The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans.PRKAR2b is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. This subunit has been shown to interact with and suppress the transcriptional activity of the cAMP responsive element binding protein 1 (CREB1) in activated T cells. Knockout studies in mice suggest that this subunit may play an important role in regulating energy balance and adiposity.
Bovine CAMP-dependent protein kinase type II-beta regulatory subunit (PRKAR2B) ELISA Kit employs a two-site sandwich ELISA to quantitate PRKAR2B in samples. An antibody specific for PRKAR2B has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and anyPRKAR2B present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for PRKAR2B 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 PRKAR2B bound in the initial step. The color development is stopped and the intensity of the color is measured.
Bovine CAMP-dependent protein kinase type II-beta regulatory subunit (PRKAR2B) 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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