Date published: 2025-9-18

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EF-CAB4B Inhibitors

Chemical inhibitors of EF-CAB4B can be understood in terms of their action on various signaling pathways and protein interactions that ultimately lead to the functional inhibition of this protein. Staurosporine, a well-known kinase inhibitor, can hinder upstream kinases that regulate EF-CAB4B, thereby reducing its activation. Similarly, Bisindolylmaleimide I targets protein kinase C (PKC), which is necessary for the function of many proteins, including EF-CAB4B. By inhibiting PKC, the cascade of activation that would normally include EF-CAB4B is blunted. Genistein, another kinase inhibitor, specifically targets tyrosine kinases, which can phosphorylate EF-CAB4B, thus reducing its activity. LY294002 is a PI3K inhibitor that can decrease activity in the AKT pathway, which may be crucial for the normal function of EF-CAB4B, leading to its reduced activity. Further, U0126 and PD98059 are inhibitors of MEK1/2, a kinase within the MAPK/ERK pathway, which is often involved in cellular proliferation and survival signals; the inhibition of this pathway can result in the downregulation of EF-CAB4B activity. Rapamycin directly inhibits the mTOR pathway, which can be central to protein synthesis and cell survival, potentially decreasing the functionality of EF-CAB4B. SB203580 and SP600125 inhibit the p38 MAPK and JNK pathways, respectively, which may also be involved in the regulatory processes of EF-CAB4B, leading to its inhibition. W-7 and KN-93 inhibit calmodulin-dependent protein kinases, which may affect EF-CAB4B if its activity is regulated by calcium signaling. Lastly, Ro-31-8220 acts on PKC as well, further ensuring the inhibition of any PKC-mediated pathways that could activate EF-CAB4B. Each of these chemicals can disrupt specific signaling pathways or kinase activities that are required for the full functional activation of EF-CAB4B, thereby effectively inhibiting this protein.

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