CASP6 Protein, Human (Active)

CASP6 Protein, Human (Active) is the recombinant human-derived CASP6, expressed by E. coli , with tag Free labeled tag.

CASP6 is a cysteine protease that plays essential roles in programmed cell death, axonal degeneration, development, and innate immunity. It acts as a non-canonical executioner caspase during apoptosis by cleaving nuclear structural proteins NUMA1 and lamin A/LMNA, inducing nuclear shrinkage and fragmentation. CASP6 promotes hepatocyte apoptosis through BID cleavage, contributing to nonalcoholic steatohepatitis. It also cleaves transcription factors like NF-kappa-B and CREBBP, and serves as a central mediator of ZBP1-induced PANoptosis (a hybrid of pyroptosis, apoptosis, and necroptosis) in antiviral defense. Additionally, CASP6 is involved in axon pruning and B-cell program regulation. Similar functions (by similar) include cleaving PARK7/DJ-1 and phospholipid scramblase proteins XKR4/XKR9. During viral infection, CASP6 proteolytically cleaves coronavirus N proteins (e.g., MERS-CoV, SARS-CoV), modulating viral replication by inhibiting IRF3 nuclear translocation and interferon signaling.

Human

E. coli

Tag Free

P55212-1 (A24-N293)

839

Full Length of Isoform-1 Mature Protein

<1 EU/μg, determined by LAL method.