Caspase 1 [14F468]

GWB-EFA82C

IgG1Light chain: kappa

Human

Caspase 1

0. 05% Sodium Azide; Constituents: 0. 2% Gelatin PBS

Cytoplasmic Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis. The precursor form of all caspases is composed of a prodomain and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit which associate into a2b2 tetramer to form the active enzyme. Caspase 1 is similar to the cell death gene CED3 of C. elegans and regulates multiple proinflammatory cytokines including Interleukin 1b and interferon-gamma-inducing factor. Caspase 1 plays a role in down stream of Caspase 8 which is involved in Fas-mediated apoptosis.

Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|-.

Heterotetramer that consists of two anti-parallel arranged heterodimers each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit. The p20 subunit can also form a heterodimer with the epsilon isoform which then has an inhibitory effect. May be a component of the inflammasome a protein complex which also includes PYCARD CARD8 and NALP2 and whose function would be the activation of proinflammatory caspases. Interacts with INCA.

Expressed in larger amounts in spleen and lung. Detected in liver heart small intestine colon thymus prostate skeletal muscle peripheral blood leukocytes kidney and testis. No expression in the brain.

Belongs to the peptidase C14A family [view classification].