anti-Gasdermin D (mouse), pAb (IN110)

AdipoGen Life Sciences

anti-Gasdermin D (mouse), pAb (IN110)

10

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

Western Blot, ELISA

Research Use Only

Polyclonal

1 mg/ml

>95%

Liquid

Gsdmd

gasdermin D

1810036L03Rik; AW558049; DF5; DF5L; Dfn; Dfna5l; gasdermin domain containing 1; gasdermin domain-containing protein 1; gasdermin-D; gasderminD-1; GsdmD-1; Gsdmdc; Gsdmdc1; M2-4

Guinea Pig

Gasdermin-D

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. - 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.

Mouse

-20°C,2°C to 8°C

12352203