Description
Description: This assay employs a two-site sandwich ELISA to quantitate MAP3K7 in samples. An antibody specific for MAP3K7 has been pre-coated onto a microplate. Standards and samples are pipetted into the wells and any MAP3K7 present is bound by the immobilized antibody. After removing any unbound substances, a biotin-conjugated antibody specific for MAP3K7 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 MAP3K7 bound in the initial step. The color development is stopped and the intensity of the color is measured.
Overview: MAP3K7IP1was identified as a regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is known to mediate various intracellular signaling pathways, such as those induced by TGF beta, interleukin 1, and WNT-1. This protein interacts and thus activates TAK1 kinase. It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1. This protein can also interact with and activate the mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus represents an alternative activation pathway, in addition to the MAPKK pathways, which contributes to the biological responses of MAPK14 to various stimuli