Description
Principle of the assay: This assay employs a two-site sandwich ELISA to quantitative CAM1 in Human serum, plasma. An antibody specific for CAM1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any CAM1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin - conjugated antibody specific for CAM1 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 CAM1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Background: Mast cell chymase is a chymotryptic serine proteinase that belongs to the peptidase family S1. It is expressed in mast cells and thought to function in the degradation of the extracellular matrix, the regulation of submucosal gland secretion, and the generation of vasoactive peptides. In the heart and blood vessels, this protein, rather than angiotensin converting enzyme, is largely responsible for converting angiotensin I to the vasoactive peptide angiotensin II. Angiotensin II has been implicated in blood pressure control and in the pathogenesis of hypertension, cardiac hypertrophy, and heart failure. Thus, this gene product is a target for cardiovascular disease therapies. This gene maps to 14q11.2 in a cluster of genes encoding other proteases