Chemical inhibitors of MPP3 function through various modes of action to disrupt the protein's role in cellular signaling pathways. Staurosporine, a broad-spectrum protein kinase inhibitor, can interfere with the phosphorylation processes that are essential for MPP3's activity within the cell. By obstructing these phosphorylation events, Staurosporine can prevent MPP3 from properly engaging in protein-protein interactions or signal transduction, leading to its functional inhibition. Similarly, Bisindolylmaleimide I, which is a specific inhibitor of protein kinase C (PKC), can disrupt MPP3's functional activity by inhibiting PKC, a kinase that MPP3 may interact with during signaling cascades. Calphostin C and Gö 6983, both inhibitors of PKC, can further disrupt the signaling pathways involving MPP3. Calphostin C does so with specificity, while Gö 6983 provides a broader inhibition of all PKC isoforms, both leading to MPP3 inhibition.
LY333531 and Ro-31-8220, which selectively inhibit PKC beta and a broad spectrum of PKC isoforms respectively, can also suppress the signaling pathways in which MPP3 is involved. By blocking PKC beta's activity, these inhibitors can interrupt the functional activity of MPP3. Genistein, as a tyrosine kinase inhibitor, can inhibit the phosphorylation necessary for MPP3's role in signal transduction. Wortmannin and LY294002, both PI3K inhibitors, can prevent the activation of pathways that involve MPP3, thereby inhibiting MPP3 function. U0126 and PD98059, as MEK inhibitors, can impede the ERK/MAPK pathway, a pathway that MPP3 may participate in. By inhibiting MEK1/2, U0126 and PD98059 can subsequently inhibit the functional activity of MPP3 within those pathways.
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