Date published: 2025-10-12

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CC2D2B Activators

CC2D2B Activators encompass a collection of chemical entities that facilitate the enhancement of CC2D2B's functional activity through distinct signaling mechanisms. Forskolin and Isoproterenol, by increasing intracellular cAMP, indirectly elevate the activity of CC2D2B by stimulating PKA, which may phosphorylate proteins involved in CC2D2B-dependent processes. Similarly, Rolipram preserves cAMP levels by inhibiting PDE4, thereby potentially augmenting PKA's influence on CC2D2B activity. The calcium ionophores Ionomycin and A23187 significantly increase intracellular calcium levels, which could activate calcium-dependent protein kinases that modulate CC2D2B's functionality. Epigallocatechin gallate (EGCG), through its kinase inhibition, could enhance CC2D2B's role by decreasing negative regulatory phosphorylation, while the PI3K inhibitor LY294002and the MEK1/2 inhibitor U0126 may indirectly influence CC2D2B's activity through alterations in downstream signaling pathways.

Dibutyryl-cAMP (db-cAMP) directly raises cAMP levels within cells, potentially leading to an enhancement of CC2D2B through PKA-mediated pathways. Sildenafil, by preventing cGMP breakdown, may also impact signaling cascades that positively affect CC2D2B's function. Okadaic acid, a potent inhibitor of protein phosphatases, could indirectly lead to the activation of CC2D2B by maintaining the phosphorylation state of key proteins involved in its regulation. Phorbol 12-myristate 13-acetate (PMA) activates PKC, which may then phosphorylate substrates that modulate CC2D2B's activity, either directly or indirectly. These compounds, through their targeted actions on enzymes and second messengers, collectively amplify CC2D2B's role by modulating the phosphorylation status and signaling milieu within the cell, thereby facilitating the functional enhancement of CC2D2B without necessitating a direct interaction with the protein itself.

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