Kinase inhibitors such as staurosporine exert their influence by impeding the function of a multitude of protein kinases, thus having the capacity to modulate the activity of proteins by interfering with phosphorylation events and altering signaling cascades. Similarly, LY294002 and wortmannin, as PI3K inhibitors, effectively diminish PI3K/Akt signaling, a pathway fundamental to a variety of cellular functions, which when inhibited, can alter the behavior and interaction of numerous proteins, possibly including C2orf90.
Additionally, compounds such as U0126 and PD98059 directly inhibit the MAPK/ERK pathway, a key regulator of cell proliferation and differentiation, while rapamycin targets mTOR signaling, which is central to cell growth and metabolism. The suppression of these pathways can precipitate changes in the cellular environment that may influence the function of C2orf90. In a similar vein, SB203580 and SP600125, which inhibit the p38 MAP kinase and JNK respectively, are capable of modulating cellular responses to stress and inflammation, potentially affecting C2orf90's activity within these contexts.
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