Date published: 2025-9-5

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Fibulin-7 Activators

Fibulin-7 Activators encompass a diverse array of chemical entities that modulate the functional activity of Fibulin-7 through various intracellular signaling mechanisms. Forskolin is one such activator that directly stimulates adenylyl cyclase, causing an increase in intracellular cAMP levels; this cascade triggers protein kinase A (PKA) activation, which is known to phosphorylate proteins that interact with and enhance the function of Fibulin-7, particularly in the context of the extracellular matrix and cell adhesion dynamics. Another compound, Y-27632, operates as a selective inhibitor of ROCK kinases, which upon inhibition, can lead to changes in actin cytoskeleton dynamics, potentially augmenting Fibulin-7's role in cell-matrix adhesion processes. Similarly, Sphingosine 1-phosphate, by binding to G-protein coupled receptors, initiates downstream signaling that can affect cytoskeletal organization and thereby potentiate Fibulin-7 mediated functions in the extracellular matrix and cell adhesion. Additionally, Staurosporine, although a broad kinase inhibitor, at low concentrations may selectively alter kinase activity, which could activate signaling pathways that increase the activity of Fibulin-7 in the extracellular matrix.

In parallel, other chemicals act to modify the activity of Fibulin-7 through different mechanisms. Blebbistatin, by inhibiting myosin II ATPase activity, indirectly affects cellular processes such as migration and adhesion, which are crucial for the roles of Fibulin-7 in stabilizing extracellular matrix interactions. Wiskostatin targets the N-WASP-Arp2/3 complex, critical for actin polymerization; by modulating actin dynamics, it can enhance Fibulin-7's involvement in cell adhesion and matrix organization. LY294002, a PI3K inhibitor, alters the PI3K/AKT signaling pathway, which plays a significant role in regulating extracellular matrix composition, thus influencing Fibulin-7's function in cell-matrix interactions. Additionally, Epigallocatechin Gallate (EGCG) inhibits various protein kinases, which may lead to the activation of pathways that promote Fibulin-7's role in matrix formation and remodeling by affecting the phosphorylation state of associated proteins. Lastly, Jasplakinolide, by stabilizing actin filaments and promoting polymerization, can enhance the integrity of the extracellular matrix where Fibulin-7 is active, emphasizing the compound's role in supporting the structural basis for cell-matrix adhesion and stability.

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