Detection Method:Sandwich
Test principle:This assay employs a two-site sandwich ELISA to quantitate DNAJC12 in samples. An antibody specific for DNAJC12 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyDNAJC12 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for DNAJC12 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 DNAJC12 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Product Overview:Highly conserved C terminus, but lack the G/F-rich and CRR domains. Hahn et al. (1999) identified a J domain-containing protein in mouse and Drosophila. By database searching for sequences homologous to these proteins, Lee et al. (2000) identified a human homolog, which they designated JDP1, that has 2 isoforms generated by alternative use of polyadenylation sites. The primary isoform is 1.2 kb long and encodes a 198-amino acid protein; the other is 0.7 kb long and encodes a 107-amino acid protein. The 198-amino acid protein shares approximately 77% sequence identity with the mouse protein. Northern blot analysis detected a single transcript of 1.3 kb at high levels in brain, heart, and testis, and at reduced levels in kidney and stomach. In mouse and Drosophila, expression is highest in kidney and restricted to heads, respectively.
