Date published: 2025-9-15

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IGFL3 Activators

IGFL3 can engage diverse cellular signaling pathways to modulate the activity of this protein. Forskolin is a compound that directly stimulates adenylyl cyclase, which increases the levels of cAMP within the cell, leading to the activation of protein kinase A (PKA). PKA, in turn, can phosphorylate various proteins, potentially including IGFL3 if it falls under PKA's substrate profile. Similarly, Dibutyryl-cAMP (db-cAMP), a cell-permeable analog of cAMP, can also activate PKA, which could result in the phosphorylation and consequent activation of IGFL3. (-)-Isoproterenol hydrochloride functions as a beta-adrenergic receptor agonist and raises cAMP levels, similarly leading to PKA activation and possibly impacting IGFL3 activity.

PDBu (Phorbol 12,13-dibutyrate) activates protein kinase C (PKC), which phosphorylates a wide array of proteins and could include IGFL3 if it is a substrate for PKC. Ionomycin, by raising intracellular calcium levels, could initiate calcium-dependent kinase pathways such as calmodulin-dependent kinase (CaMK), which may phosphorylate IGFL3. Insulin, through its receptor, triggers a cascade involving phosphoinositide 3-kinase (PI3K) and AKT, which could lead to the activation of IGFL3 if it is a downstream effector. Epidermal Growth Factor (EGF) stimulates its receptor to activate both MAPK and PI3K-AKT pathways, which may impinge upon IGFL3. Anisomycin, known as a protein synthesis inhibitor, also activates stress-activated protein kinases such as JNK, which might target IGFL3 in stress response signaling. Calyculin A and Okadaic Acid, both inhibitors of protein phosphatases PP1 and PP2A, could maintain IGFL3 in a phosphorylated, and thus active, state by preventing dephosphorylation. Lastly, Lithium chloride inhibits glycogen synthase kinase 3 (GSK-3), potentially leading to the activation of Wnt signaling pathway, which might involve IGFL3 activation if it is associated with this pathway or with proteins regulated by GSK-3.

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