Research area: Apoptosis

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.

Caspase 1 human has been used:

• in in vitro cleavage assay with Rab interacting lysosomal protein (RILP).
• in the cleavage of caspases-3/7 in human monocytic cells (THP1).
• in SDS-PAGE for digesting purified protein samples to understand the structural and functional significance of conserved extracellular loop cysteines in the yeast sterol transporter Pdr11p.
• to assess the inhibitory activity of the compounds by conducting a fluorimetric assay using Ac-YVAD-AMC as a substrate.

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.

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

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.

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