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About This Item
Specific activity:
≥5000 units/mg protein
Recombinant:
expressed in E. coli
recombinant
expressed in E. coli
form
powder
specific activity
≥5000 units/mg protein
mol wt
30 kDa
UniProt accession no.
storage temp.
−70°C
Gene Information
human ... CASP1(834)
General description
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, 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.
Application
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.
Biochem/physiol Actions
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.
Physical form
Powder also contains 0.052% ammonium sulfate, 0.158% Tris HCl, and 0.76% sodium chloride.
Other Notes
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.
Storage Class
11 - Combustible Solids
wgk
WGK 3
Regulatory Information
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Functional Significance of Conserved Cysteines in the Extracellular Loops of the ATP Binding Cassette Transporter Pdr11p
Stanchev LD, et al.
Journal of Fungi, 7(1), 2-2 (2021)
Franz Kapplusch et al.
Clinical immunology (Orlando, Fla.), 208, 108232-108232 (2019-06-30)
CASP1 variants result in reduced enzymatic activity of procaspase-1 and impaired IL-1β release. Despite this, affected individuals can develop systemic autoinflammatory disease. These seemingly contradictory observations have only partially been explained by increased NF-κB activation through prolonged interaction of variant
Cornelius Y Taabazuing et al.
Cell chemical biology, 24(4), 507-514 (2017-04-11)
Pyroptosis is a lytic form of programmed cell death mediated by the inflammatory caspase-1, -4, and -5. We recently discovered that small-molecule inhibitors of the serine peptidases DPP8 and DPP9 (DPP8/9) induce pro-caspase-1-dependent pyroptosis in monocytes and macrophages. Notably, DPP8/9 inhibitors
A Denes et al.
Cell death & disease, 3, e338-e338 (2012-07-06)
Caspase-1, formerly known as interleukin (IL)-1-converting enzyme is best established as the protease responsible for the processing of the key pro-inflammatory cytokine IL-1β from an inactive precursor to an active, secreted molecule. Thus, caspase-1 is regarded as a key mediator
Caspase-1 inhibition prevents glial inflammasome activation and pyroptosis in models of multiple sclerosis
McKenzie BA, et al.
Proceedings of the National Academy of Sciences, 115(26), E6065-E6074 (2018)
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