Anti-Caspase-1 (P10) /CASP1 Antibody Picoband® Fluoro488 Conjugated

Caspase 1, apoptosis-related cysteine protease, is a cysteine protease that regulates inflammatory processes through its capacity to process and activate the interleukin-1-beta, IL18, and IL33 precursor proteins. Caspase 1 was purified ICE from the cytosol of the THP. human monocytic cell line and found that the active protease was made up of 2 peptides, which they called p20 and p10 based on their apparent molecular masses by SDS-PAGE. It belongs to a family of cysteine proteases known as caspases that always cleave proteins following an aspartic acid residue. The Caspase1 gene consists of 10 exons spanning at least 10.6 kb. The Caspase 1 gene is mapped to 11q23, a site frequently involved in rearrangement in human cancers, including a number of leukemias and lymphomas, by Southern DNA blot analysis of rodent-human hybrids and by in situ hybridization to normal human metaphase chromosomes. Caspase 1 has been shown to induce cell necrosis or pyroptosis and may function in various developmental stages.

Caspase-1; CASP-1;3.4.22.36; Interleukin-1 beta convertase; IL-1BC; Interleukin-1 beta-converting enzyme; ICE; IL-1 beta-converting enzyme; p45; Caspase-1 subunit p20; Caspase-1 subunit p10; CASP1; IL1BC, IL1BCE

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. .

Thiol protease that cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes. Important for defense against pathogens. Cleaves and activates sterol regulatory element binding proteins (SREBPs) . Can also promote apoptosis. .

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