Date published: 2025-9-15

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N4BP1 Inhibitors

Chemical inhibitors of N4BP1 can exert their effects through various cellular signaling pathways. Alsterpaullone acts as a cyclin-dependent kinase (CDK) inhibitor, potentially reducing the phosphorylation events critical for N4BP1's interaction with its targets. Similarly, SP600125, a c-Jun N-terminal kinase (JNK) inhibitor, disrupts JNK signaling, which is vital for the signal transduction roles of N4BP1. SB203580, another inhibitor in this cadre, targets p38 MAP kinase, which is integral to the stress response and apoptosis pathways involving N4BP1. Inhibition of p38 MAPK by SB203580 can impair N4BP1's functionality in these processes. LY294002 and Wortmannin, both phosphoinositide 3-kinases (PI3K) inhibitors, can diminish N4BP1's functional activity by impeding upstream signals in cell survival pathways. This disruption can lead to reduced activity of N4BP1 in processes regulated by PI3K/Akt pathways.

Continuing with the theme of pathway-specific inhibition, PD98059 and U0126, as MEK inhibitors, can hinder the ERK/MAPK signaling cascade, thereby potentially impairing N4BP1's role in signal transduction. Gö 6983's broad-spectrum inhibition of protein kinase C (PKC) can disrupt PKC-mediated phosphorylation, which is essential for N4BP1's activity in certain pathways. KN-93, which hampers Ca2+/calmodulin-dependent protein kinase II (CaMKII), can lead to a reduction in N4BP1's role in CaMKII-related signaling pathways. Y-27632, a ROCK inhibitor, can interfere with actin cytoskeleton remodeling processes where N4BP1 may play a role, leading to inhibition of N4BP1's function in cytoskeletal dynamics. BIX 02189, by inhibiting MEK5, can disrupt the MEK5/ERK5 signaling pathway, potentially essential for N4BP1's function, leading to a subsequent decrease in its activity. Lastly, SL327's inhibition of MEK1/2 prevents the phosphorylation necessary for N4BP1's activity in ERK/MAPK-dependent signal transduction processes, thereby inhibiting the functional capacity of N4BP1.

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