|NLRP3 (D4D8T) Rabbit mAb 15101||20 µl||
||H M||110||Rabbit IgG|
|AIM2 Antibody 63660||20 µl||
|ASC/TMS1 (D2W8U) Rabbit mAb 67824||20 µl||
|Cleaved-IL-1β (Asp117) (E7V2A) Rabbit mAb 63124||20 µl||
|IL-1β (D6D6T) Rabbit mAb 31202||20 µl||
||M||17, 31||Rabbit IgG|
|Cleaved Caspase-1 (Asp296) (E2G2I) Rabbit mAb 89332||20 µl||
|Caspase-1 (E2Z1C) Rabbit mAb 24232||20 µl||
||M||48, 10||Rabbit IgG|
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Monoclonal antibodies are produced by immunizing animals with recombinant mouse ASC/TMS1 protein, recombinant mouse IL-1β protein, or with synthetic peptides corresponding to residues surrounding Asp117 of mouse IL-1β, Asp296 of mouse caspase-1, residues near the carboxy terminus of mouse caspase-1, or residues surrounding Ala306 of mouse NLRP3. Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Val104 of mouse AIM2 protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography.
The innate immune system works as the first line of defense in protection from pathogenic microbes and host-derived signals of cellular distress. One way in which these “danger” signals trigger inflammation is through activation of inflammasomes, which are multiprotein complexes that assemble in the cytosol after exposure to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) and result in the activation of caspase-1 and subsequent cleavage of proinflammatory cytokines IL-1β and IL-18 (Reviewed in 1-6). Inflammasome complexes typically consist of a cytosolic pattern recognition receptor (PRR; a nucleotide-binding domain and leucine-rich-repeat [NLR] or AIM2-like receptor [ALR] family member), an adaptor protein (ASC/TMS1), and pro-caspase-1. A number of distinct inflammasome complexes have been identified, each with a unique PRR and activation triggers. The best characterized is the NLRP3 complex, which contains NLRP3, ASC/TMS1, and pro-caspase-1. The NLRP3 inflammasome is activated in a two-step process. First, NF-κB signaling is induced through PAMP- or DAMP-mediated activation of TLR4 or TNFR, resulting in increased expression of NLRP3, pro-IL-1β, and pro-IL-18 (priming step, signal 1). Next, indirect activation of NLRP3 occurs by a multitude of signals (whole pathogens, PAMPs/DAMPs, potassium efflux, lysosomal-damaging environmental factors [uric acid, silica, alum] and endogenous factors [amyloid-β, cholesterol crystals], and mitochondrial damage), leading to complex assembly and activation of caspase-1 (signal 2). The complex inflammasome structure is built via domain interactions among the protein components. Other inflammasomes are activated by more direct means: double-stranded DNA activates the AIM2 complex, anthrax toxin activates NLRP1, and bacterial flagellin activates NLRC4. Activated caspase-1 induces secretion of proinflammatory cytokines IL-1β and -18, but also regulates metabolic enzyme expression, phagosome maturation, vasodilation, and pyroptosis, an inflammatory programmed cell death. Inflammasome signaling contributes to the onset of a number of diseases, including atherosclerosis, type II diabetes, Alzheimer’s disease, and autoimmune disorders.
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