Date published: 2025-9-14

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MS4A10 Activators

MS4A10 can influence its activity through various intracellular signaling pathways. Phorbol 12-myristate 13-acetate (PMA) is known to directly activate protein kinase C (PKC), a family of enzymes that play critical roles in several signal transduction cascades. PKC can phosphorylate a broad spectrum of target proteins, possibly including MS4A10 or its associated regulatory proteins, leading to changes in their activity. Forskolin, by elevating cAMP levels, can activate protein kinase A (PKA), another kinase that phosphorylates multiple substrates within the cell, potentially impacting the activity of MS4A10. Ionomycin, by functioning as a calcium ionophore, can increase intracellular calcium concentrations, which then activates calcium-dependent proteins and enzymes, also possibly influencing MS4A10's activity.

Further influencing the activity of MS4A10, retinoic acid can modulate gene expression by interacting with nuclear receptors, leading to changes in protein synthesis that can include proteins in the same pathway as MS4A10. Insulin triggers signaling through its receptor, initiating a cascade that can lead to the phosphorylation of various proteins that may interact with MS4A10. Similarly, epinephrine and isoproterenol, by binding to their respective receptors, can increase cAMP and activate PKA, which in turn can phosphorylate proteins associated with MS4A10. Histamine, through its action on phospholipase C (PLC), can lead to the activation of PKC and the subsequent phosphorylation of proteins that may be involved in modulating MS4A10. Anisomycin, as an activator of stress-activated protein kinases, can phosphorylate targets that may include proteins influencing MS4A10's activity. Bryostatin 1, another PKC activator, and thapsigargin, a disruptor of calcium homeostasis, can also lead to the activation of kinases that phosphorylate proteins related to MS4A10. Lastly, ouabain, by inhibiting the Na+/K+ ATPase, can alter intracellular ion concentrations, indirectly affecting calcium-dependent signaling pathways and possibly the activity of MS4A10.

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