5A1E) Rabbit mAb #9664.
Function: Activation of caspase-3 requires cleavage at Asp175 into the activated p17/p19 and p12 protein fragments.
Samples: Jurkat cells were treated with etoposide, an anti-cancer agent that is commonly used to induce apoptosis.
| CST #9664 | Competitor 1 | Competitor 2 | |
|---|---|---|---|
| Product | 9664 | ||
| Dilution | 1:1000 | 1:200* | 1:500* |
| Conc. (μg/mL) | 0.07 | 1 | 1 |
*manufacturer’s recommended starting dilutions.
Function: Activation of caspase-3 requires cleavage at Asp175 into the activated p17/p19 and p12 protein fragments.
Samples: Jurkat cells were treated with Etoposide, an anti-cancer agent that is commonly used to induce apoptosis. C2C12 cells were treated with Staurosporine, a PKC inhibitor that induces apoptosis (1 μM for 3 hours).
