Date published: 2025-9-28

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1700010B08Rik Inhibitors

Chemical inhibitors of 1700010B08Rik can be characterized by their specific actions on various signaling pathways and enzymes that are crucial to the functional activity of the protein. Staurosporine is a potent protein kinase inhibitor, and by inhibiting these enzymes, it disrupts phosphorylation events that are essential for many proteins, including 1700010B08Rik, thus leading to its functional inhibition. Similarly, Wortmannin and LY294002 act as PI3K inhibitors, which is a key signaling molecule that regulates a multitude of cellular processes. By blocking PI3K, these inhibitors can lead to a reduction in downstream signaling necessary for 1700010B08Rik function, effectively diminishing its activity within the cell.

Continuing with the theme of pathway-specific inhibition, PD98059 and U0126 are selective for MEK1/2, a kinase that is upstream of various signaling cascades. Inhibition with these chemicals would prevent activation of downstream kinases that may regulate 1700010B08Rik, thereby inhibiting its function. SB203580 targets p38 MAP kinase and SP600125 inhibits JNK, both of which are stress-activated protein kinases. By preventing the activation of these kinases, the inhibitors can reduce the functional activity of 1700010B08Rik if it is regulated by stress response pathways. Erlotinib, Gefitinib, and Lapatinib are tyrosine kinase inhibitors that target EGFR, with Lapatinib also inhibiting HER2. These receptors are often involved in complex signaling networks, and their inhibition can lead to a decrease in 1700010B08Rik activity if it is modulated by these pathways. Lastly, Sorafenib and Sunitinib are multi-targeted receptor tyrosine kinase inhibitors, which by inhibiting their targets, can lead to a decrease in the activity of proteins that are regulated by these kinases, including 1700010B08Rik, thus achieving functional inhibition of the protein.

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