Date published: 2025-9-13

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LOC729005 Inhibitors

LOC729005 inhibitors Wortmannin and LY294002 target PI3K, a pivotal kinase in cell signaling, potentially affecting proteins regulated by this pathway. Their binding impedes PI3K's kinase activity, thereby influencing downstream signaling events. Rapamycin, engaging with mTOR, acts to dampen the mTOR pathway, which is integral to protein synthesis and cell proliferation. This interaction can lead to a cascade of effects on proteins that are regulated by mTOR signaling. Compounds like SB203580 and PD98059 exhibit selectivity towards MAP kinases, pivotal in cellular responses to extracellular stimuli. SB203580 inhibits p38 MAP kinase, while PD98059 targets MEK, an upstream regulator of MAP kinases, thereby modulating the phosphorylation state and activity of proteins downstream of these kinases. SP600125 and U0126, by inhibiting JNK and MEK1/2 respectively, alter the signaling trajectory of their respective pathways, potentially affecting proteins that are responsive to stress and mitogenic signals controlled by these kinases.

Trichostatin A and 5-Azacytidine mediate changes in gene expression by modifying chromatin structure and DNA methylation status, respectively. Trichostatin A inhibits HDACs, affecting histone acetylation and thus gene transcription, which in turn can influence protein expression and function. 5-Azacytidine, by incorporating into nucleic acids, induces DNA hypomethylation, leading to changes in gene expression profiles that can affect protein regulation. Brefeldin A, Cyclosporin A, and Thapsigargin interact with distinct cellular targets involved in protein processing and intracellular signaling. Brefeldin A disrupts protein transport by inhibiting Golgi function, which can affect the localization and function of proteins reliant on the secretory pathway. Cyclosporin A binds to calcineurin, impacting T-cell activation and subsequent protein activities within the immune signaling cascade. Thapsigargin, by inhibiting SERCA pumps, elevates cytosolic calcium levels, thereby affecting proteins that are sensitive to calcium signaling.

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