Date published: 2025-11-5

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LOC391747 Activators

LOC391747 Activators encompass a diverse array of chemical compounds that indirectly increase the functional activity of LOC391747 through modulation of various signaling cascades. Forskolin acts by raising intracellular cAMP, which in turn activates PKA, potentially leading to downstream phosphorylation events that enhance LOC391747 activity. Similarly, PMA, through PKC activation, could phosphorylate substrates that influence LOC391747's function, assuming it is intertwined with PKC-regulated pathways. The polyphenol EGCG, known for its kinase inhibitory properties, may indirectly augment LOC391747 by reducing competitive kinase signaling, thus favoring pathways where LOC391747 is active. Sphingosine-1-phosphate, engaging with G protein-coupled receptors, initiates signaling that could alter the cellular environment to benefit LOC391747's role, while ionomycin and A23187, by increasing intracellular calcium, might activate calcium-dependent kinases or phosphatases that impact LOC391747's activity.

Further influencing the activity of LOC391747 are compounds that modulate key signaling molecules and pathways. LY294002, a PI3K inhibitor, and U0126, a MEK1/2 inhibitor, both act to shift the signaling equilibrium in the cell, which could lead to an indirect enhancement of LOC391747 function. SB203580 specifically targets p38 MAPK and, by inhibiting this pathway, may indirectly promote signaling pathways that activate LOC391747. Thapsigargin, by disrupting calcium storage, and H-89, through PKA inhibition, may instigate compensatory cellular responses that affect the activity of LOC391747. Lastly, staurosporine, despite its broad kinase inhibition profile, might selectively enhance LOC391747 activity by inhibiting kinases that suppress LOC391747-associated pathways. Collectively, these activators utilize their effects on cellular signaling molecules and pathways to facilitate the functional enhancement of LOC391747 without directly increasing its expression.

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