Description
Description: This assay employs a two-site sandwich ELISA to quantitate ZCWPW1 in samples. An antibody specific for ZCWPW1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any ZCWPW1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for ZCWPW1 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 ZCWPW1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: The zinc finger CW (zf-CW) domain is a motif of about 60 residues that is frequently found in proteins involved in epigenetic regulation. The NMR solution structure of the zf-CW domain of the human zf-CW and PWWP domain containing protein 1 (ZCWPW1). The zf-CW domain adopts a new fold in which a zinc ion is coordinated tetrahedrally by four conserved Cys ligand residues. The tertiary structure of the zf-CW domain partially resembles that adopted by the plant homeo domain (PHD) finger bound to the histone tail, suggesting that the zf-CW domain and the PHD finger have similar functions. The solution structure of the complex of the zf-CW domain with the histone H3 tail peptide (1-10) with trimethylated K4 clarified its binding mode. zf-CW domain as a member of the histone modification reader modules for epigenetic regulation