Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate USP6NL in samples. An antibody specific for USP6NL has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyUSP6NL present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for USP6NL 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 USP6NL bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:HAUSPis a ubiquitin specific protease or a deubiquitylating enzyme that cleaves ubiquitin from its substrates.Since ubiquitylation (polyubiquitination) is most commonly associated with the stability and degradation of cellular proteins, HAUSP acitivity generally stabilizes its substrate proteins. HAUSP is most popularly known as a direct antagonist of Mdm2, the E3 ubiquitin ligase for the tumor suppressor protein, p53. Normally, p53 levels are kept low in part due to Mdm2-mediated ubiquitylation and degradation of p53. Interestingly, in response to oncogenic insults, HAUSP can deubiquitinate p53 and protect p53 from Mdm2-mediated degradation, indicating that it may possess a tumor suppressor function for the immediate stabilization of p53 in response to stress.
