Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate STK17B in samples. An antibody specific for STK17B has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySTK17B present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for STK17B 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 STK17B bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The full-length STK17B cDNA clone encodes a deduced 372-amino acid protein with a molecular mass of 42.34 kD. The putative kinase domain is located at the N terminus and contains all 11 subdomains conserved among ser/thr kinases. STK17A and STK17B share 59.7% amino acid identity. Northern blot analysis revealed that STK17B is expressed in various tissues, such as heart, placenta, liver, and pancreas, as different sized transcripts, presumably due to differences in the 3-prime untranslated region. An in vitro assay demonstrated that STK17B is capable of autophosphorylation and of phosphorylating myosin light chain as an exogenous substrate, but with lower kinase activity than STK17A. Unlike STK17A, an STK17B mutant lacking the noncatalytic C terminus had higher kinase activity than the full-length STK17B.
