Chemical inhibitors of the protein 1700016D06Rik act through various biochemical pathways to modulate its activity within cells. Staurosporine is a potent kinase inhibitor, known for its ability to broadly target protein kinases, and can thus inhibit the phosphorylation of 1700016D06Rik, affecting its activity if phosphorylation is a crucial modification for its function. Similarly, both LY294002 and Wortmannin target PI3K, a key component of intracellular signaling pathways. These inhibitors can suppress the activity of PI3K, which may indirectly influence the role of 1700016D06Rik by preventing its activation or recruitment to essential cellular signaling complexes. In a related mechanism, Rapamycin focuses on mTOR, a central regulator of cell growth, which can impinge upon the functionality of 1700016D06Rik by disrupting processes it may be involved in.
Inhibitors like PD98059 and U0126 are specifically designed to inhibit MEK, which subsequently prevents the activation of ERK, a kinase that plays a pivotal role in cell signaling. By impeding the MEK/ERK pathway, these inhibitors can indirectly lead to a decrease in 1700016D06Rik activity. Similarly, SB203580 targets p38 MAP Kinase, a molecule that responds to stress stimuli, and by inhibiting it, SB203580 may impact the role of 1700016D06Rik in related signaling pathways. SP600125 acts upon JNK, another kinase involved in stress and cytokine signaling, and its inhibition can affect 1700016D06Rik if it operates downstream or in concert with the JNK pathway. PP2 and Dasatinib serve as kinase inhibitors with a broader range, targeting Src family kinases and Bcr-Abl, respectively. The Src family of kinases is involved in multiple signaling cascades, and their inhibition could result in diminished 1700016D06Rik activity. Lastly, Y-27632 and Palbociclib inhibit ROCK and CDK4/6 kinases, respectively, with potential effects on 1700016D06Rik activity if it is engaged in ROCK-mediated cytoskeletal dynamics or CDK4/6-regulated cell cycle progression.
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