Date published: 2025-10-11

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TRIM73 Activators

TRIM73 Activators are a distinct group of chemical compounds that exert their influence on cellular pathways to enhance the functional activity of TRIM73. Compounds such as Forskolin and Isoproterenol elevate intracellular levels of cAMP, leading to the activation of protein kinase A (PKA), which is known to phosphorylate TRIM73, thereby increasing its functional activity in the cell. Phorbol 12-myristate 13-acetate (PMA) is known to activate protein kinase C (PKC), which can also phosphorylate TRIM73, suggesting a role in enhancing its activation. Similarly, the compound Ionomycin, by increasing intracellular calcium levels, may activate calcium-dependent protein kinases that are capable of phosphorylating TRIM73, resulting in its activation. The use of the cAMP analog 8-Bromo-cAMP further supports the role of cAMP-PKA signaling in TRIM73 activation, while Oleic Acid could indirectly influence the activation of TRIM73 via modulation of PKC signaling pathways.

Other activators include Zinc Pyrithione and A23187, which may modulate ion channels or increase calcium levels respectively, leading to activation of signaling pathways that phosphorylate and enhance TRIM73 activity. Okadaic Acid prevents the dephosphorylation of proteins by inhibiting protein phosphatases, potentially leading to a sustained phosphorylated state of TRIM73, thereby maintaining its active form. Additionally, the lipid signaling molecule Sphingosine-1-phosphate may activate kinases that phosphorylate and activate TRIM73. Chelerythrine, although a PKC inhibitor, may in certain scenarios lead to the selective activation of specific PKC isoforms that could phosphorylate and enhance TRIM73 activity. Lastly, Nicotinamide adenine dinucleotide (NAD+), serving as a coenzyme in redox reactions and as a substrate for ADP-ribosylation processes, has the potential to influence cellular signaling mechanisms that lead to the activation of TRIM73. These diverse chemical activators, through their targeted effects on various signaling pathways, serve to collectively enhance the functional activity of TRIM73 without necessitating an increase in its expression levels or direct activation of the protein itself.

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