Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SRMS in samples. An antibody specific for SRMS has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySRMS present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SRMS 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 SRMS bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:It has SH2, SH2', and SH3 domains and a tyrosine residue for autophosphorylation in the kinase domain but lacks an N-terminal glycine for myristylation and a C-terminal tyrosine which, when phosphorylated, suppresses kinase activity. These are structural features of the recently identified Tec family of nonreceptor tyrosine kinases. The Srm N-terminal unique domain, however, lacks the structural characteristics of the Tec family kinases, and the sequence similarity is highest to Src in the SH region. Mutant mice were generated by gene targeting in embryonic stem cells but displayed no apparent phenotype as in mutant mice expressing Src family kinases. These results suggest that Srm constitutes a new family of nonreceptor tyrosine kinases that may be redundant in function.
