Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate SRRM2 in samples. An antibody specific for SRRM2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySRRM2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for SRRM2 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 SRRM2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:The deduced 2,752-amino acid protein has multiple R, S, and P residues, numerous phosphorylation sites, and a predicted molecular mass of 300 kD, suggesting that it may be the full-length protein. Immunoblot analysis detected GST fusion proteins of greater than 300 kD in human and rat cells. Northern blot analysis revealed expression of a 9.0- to 10.0-kb SRL300 transcript in all tissues and cell lines tested.Like SRM160, the deduced 2,296-amino acid SRM300 protein is rich in serine (S), arginine (R), and proline (P), has numerous SR dipeptides and 2 long polyserine domains, and lacks an RNA recognition domain. Reconstitution of SRM160/SRM300-depleted splicing reactions with recombinant SRM160 restored splicing activity, suggesting that SRM160 is the more important component of the complex.
