anti-Gasdermin D (mouse) pAb (IN110)

Gasdermin Domain-containing Protein 1; Gasdermin-D (C-terminal); GSDMD-CT; Gsdmd

1mg/ml

32160000

liquid

Liquid. In PBS containing 10% glycerol and 0.02% sodium azide.

After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.

Recombinant mouse gasdermin D (C-terminus).

Polyclonal Antibody. Recognizes full-length and cleaved C-terminus domain of mouse gasdermin D. Does not cross-react with human gasdermin D. Source/Host: Guinea pig. Applications: ELISA, WB. Liquid. In PBS containing 10% glycerol and 0.02% sodium azide. 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-1beta and -18 (IL-1beta and IL-18) through proteolytic cleavage of pro-IL-1beta 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.

Q9D8T2

Plastic Vial

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-1beta and -18 (IL-1beta and IL-18) through proteolytic cleavage of pro-IL-1beta 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.

>95% (SDS-PAGE)

Guinea pig

Recognizes full-length and cleaved C-terminus domain of mouse gasdermin D. Does not cross-react with human gasdermin D.

Non-hazardous

Primary Antibodies

12352203

Stable for at least 1 year after receipt when stored at -20°C.