Gasdermin D (mouse) ELISA Kit

CHF 690.00
In stock
AG-45B-0011-KI0196 wellsCHF 690.00
NEW
More Information
Product Details
Synonyms Gasdermin Domain-containing Protein 1; Gasdermin-D (C-terminal); GSDMD-CT; Gsdmd
Product Type Kit
Properties
Application Set Quantitative ELISA
Specificity

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.

Crossreactivity Mouse
Quantity

1 x 96 wells

Sensitivity 14pg/ml
Range 15.6 to 1000pg/ml
Sample Type Cell Culture Supernatant
Cell Lysate
Assay Type Sandwich
Detection Type Colorimetric
Other Product Data

UniProt link Q9D8T2: Gasdermin D (mouse)

Also available: EMBO Inflammasome Symposia 2018 - Official Gasdermin D (mouse) ELISA Kit Poster! for download

Accession Number Q9D8T2
Shipping and Handling
Shipping BLUE ICE
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.
Documents
Manual Download PDF
MSDS Inquire
Product Specification Sheet
Datasheet Download PDF

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.

© 2017 Adipogen Life Sciences. Pictures: © 2012 Martin Oeggerli. All Rights Reserved.