Date published: 2025-10-11

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C10orf95 Activators

C10orf95 activators encompass a range of compounds that exert their effects by manipulating various cellular signaling mechanisms, ultimately enhancing the activity of C10orf95. Certain activators work by elevating intracellular cyclic AMP (cAMP) levels, either through direct stimulation of adenylyl cyclase or inhibition of phosphodiesterases responsible for cAMP degradation; this rise in cAMP triggers protein kinase A (PKA), which may phosphorylate and activate C10orf95. Other activators influence intracellular calcium dynamics, for instance, by acting as calcium ionophores or by activating L-type calcium channels, thus increasing calcium influx. This elevation in calcium ions can activate calcium-dependent kinases, which are potential candidates for directly phosphorylating and activating C10orf95. Additionally, some activators function by inhibiting protein synthesis, which paradoxically initiates stress-activated protein kinase pathways that could target C10orf95 for activation by phosphorylation.

Moreover, the modulation of protein kinase C (PKC) signaling is another avenue through which C10orf95 activity can be influenced. Specific activators mimic diacylglycerol, a physiological activator of PKC, leading to PKC-mediated phosphorylation events. This could include the phosphorylation of C10orf95, resulting in its functional activation. The inhibition of protein phosphatases by certain compounds also indirectly contributes to the activation of C10orf95 by preventing the dephosphorylation of proteins, thereby maintaining C10orf95 in a phosphorylated and active state. Additionally, some compounds have the capability to disrupt the equilibrium of kinase activity by inhibiting key kinases such as Ca2+/calmodulin-dependent protein kinase II (CaMKII), potentially creating a compensatory upregulation of alternative kinases that might act on C10orf95, ensuring its phosphorylation and consequent activation.

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