Mouse Caspase-3 Recombinant mAb (S-3976-60)

Caspase-3 (cysteine-aspartic protease 3) is the most critical enzyme in the execution phase of apoptosis (programmed cell death), often referred to as the "death execution protease," and occupies a central hub in the apoptotic cascade. It typically exists in the cytoplasm as an inactive zymogen (pro-caspase-3). Upon receiving intrinsic (such as cytochrome c release from mitochondria) or extrinsic (such as death receptor activation) apoptotic signals, it is activated through proteolytic cleavage by upstream initiator caspases (such as caspase-8 and caspase-9). Activated caspase-3 subsequently cleaves a series of key substrates, including the DNA repair enzyme PARP, structural proteins (such as nuclear lamins), and cytoskeletal proteins, ultimately leading to a series of characteristic apoptotic morphological features including DNA fragmentation, membrane blebbing, and cell shrinkage. This irreversible execution function makes caspase-3 a hallmark molecule in apoptosis research, and its aberrant activity plays a decisive role in various diseases—insufficient activity leads to tumor immune evasion and resistance to chemotherapy, representing a major mechanism of drug resistance in cancer; conversely, excessive activity is closely associated with excessive neuronal death in neurodegenerative diseases (such as Alzheimer's disease and Huntington's disease) and ischemic injury. Therefore, caspase-3 as a drug target—whether as inhibitors for neuroprotection or as activators for cancer therapy—holds significant value in both basic research and clinical translation.