Description
Description: This assay employs a two-site sandwich ELISA to quantitate ZBTB8OS in samples. An antibody specific for ZBTB8OS has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any ZBTB8OS present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for ZBTB8OS 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 ZBTB8OS bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: The archease protein family is a good example of one of the paradoxes of structural genomics: Approximately one third of protein structures produced by structural genomics centers have no known function and are still annotated as œhypothetical proteins in the Protein Data Bank. In the case of archeases, despite the existence of two protein structures and abundant sequence information, there is still no function assigned to this protein family. based on structural similarity, sequence conservation, and gene context analyses, that members of this protein family might function as chaperones or modulators of proteins involved in DNA/RNA processing. The conservation of genomic context for this protein family is constant from Archaea and Bacteria to humans, and suggests that unannotated open reading frames contiguous to them could be novel RNA/DNA binding proteins