CASP2 Human

Caspase-2, also known as CASP2, is a member of the cysteine-aspartic acid protease (caspase) family. Caspases are crucial for mediating cellular apoptosis through the proteolytic cleavage of specific protein substrates . Caspase-2 is unique among caspases due to its dual role in apoptosis and non-apoptotic cellular processes, including cell cycle regulation and tumor suppression .

Caspase-2 is synthesized as an inactive zymogen that requires proteolytic cleavage to become active. The human recombinant form of Caspase-2 is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 126 amino acids, with a molecular mass of 14.1 kDa . This recombinant protein is often fused to a His-tag for purification purposes .

Caspase-2 is classified as an initiator caspase, meaning it responds to apoptotic stimuli by initiating the apoptotic cascade . It is considered a pro-apoptotic caspase that can induce cell death through the cleavage of various substrates. However, its exact role in apoptosis has been a subject of debate due to conflicting evidence regarding its necessity for this process .

Emerging evidence suggests that Caspase-2 also plays a role in non-apoptotic processes such as cell cycle regulation and protection from genomic instability . These functions are particularly relevant to its role as a tumor suppressor. Caspase-2 has been identified as a tumor suppressor in multiple tissue types, although the mechanisms underlying this function are not fully understood .

Increased expression of Caspase-2 has been implicated in various neurodegenerative disorders, including Alzheimer’s disease, Huntington’s disease, and temporal lobe epilepsy . Its role in stress-induced cell death pathways and tumor suppression makes it a potential target for therapeutic interventions in cancer and neurodegenerative diseases .