Chemicals postulated to be FAM83E activators have been broadly selected based on their capacity to influence signaling pathways where FAM83E plays a role due to its kinase binding activity. EGF and Insulin, for instance, both stimulate pathways where downstream effectors, like PI3K/AKT, have widespread influence on cellular signaling. Given FAM83E's in signal transduction, chemicals that stimulate these primary pathways can inadvertently emphasize the significance of FAM83E in cellular processes. Similarly, compounds like PMA, activating Protein Kinase C (PKC), underline the complexities of cellular signaling, where the activation of one kinase can influence several downstream pathways.
On the other side of the spectrum, chemicals such as Anisomycin, Etoposide, and Sodium Vanadate, work through various mechanisms, be it DNA damage, JNK activation, or tyrosine phosphorylation enhancement. These varied pathways might seem unrelated at first, but within the intricate cellular signaling networks, they may eventually overlap or intersect with FAM83E's function, especially when considering its protein kinase binding activity. The importance of understanding these activators lies not just in modulating FAM83E directly, but in appreciating the broader signaling landscape in which FAM83E operates. Chemicals such as AICAR, Dorsomorphin, and Okadaic Acid further emphasize this intricate balance, showing how modulation of cellular energy status or inhibition of specific signaling components can still have repercussions on proteins like FAM83E, emphasizing its role in the broader cellular signaling network.
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