Cat. # AG-25B-0036-C100
|Synonyms||Gasdermin Domain-containing Protein 1; Gasdermin-D (C-terminal); GSDMD-CT; Gsdmd|
|Product Type||Polyclonal Antibody|
|Immunogen/Antigen||Recombinant mouse gasdermin D (C-terminus).|
Western Blot: (1:2'000)*
*Note: We recommend a starting dilution of 1:2'000 and to optimize the dilution depending on your cells/tissues.
Recognizes full-length and cleaved C-terminus domain of mouse gasdermin D. Does not cross-react with human gasdermin D.
|Purity Detail||Protein A affinity purified.|
|Formulation||Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.|
|Other Product Data|
UniProt link Q9D8T2: Gasdermin D (mouse)
|Shipping and Handling|
|Short Term Storage||+4°C|
|Long Term Storage||-20°C|
|Handling Advice||After opening, prepare aliquots and store at -20°C.|
Avoid freeze/thaw cycles.
|Use/Stability||Stable for at least 1 year after receipt when stored at -20°C.|
anti-Gasdermin D (mouse), pAb (IN110) 100 µg
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.