Chemical inhibitors of BC017647 act through various mechanisms to regulate its activity by targeting different components of signaling pathways. Wortmannin and LY294002 are two such inhibitors that directly target phosphoinositide 3-kinases (PI3K), a group of enzymes that are crucial for the activation of BC017647. By inhibiting PI3K, these chemicals prevent the phosphorylation and subsequent activation of downstream targets including BC017647. Rapamycin, on the other hand, specifically impedes the mechanistic target of rapamycin (mTOR), another kinase critical in the same pathway as PI3K. The inhibition of mTOR by rapamycin leads to a decrease in BC017647 activity due to its dependence on mTOR signaling for activation. Similarly, U0126 and SB203580 target upstream kinases MEK1/2 and p38 MAP kinase, respectively. Inhibition of these kinases by U0126 and SB203580 results in reduced phosphorylation of downstream targets, which includes BC017647, thereby dampening its activity.
Further regulating BC017647, Staurosporine serves as a broad-spectrum kinase inhibitor that can affect a myriad of kinases responsible for the phosphorylation of BC017647. In contrast, PP2 is more selective, targeting Src family tyrosine kinases which, when inhibited, reduce the activation state of BC017647. PD168393 works by irreversibly inhibiting the epidermal growth factor receptor (EGFR) tyrosine kinase, a receptor that can activate several downstream pathways involving BC017647. SP600125 and NF449 exhibit their regulatory effects by inhibiting c-Jun N-terminal kinase (JNK) and the Gs-alpha subunit of G-proteins, respectively. The inhibition of JNK by SP600125 and the G-protein signaling by NF449 both lead to a decrease in BC017647 activity. Lastly, Bisindolylmaleimide I and Genistein target Protein Kinase C (PKC) and tyrosine kinase activities, respectively. The inhibition of PKC by Bisindolylmaleimide I and the blockade of tyrosine kinase activity by Genistein result in lower activation levels of BC017647.
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