Date published: 2025-9-15

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CIB3 Activators

CIB3 can initiate a series of intracellular signaling events through various mechanisms. Calcium chloride, for instance, introduces calcium ions that directly bind to the EF-hand domain of CIB3, a motif known for calcium ion coordination. This binding event triggers a change in the protein's conformation, enabling it to participate actively in cellular signaling pathways. Similarly, ionomycin, as a calcium ionophore, elevates intracellular calcium levels that can bind to CIB3, potentially causing structural changes that activate its signaling functions. Thapsigargin also plays a role in increasing cytosolic calcium concentration, which might interact with CIB3, leading to its activation through calcium-induced conformational changes. Furthermore, BAY K8644, by activating L-type calcium channels, raises intracellular calcium, which may lead to the activation of CIB3.

Other chemical activators influence CIB3 through different mechanisms. Zinc sulfate and magnesium sulfate supply zinc and magnesium ions, respectively, which can interact with the protein, possibly resulting in structural modifications that enhance CIB3's functional activity. Phorbol 12-myristate 13-acetate and 4-α-Phorbol 12,13-didecanoate, both phorbol esters, mimic diacylglycerol and activate protein kinase C (PKC). PKC, in turn, may phosphorylate CIB3, leading to its activation. Forskolin increases cAMP levels within the cell, activating protein kinase A (PKA), which can then target CIB3 for phosphorylation, and N6-Benzoyladenosine-3',5'-cyclic monophosphate, a cAMP analog, also activates PKA, potentially culminating in the phosphorylation of CIB3. Sodium fluoride acts as a phosphorylating agent, which might lead to the direct phosphorylation of CIB3, altering its signaling capabilities. Lastly, 1,2-Dioctanoyl-sn-glycerol, a synthetic DAG analog, activates PKC, which might phosphorylate CIB3, thereby modulating its role in cellular signaling pathways.

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