Description
Principle of the assay: This assay employs a two-site sandwich ELISA to quantitative CAMP in Mouse serum, plasma. An antibody specific for CAMP has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any CAMP present is bound by the immobilized antibody. After removing any unbound substances, a biotin - conjugated antibody specific for CAMP 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 CAMP bound in the initial step. The color development is stopped and the intensity of the color is measured.
Background: Cathelicidin antimicrobial peptide is a family of polypeptides found in lysosomes in polymorphonuclear leukocytes (PMNs).Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain. Cathelicidin peptides have been isolated from many different species of mammals. Cathelicidins were originally found in neutrophils but have since been found in many other cells including epithelial cells and macrophages activated by bacteria, viruses, fungi, or the hormone 1,25-D. The cathelicidin family shares primary sequence homology with the cathepsin family of cysteine proteinase inhibitors, although amino acid residues thought to be important in such protease inhibition are usually lacking