SNED1 activators comprise a group of chemical entities, each with unique mechanisms to amplify the functionality of SNED1, a protein integral to cellular processes including cell growth, apoptosis, and metabolism. Several of these activators operate by inhibiting protein phosphatases like PP2A, PP1, and PP4. Epigallocatechin Gallate, Okadaic Acid, Fostriecin, Calyculin A, and Cantharidin are such compounds that, by impeding these phosphatases, elevate overall phosphorylation to directly enhance the activation of SNED1.
Conversely, indirect activators such as Ionomycin, A23187, Forskolin, Isoprenaline, Phorbol 12-myristate 13-acetate (PMA), Diacylglycerol (DAG), and cAMP function by modulating various cellular mechanisms. These processes ultimately foster the phosphorylation and activation of SNED1. Ionomycin and A23187 elevate intracellular calcium levels, sparking the activation of calcium/calmodulin-dependent protein kinases (CaMKs) capable of phosphorylating SNED1. Similarly, Forskolin, Isoprenaline, and cAMP increase intracellular cAMP levels, leading to the activation of Protein Kinase A (PKA), another kinase capable of phosphorylating and activating SNED1. Lastly, PMA and DAG serve as potent activators of Protein Kinase C (PKC), which also has the potential to phosphorylate and thus activate SNED1.
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