The CHIP protein encoded by this gene binds to and inhibits the ATPase activity of the chaperone proteins HSC70 and HSP70 and blocks the forward reaction of the HSC70-HSP70 substrate-binding cycle. In addition, CHIP possesses E3 ubiquitin ligase activity and promotes ubiquitylation. CHIP enhances HSP70 induction during acute stress and also mediates its turnover during the stress recovery process. The deduced 303-amino acid proteinhas a molecular mass of 35 kD and contains three 34-amino acid TPR domains at its N terminus, a central domain rich in charged residues, and 2 potential nuclear localization signals. Human CHIP shares 97% and 53% amino acid identity with its mouse and Drosophila homologs, respectively, with the highest conservation in the 94 residues of the C terminus.
Human E3 ubiquitin-protein ligase CHIP (STUB1) ELISA Kit employs a two-site sandwich ELISA to quantitate STUB1 in samples. An antibody specific for STUB1 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anySTUB1 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for STUB1 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 STUB1 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Human E3 ubiquitin-protein ligase CHIP (STUB1) ELISA Kit listed herein is for research use only and is not intended for use in human or clinical diagnosis. Suggested applications of our products are not recommendations to use our products in violation of any patent or as a license. We cannot be responsible for patent infringements or other violations that may occur with the use of this product.
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