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Porcine CASP1 (Caspase-1) ELISA Kit
Porcine CASP1 (Caspase-1) ELISA Kit
The Porcine (CASP1) Caspase-1 ELISA Kit measures Caspase-1 in Porcine samples. The plate has been pre-coated with Porcine CASP1 antibody. CASP1 present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Porcine CASP1 Antibody is added and binds to CASP1 in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated CASP1 antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Porcine CASP1. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
Catalog No:
E0541Po
Regular price
$595.00 USD
Regular price
$458.00 USD
Sale price
$595.00 USD
Unit price
/
per
2.5 weeks
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Product Details
Species Reactivity
Porcine
Sensitivity
7.15 ng/L
Detection Range
15-3000 ng/L
Sample Type
Serum, plasma, cell culture supernates
Incubation(s)
1.5 hour(s)
Research Areas
Cell Biology, Cancer, Metabolism, Apoptosis
Background
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 proinflammatory 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 interleukins IL1B and 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. 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. Source: UniProt Consortium (2025)
Shipping Condition
Shipped on cold gel packs.
Storage Condition and Shelf Life
2-8C
Analyte
Caspase-1
Regulatory Status
For Research Use Only
