Recombinant CASP4 protein (His tag)

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Recombinant Human Caspase-4 Fragment (CASP-4, residues 105-261) is a high-purity protein product designed for structural and biochemical studies. This 157-amino acid fragment, derived from the inflammatory caspase involved in non-canonical inflammasome signaling and pyroptosis, offers a stable and soluble unit ideal for investigating caspase-4 function and interactions in innate immunity.

Caspase-4 (CASP-4) is an inflammatory caspase that serves as the effector of the non-canonical inflammasome, mediating lipopolysaccharide (LPS)-induced pyroptosis and indirectly activating NLRP3 and NLRP6 inflammasomes. It functions as a thiol protease, cleaving substrates like GSDMD, IL18, and CGAS after Asp residues, and plays a critical role in host defense against cytosolic bacteria, endoplasmic reticulum stress, and Alzheimer's-related cell death. The full-length protein localizes to the cytoplasm, endoplasmic reticulum membrane, mitochondria, and inflammasomes, with secretion observed in specific contexts such as UVB irradiation. This fragment corresponds to a computationally selected region (residues 105-261) that excludes known domains, providing a focused tool for exploring caspase-4 mechanisms without confounding functional elements.