Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate PYDC2 in samples. An antibody specific for PYDC2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyPYDC2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PYDC2 is added to the wells. After washing, Streptavidin conjugated Horseradish Peroxidase (HRP) is added to the wells. Following a wash to remove any unbound avidin-enzyme reagent, a substrate solution is added to the wells and color develops in proportion to the amount of PYDC2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Pyrin domain (PYD) proteins have recently emerged as important signaling molecules involved in the development of innate immunity against intracellular pathogens through activation of inflammatory mediator pathways. It is modulated by a cellular PYD-only protein (cPOP1), which binds to ASC and interferes with the recruitment of ASC to activated PYD-NLRs. POP (cPOP2), which shows highest homology to the PYD of PAN1. cPOP2 binds to ASC and PAN1, thereby blocking formation of cryopyrin and PAN1-containing inflammasomes, activation of caspase-1, and subsequent processing and secretion of bioactive interleukin-1beta. Existence of a second cPOP provides additional insights into inflammasome formation and suggests that POPs might be a common regulatory mechanism to "fine-tune" the activity of specific PYD-NLR family protein-containing inflammasomes.
