Date published: 2025-9-15

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RIM-BP3C Activators

Chemical activators of RIM-BP3C can exert their influence through various intracellular signaling pathways leading to the activation of the protein. Forskolin, by activating adenylyl cyclase, can increase the concentration of cAMP within the cell. This rise in cAMP levels can then activate protein kinase A (PKA), which is known to phosphorylate target proteins, including RIM-BP3C, leading to its activation. Ionomycin, on the other hand, increases intracellular calcium levels, and this boost in calcium can activate calcium/calmodulin-dependent protein kinases, which can then target RIM-BP3C for phosphorylation and subsequent activation. Similarly, Thapsigargin can indirectly bring about the activation of RIM-BP3C by inhibiting the SERCA pump, thereby elevating intracellular calcium levels which in turn may activate kinases capable of phosphorylating RIM-BP3C.

Another chemical, Phorbol 12-myristate 13-acetate (PMA), can activate protein kinase C (PKC), and the activated PKC can phosphorylate RIM-BP3C, leading to its activation. Okadaic Acid and Calyculin A, as inhibitors of protein phosphatases 1 and 2A, prevent the dephosphorylation of proteins, which can cause a sustained phosphorylation state and activation of RIM-BP3C. Anisomycin activates stress-activated protein kinases that may also target RIM-BP3C for phosphorylation, thereby activating the protein. The Epidermal Growth Factor (EGF) stimulates the MAPK/ERK pathway, which is another route through which the phosphorylation and activation of RIM-BP3C can be achieved. Furthermore, Staurosporine and Bisindolylmaleimide I, although typically kinase inhibitors, can have off-target effects that result in the phosphorylation and activation of RIM-BP3C. Lastly, Dibutyryl-cAMP, a cAMP analog, can activate PKA and A23187, a calcium ionophore, can increase intracellular calcium, both of which may result in the activation of kinases that phosphorylate and activate RIM-BP3C. These diverse chemicals, through their unique mechanisms, all contribute to the phosphorylation state and activation of RIM-BP3C within cellular signaling pathways.

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