Chemicals associated with the indirect activation of ANKRD25 typically interact with a diverse range of signaling pathways, consequently influencing the protein's modulation. Agents like Retinoic Acid, which operates via retinoic acid receptors, exert influence on gene transcription processes. Such modulation of transcriptional landscapes can impact proteins like ANKRD25 that are speculated to play roles in these cascades. Similarly, chemicals like AICAR and Metformin, renowned AMPK activators, elucidate the interconnection between cellular energy dynamics and proteins like ANKRD25. Activation of AMPK can trigger a cascade of events, leading to the indirect modulation of ANKRD25.
Another profound domain influencing ANKRD25 activation revolves around intracellular cAMP levels. Dibutyryl-cAMP, a cell-permeable analog, and Rolipram, a PDE4, both elevate intracellular cAMP levels, a key secondary messenger. As cAMP modulates a multitude of signaling cascades, its increase can steer the pathways in which ANKRD25 operates, fostering its indirect modulation. In a similar vein, PMA, a potent PKC activator, underscores the relevance of protein kinases in cellular signaling. Enhancement of PKC activity can ripple through to downstream effectors and pathways, indirectly modulating ANKRD25. Moreover, agents such as SAG and DAPT, which modulate the Hedgehog and Notch signaling pathways respectively, highlight the intricate network of signaling events that proteins like ANKRD25 are possibly entrenched in. Chemicals such as these, even in the absence of direct binding or interaction with ANKRD25, shed light on the versatile means by which ANKRD25's function can be swayed, predominantly via the indirect activation of associated signaling pathways.
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