Explore Our Biomarker Menu



Biological or Clinical Significance:

Caspase-1 was first described in 1989 as the cysteine proteinase responsible for the production of interleukin 1-beta (IL-1-beta) in monocytes, hence its original name, interleukin 1beta-converting enzyme (ICE). When it was first purified, cloned and sequenced in 1992, it was found to be unrelated to any known protein. Late in 1993, it was shown to be homologous to CED-3, the product of a gene required for programmed cell death in the nematode Caenorhabditis elegans.

The crystallographic structure of caspase-1 reported in 1994 identified the residues important for binding and catalysis, and confirmed its relationship to CED-3. To date, 12 related paralogs of human origin have been described. In 1996, a unified nomenclature was introduced for these enzymes, which uses the trivial name ‘caspase’ as a root for serial names. The ‘c’ reflects a cysteine proteinase mechanism, and ‘aspase’ relates to their ability to cleave after Asp, the most distinguishing catalytic property of this family.





Human Serum


Experienced Running


0.66 pg/mL




Required Sample Volume

Disease State:

MSD Panel:

Speak To A Scientist

    I consent to receive communications (which may include, phone, email, social, and re-targeting ads) from BioAgilytix. I understand I may proactively manage my preferences or opt-out of communications with BioAgilytix at any time using the unsubscribe link provided in all of BioAgilytix’s email communications and can learn more by reading the privacy policy.


    Learn why BioAgilytix is a world-leading authority on immunogenicity studies related to ADA, NAb assay development and validation, isotyping, and more.

    Case Studies

    Learn why we’re a trusted partner to 22 of the top 25 global pharma and biotech companies.