This Casp1 Sandwich ELISA is an in-vitro enzyme-linked immunosorbent assay for the measurement of samples in mouse serum, plasma and other biological fluids.
Applications
ELISA
Reactivity
Mouse
Sensitivity
18.75pg/mL
Detection Limit
31.25~2000pg/mL
Note
FOR SCIENTIFIC EDUCATIONAL RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR OTHER MEDICAL APPLICATIONS.
Product Properties
Storage Instruction
If unopened the kit may be stored at 2-8°C for up to 1 month. If the kit will not be used within 1 month, store the components separately, according to the component table in the manual.
This kit recognizes Mouse CASP1 in samples. No significant cross-reactivity or interference between Mouse CASP1 and analogues was observed.
Sample Type
Serum, plasma and other biological fluids
Additional Info
Post Translational Modifications
The two subunits are derived from the precursor sequence by an autocatalytic mechanism. Ubiquitinated via 'Lys-11'-linked polyubiquitination. Deubiquitinated by USP8.
Function
Thiol protease involved in a variety of inflammatory processes by proteolytically cleaving other proteins, such as the precursors of the inflammatory cytokines interleukin-1 beta (IL1B) and interleukin 18 (IL18) as well as the pyroptosis inducer Gasdermin-D (GSDMD), into active mature peptides. Plays a key role in cell immunity as an inflammatory response initiator: once activated through formation of an inflammasome complex, it initiates a pro-inflammatory response through the cleavage of the two inflammatory cytokines IL1B and IL18, releasing the mature cytokines which are involved in a variety of inflammatory processes. Cleaves a tetrapeptide after an Asp residue at position P1. Also initiates pyroptosis, a programmed lytic cell death pathway, through cleavage of GSDMD. In contrast to cleavage of interleukin IL1B, recognition and cleavage of GSDMD is not strictly dependent on the consensus cleavage site but depends on an exosite interface on CASP1 that recognizes and binds the Gasdermin-D, C-terminal (GSDMD-CT) part. Cleaves and activates CASP7 in response to bacterial infection, promoting plasma membrane repair. Upon inflammasome activation, during DNA virus infection but not RNA virus challenge, controls antiviral immunity through the cleavage of CGAS, rendering it inactive. In apoptotic cells, cleaves SPHK2 which is released from cells and remains enzymatically active extracellularly.
