Date published: 2025-9-13

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TM9SF1 Activators

TM9SF1 activators encompass a variety of chemical compounds that influence different biochemical pathways, ultimately leading to the upregulation of the protein's activity. Certain activators work by directly stimulating adenylyl cyclase, resulting in a surge of cAMP, which activates protein kinase A. This kinase can phosphorylate and increase the activity of TM9SF1, effectively modulating its role within the cell. Other compounds operate by a similar principle, acting either as beta-adrenergic agonists to trigger this cascade or by inhibiting phosphodiesterase, thereby preventing the breakdown of cAMP and sustaining its activating signal. Further, some activators target the phosphoinositide signaling pathway, utilizing ionophores to raise intracellular calcium levels, which could activate calcium-dependent kinases with the potential to phosphorylate TM9SF1.

Additional mechanisms of TM9SF1 activation involve modulation of sphingosine-1-phosphate receptors, which can have far-reaching effects within the cell, including the activation of this protein. Another approach involves the use of cAMP analogs that mimic the action of cAMP and elicit a response from PKA, which may influence TM9SF1 activity. Certain activators might also perturb the protein's phosphorylation state by inhibiting tyrosine kinases, leading to an indirect upregulation of its activity.

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