Application

Caspase 1 human has been used in in vitro cleavage assay with Rab interacting lysosomal protein (RILP) and in the cleavage of caspases-3/7 in human monocyticcells (THP1).

Biochem/physiol Actions

Useful in screening caspase inhibitors, studying enzyme regulation and kinetics, determining target substrate or as a positive control in caspase-1 activity assays.

Caspase 1 catalyzes the conversion of pro-inflammatory cytokine, pro-interleukin (IL)-1β to its active form. It has broad substrate specificity and is an apoptosis regulator. Caspase-1 is indirectly implicated in the pathology of cryopyrin-associated periodic syndrome (CAPS). It is a multiple inflammasome-associated protein associated with multiple sclerosis (MS) lesions and is a prime target for inhibitor screening.

General description

Caspase 1, also called interleukin (IL)-1-converting enzyme, is mapped to human 11q22.3. It belongs to the aspartate-specific cysteine proteases family and is primarily synthesized as procaspase-1 zymogen, which later become catalytically active post autoproteolysis. The enzymatically active caspase-1 comprises two p20/p10 heterodimer making it a tetramer.

Physical form

Powder also contains 0.052% ammonium sulfate, 0.158% Tris HCl, and 0.76% sodium chloride.

Unit Definition

One unit will hydrolyze 1 nmol of the caspase substrate, YVAD-pNA to YVAD and p-nitroaniline per hour at pH 7.2 and 37 °C.