Recombinant Human CASP6 protein

**Background of CASP6 Recombinant Protein**

Caspase-6 (CASP6) is a member of the cysteine-aspartic protease (caspase) family, primarily involved in apoptosis (programmed cell death) and inflammation. As an executioner caspase, it is activated during the later stages of apoptosis, cleaving specific substrates to dismantle cellular structures and promote cell death. CASP6 is synthesized as an inactive zymogen (procaspase-6) containing an N-terminal prodomain, followed by large and small catalytic subunits. Proteolytic processing by upstream caspases (e.g., caspase-3 or -7) removes the prodomain, enabling CASP6 to form an active heterotetramer. Beyond apoptosis, CASP6 is implicated in neurodegenerative diseases, such as Alzheimer’s and Huntington’s, due to its role in cleaving pathogenic proteins like amyloid precursor protein (APP) and huntingtin.

Recombinant CASP6 protein is produced via genetic engineering, typically using bacterial (e.g., *E. coli*) or mammalian expression systems. The recombinant form retains enzymatic activity, enabling studies on its substrate specificity, activation mechanisms, and interaction with inhibitors. Purification often involves affinity tags (e.g., His-tag) followed by chromatography. Researchers use recombinant CASP6 to investigate its pathological roles, screen therapeutic inhibitors, and model caspase-driven pathways *in vitro*. Its study is critical for understanding disease mechanisms and developing targeted therapies, particularly for neurodegeneration. However, CASP6’s dual roles in apoptosis and disease underscore the need for precise regulation, making it a complex but compelling target for biomedical research.