Description
Description: This assay employs a two-site sandwich ELISA to quantitate DNAJB11 in samples. An antibody specific for DNAJB11 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any DNAJB11 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for DNAJB11 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 DNAJB11 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: DNAJB11 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus; a glycine/phenylalanine (G/F)-rich region; and a C-terminal cysteine-rich region.The deduced 358-amino acid protein has a calculated molecular mass of 40.5 kD and shares 99% sequence identity with the mouse protein. DNAJB11 contains a conserved J domain, a weak G/F region, and a region that contains 4 cysteines but lacks the zinc finger domain found in some DNAJ proteins. The secondary and tertiary structures of DNAJB11 closely resemble those of HDJ1 (DNAJB1). Northern blot analysis detected transcripts of 1.5 and 2.0 kb in all tissues examined