Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SH3BP2 in samples. An antibody specific for SH3BP2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySH3BP2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SH3BP2 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 SH3BP2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:SH3BP2 has an N-terminal pleckstrin homology (PH) domain, an SH3-binding proline-rich region, and a C-terminal SH2 domain. The protein binds to the SH3 domains of several proteins including the ABL1 and SYK protein tyrosine kinases , and functions as a cytoplasmic adaptor protein to positively regulate transcriptional activity in T, natural killer (NK), and basophilic cells. Mutations in this gene result in cherubism. Multiple transcript variants encoding different isoforms have been found for this gene.
The deduced 561-residue protein contains an Src homology 2 (SH2) domain, an Src homology 3 (SH3)-binding domain, and a pleckstrin homology domain, suggesting a possible role in signal transduction.
