Description
Description: This assay employs a two-site sandwich ELISA to quantitate MOCS2 in samples. An antibody specific for MOCS2 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any MOCS2 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for MOCS2 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 MOCS2 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: Eukaryotic molybdoenzymes use a unique molybdenum cofactor (MoCo) consisting of a pterin, termed molybdopterin, and the catalytically active metal molybdenum. MoCo is synthesized from precursor Z by the heterodimeric enzyme molybdopterin synthase. The large and small subunits of molybdopterin synthase are both encoded from this gene by overlapping open reading frames. The proteins were initially thought to be encoded from a bicistronic transcript. They are now thought to be encoded from monocistronic transcripts. Alternatively spliced transcripts have been found for this locus that encode the large and small subunits. Highest levels are found in heart and skeletal muscle. Lower levels are present in brain, kidney and pancreas. Very low levels are found in lung and peripheral blood leukocytes