Date published: 2025-9-21

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FRMPD2L2 Activators

Chemical activators of FRMPD2L2 can modulate the protein's function through various intracellular signaling pathways. Bisindolylmaleimide I, for example, functions by inhibiting protein kinase C (PKC), which normally acts as a negative regulator within certain pathways. Inhibition of PKC by Bisindolylmaleimide I leads to enhanced phosphorylation statuses of proteins, including FRMPD2L2, thereby promoting its activation. Phorbol 12-myristate 13-acetate (PMA) also targets PKC but in a different manner; it directly activates PKC, which then phosphorylates FRMPD2L2, leading to its activation. Similarly, Forskolin and Dibutyryl-cAMP can elevate intracellular cAMP levels, which activate protein kinase A (PKA). PKA then phosphorylates target proteins, which may include FRMPD2L2, resulting in its activation. Ionomycin and Calcium ionophore A23187 both raise intracellular calcium levels, which in turn activate calmodulin-dependent kinases capable of phosphorylating FRMPD2L2.

Additionally, the lipid molecule Phosphatidic acid can activate the mTOR signaling pathway, which oversees protein synthesis and may result in the activation of FRMPD2L2. On the other hand, IBMX works by inhibiting phosphodiesterases, thus preventing the breakdown of cAMP and sustaining the activation of PKA, leading to the phosphorylation of FRMPD2L2. Okadaic acid and Calyculin A both inhibit protein phosphatase activity, which prevents the dephosphorylation of FRMPD2L2, keeping the protein in an active state. Epidermal Growth Factor (EGF) influences FRMPD2L2 by activating the MAPK/ERK pathway, which could lead to the phosphorylation and subsequent activation of FRMPD2L2. Lastly, the chemical LY294002, an inhibitor of PI3K, can indirectly promote the activation of alternative pathways that may include the activation of FRMPD2L2, highlighting the complex interplay of intracellular signaling molecules in regulating protein function.

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