Cat. # AG-45B-0011-KI01
|Synonyms||Gasdermin Domain-containing Protein 1; Gasdermin-D (C-terminal); GSDMD-CT; Gsdmd|
|Application Set||Quantitative ELISA|
Detects full-length and cleaved mouse Gasdermin D (C-terminus) in cell culture supernatants and cell extracts. Does not cross-react with human gasdermin D.
1 x 96 wells
|Range||15.6 to 1000pg/ml|
|Sample Type||Cell Culture Supernatant |
|Other Product Data|| |
UniProt link Q9D8T2: Gasdermin D (mouse)
Also available: EMBO Inflammasome Symposia 2018 - Official Gasdermin D (mouse) ELISA Kit Poster! for download
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||+4°C|
|Handling Advice||After standard reconstitution, prepare aliquots and store at -20°C. |
Avoid freeze/thaw cycles.
Plate and reagents should reach room temperature before use.
|Use/Stability||12 months after the day of manufacturing. See expiry date on ELISA Kit box.|
Gasdermin D (mouse) ELISA Kit 96 wells
Inflammasomes are multimeric protein complexes that comprise a sensor (e.g. NLRP3), an adaptor (ASC/Pycard) and the procaspase-1. An inflammasome assembles in response to a diverse range of pathogen-associated or danger-associated molecular patterns (PAMPs or DAMPs). The inflammasome platform leads to activation of caspase-1, which further induces maturation of interleukin-1β and -18 (IL-1β and IL-18) through proteolytic cleavage of pro-IL-1β and pro-IL-18. Activated caspase-1, and also the recently characterized caspase-11 non-canonical inflammasome pathway, also cleave the intracellular gasdermin D, which leads to a particular form of inflammatory cell death called pyroptosis. The gasdermin family members contain N-terminal domains that are capable of forming membrane pores to induce cytolysis, whereas the C-terminal domains of gasdermins function as inhibitors of such cytolysis through intramolecular domain association. Caspase-1 or -11 cleavage of gasdermin D is required for regulation of pyroptosis: upon protease cleavage of the gasdermin N- and C-domain linker, the disruption of the intramolecular domain interaction in the presence of lipids releases the N-domain to assemble oligomeric membrane pores that trigger cell death. Gasdermin D seems to be a key effector in the LPS-induced lethal sepsis.