Description
Description: This assay employs a two-site sandwich ELISA to quantitate XPNPEP1 in samples. An antibody specific for XPNPEP1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any XPNPEP1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for XPNPEP1 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 XPNPEP1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: X-prolyl aminopeptidase is a proline-specific metalloaminopeptidase that specifically catalyzes the removal of any unsubstituted N-terminal amino acid that is adjacent to a penultimate proline residue. Because of its specificity toward proline, it has been suggested that X-prolyl aminopeptidase is important in the maturation and degradation of peptide hormones, neuropeptides, and tachykinins, as well as in the digestion of otherwise resistant dietary protein fragments, thereby complementing the pancreatic peptidases.
XPNPEPL, that encodes a 623-amino acid protein exhibiting 44% sequence identity and 62% sequence similarity to pig kidney X-prolyl aminopeptidase and high sequence homology to proteins in S. pombe and S. cerevisiae