Date published: 2025-10-29

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C6orf81 Activators

Chemical activators of C6orf81 harness a variety of cellular signaling pathways to elevate its activity. Calcium ionophore A23187 and Ionomycin are two such activators that directly increase intracellular calcium levels. This surge in calcium can activate calcium-dependent protein kinases, which in turn phosphorylate C6orf81, resulting in its activation. Phorbol 12-myristate 13-acetate (PMA) operates through a different mechanism, activating protein kinase C (PKC). Once activated, PKC phosphorylates numerous substrates, including C6orf81, thereby enhancing its activity. Forskolin, on the other hand, works by elevating intracellular cAMP, subsequently activating protein kinase A (PKA), which is known to phosphorylate and activate C6orf81.

Further into the cellular machinery, Okadaic Acid and Calyculin A disrupt the balance of phosphorylation within the cell by inhibiting protein phosphatases 1 and 2A. This inhibition prevents dephosphorylation, maintaining proteins in a phosphorylated state and potentially leading to the activation of C6orf81. Bisindolylmaleimide I, while primarily a PKC inhibitor, can paradoxically upregulate certain PKC isoforms, which may phosphorylate and activate C6orf81. Similarly, Chelerythrine can activate specific PKC isoforms, thereby having a role in phosphorylating and activating C6orf81. Dibutyryl cyclic AMP (dbcAMP) serves as a cell-permeable cAMP analog that stimulates PKA, adding another route to the phosphorylation and consequent activation of C6orf81. Epigallocatechin Gallate (EGCG) engages with signaling pathways that can lead to the activation of kinases that target C6orf81. Anisomycin triggers MAPK pathways involving kinases that can phosphorylate C6orf81, thus activating it. Lastly, (-)-Blebbistatin, by altering myosin II activity, can influence intracellular signaling cascades that culminate in the phosphorylation and activation of C6orf81.

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