|Gasdermin D (E9S1X) Rabbit mAb 39754||20 µl||
||H M R||53, 30||Rabbit IgG|
|Cleaved Gasdermin D (Asp276) (E3E3P) Rabbit mAb 10137||20 µl||
|IL-1β (D3H1Z) Rabbit mAb 12507||20 µl||
|Cleaved-IL-1β (Asp117) (E7V2A) Rabbit mAb 63124||20 µl||
|Caspase-1 (E2Z1C) Rabbit mAb 24232||20 µl||
||M||48, 10||Rabbit IgG|
|Cleaved Caspase-1 (Asp296) (E2G2I) Rabbit mAb 89332||20 µl||
|Caspase-11 (17D9) Rat mAb 14340||20 µl||
||M||38, 43||Rat IgG2a|
|ASC/TMS1 (D2W8U) Rabbit mAb 67824||20 µl||
|HMGB1 (D3E5) Rabbit mAb 6893||20 µl||
||H M R Mk||29||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Leu60 of mouse Gasdermin D, His124 of mouse IL-1β, Ala137 of human HMGB1, a peptide near the carboxy terminus of mouse caspase-1, a recombinant fragment specific to the p30 subunit of mouse caspase-11, and a recombinant fragment specific to mouse ASC/TMS1 protein. Cleavage specific monoclonal antibodies are produced by immunizing animals with synthetic peptides corresponding to residues surrounding Asp296 of mouse caspase-1, Asp117 of mouse IL-1β, and Asp276 of mouse Gasdermin D protein.
Pyroptosis is a regulated pathway of cell death with morphological features of necrosis, including cell swelling, plasma membrane pore formation, and engagement of an inflammatory response with the release of a number of damage-associated molecular patterns (DAMPs), such as HMGB1 and inflammatory cytokines like IL-1β and IL-18 (1,2). Pyroptosis is generally induced in cells of the innate immune system, such as monocytes, macrophages, and dendritic cells in the presence of pathogen-associated molecular patterns (PAMPs) expressed on microbial pathogens or by cell-derived DAMPs. It is induced through assembly of inflammasomes triggering proteolytic activation of caspase-1 which then cleaves inflammatory cytokines like IL-1β and IL-18 to their mature forms (3). A critical feature of pyroptosis is the cleavage of Gasdermin D by caspase-1 and mouse caspase-11 (or human caspase-4/5) (4-6). Upon cleavage, the N-terminal fragment of Gasdermin D oligomerizes to form a pore, allowing secretion of inflammatory DAMPs and cytokines. Canonical inflammasome assembly typically consists of a cytosolic-pattern recognition receptor (PPR; a nucleotide binding domain and leucine-rich repeat [NLR] or AIM2-like family members), an adaptor protein (ASC/TMS1), and pro-caspase-1. Distinct inflammasome complexes can recognize distinct PAMPs and DAMPs to trigger pyroptosis. The best characterized pathway triggered by the NLR, NLRP3, occurs through a two-step process. The first step is a priming signal, NF-κB is activated to induce the expression of a number of inflammasome components including NLRP3, pro-IL-1β, and pro-IL-18. In the second activation step, caspase-1 is activated and Gasdermin D and cytokines are proteolytically activated. In a non-canonical pathway, caspase-4 and caspase-5 can directly trigger Gasdermin D cleavage in monocytes following LPS stimulation (5,7).
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