Description
Description: This assay employs a two-site sandwich ELISA to quantitate MARCKSL1 in samples. An antibody specific for MARCKSL1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any MARCKSL1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for MARCKSL1 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 MARCKSL1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: The myristoylated, alanine-rich protein MARCKS is a widely expressed, prominent substrate for protein kinase C, a key enzyme of intracellular signal transduction. The predicted 200-amino acid protein, which they called F52, shares 52% amino acid identity with bovine MARCKS. The similarity between the 2 proteins is found in the consensus myristoylation sequence near the N-terminus and in the 25-amino acid protein kinase C phosphorylation site domain. F52 has a similar amino acid composition to MARCKS, although its alanine content is not as high. It is distributed throughout the mouse brain in a pattern that is distinct from that of MARCKS.A transgene containing this 433-bp fragment from mouse linked to a reporter Mrp beta-galactosidase gene produced normal patterns of Mrp expression in the developing mouse embryo