Proteases play critical roles in the initiation and execution of apoptosis. The caspases (EC 3.4.22.xx), a family of cysteine-dependent aspartate-directed proteases, are prominent among the death proteases. Caspases are synthesized as relatively inactive zymogens that become activated by scaffold-mediated transactivation or by cleavage via upstream proteases in an intracellular cascade. Regulation of caspase activation and activity occurs at several different levels. Once activated, caspases cleave a variety of intracellular polypeptides, including major structural elements of the cytoplasm and nucleus, components of the DNA repair machinery, and a number of protein kinases. Collectively, these scissions disrupt survival pathways and disassemble important architectural components of the cell, contributing to the stereotypic morphological and biochemical changes that characterize apoptotic cell death[1].

Caspase subclasses listed: Caspase, Procaspase

[1] W.C. Earnshaw et al. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 1999, 68, 383-424.

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2158 Boc-D-FMK Broad spectrum caspase inhibitor €110.00
1375 Ivachtin Caspase-3 inhibitor €55.00
3744 KEA1-97 Thioredoxin-caspase 3 interaction disruptor €90.00
3149 TC11 Anti-tumor agent; Apoptosis inducer €110.00
3857 VX-765 Caspase-1 inhibitor Inquire
2159 Z-VAD-FMK Pan-caspase inhibitor with in vivo activity Inquire

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