4.1N Activators
4.1N Activators are a suite of chemical compounds that, through their varied effects on cellular signaling pathways, indirectly enhance the functional activity of 4.1N, a protein integral to the structural integrity and organization of the cytoskeleton. Phorbol 12-myristate 13-acetate (PMA) and Forskolin, for instance, act by activating Protein Kinase C (PKC) and Protein Kinase A (PKA) respectively; PKC and PKA phosphorylate scaffolding proteins, which may bolster the interaction of 4.1N with membrane proteins and other structural components, affirming its role in the cytoskeletal framework. Compounds like Calyculin A and Okadaic Acid prevent dephosphorylation by inhibiting protein phosphatases PP1 and PP2A, potentially prolonging the activity state of proteins that associate with 4.1N, thereby reinforcing its stabilizing function. Conversely, PI3K inhibitors like LY294002 and Wortmannin might enhance 4.1N activity by modulating AKT signaling pathways, shifting cellular dynamics to depend more on the structural support 4.1N provides.
The impact of these activators extends to the nuanced regulation of kinase activity, where compounds such as Epigallocatechin Gallate (EGCG) and the broad-spectrum kinase inhibitor Staurosporine may indirectly influence 4.1N's stabilizing role in cytoskeletal integrity. Anisomycin, through its activation of stress-activated protein kinases, could augment the role of 4.1N in stress fiber formation, a critical aspect of cellular response to environmental challenges. Similarly, Bisindolylmaleimide I, while inhibiting PKC, could create a cellular environment that inadvertently supports the functions of 4.1N in organizing the cytoskeleton. Furthermore, bioactive lipids like Sphingosine-1-phosphate activate signaling pathways that govern cytoskeletal rearrangements, potentially enhancing 4.1N's activity in this domain. Lastly, Thapsigargin, by disrupting calcium homeostasis, activates calcium-dependent signaling pathways, potentially amplifying 4.1N's activity within such regulatory processes, emphasizing the protein's versatile role in cellular architecture maintenance. Together, these chemical activators, through their targeted influence on cellular signaling, facilitate the enhancement of 4.1N-mediated functions without necessitating the upregulation of its expression or direct activation.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
PMA | 16561-29-8 | sc-3576 sc-3576A sc-3576B sc-3576C sc-3576D | 1 mg 5 mg 10 mg 25 mg 100 mg | $40.00 $129.00 $210.00 $490.00 $929.00 | 119 | |
As a potent activator of Protein Kinase C (PKC), PMA influences the cytoskeleton organization in which 4.1N plays a crucial role. Activation of PKC leads to phosphorylation of scaffold proteins, potentially enhancing the stabilizing effect of 4.1N on membrane proteins and the cytoskeleton. | ||||||
Forskolin | 66575-29-9 | sc-3562 sc-3562A sc-3562B sc-3562C sc-3562D | 5 mg 50 mg 1 g 2 g 5 g | $76.00 $150.00 $725.00 $1385.00 $2050.00 | 73 | |
By elevating cAMP levels, Forskolin activates PKA which can phosphorylate cytoskeleton-associated proteins. This may indirectly enhance the stabilizing function of 4.1N within the cytoskeletal architecture by promoting interactions with other structural proteins. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A sc-24000B sc-24000C | 10 µg 100 µg 500 µg 1 mg | $160.00 $750.00 $1400.00 $3000.00 | 59 | |
As an inhibitor of protein phosphatases PP1 and PP2A, Calyculin A maintains phosphorylation states of proteins. This could lead to sustained activation states of proteins within the signaling pathways that 4.1N is part of, indirectly enhancing 4.1N’s interaction with the cytoskeleton. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Similar to Calyculin A, as a PP1 and PP2A inhibitor, Okadaic Acid could perpetuate the phosphorylation of cytoskeletal proteins, thereby potentially enhancing the role of 4.1N in maintaining cytoskeletal integrity. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $42.00 $72.00 $124.00 $238.00 $520.00 $1234.00 | 11 | |
Epigallocatechin Gallate has been shown to influence various signaling pathways, including those involving kinase activity. By modulating kinase activity, EGCG may affect the phosphorylation state of proteins associated with 4.1N, indirectly enhancing its activity. | ||||||
LY 294002 | 154447-36-6 | sc-201426 sc-201426A | 5 mg 25 mg | $121.00 $392.00 | 148 | |
As a PI3K inhibitor, LY294002 could alter the downstream AKT signaling pathway. This alteration may shift cellular dynamics in a way that necessitates the stabilizing role of 4.1N, indirectly enhancing its activity within the cytoskeleton. | ||||||
Wortmannin | 19545-26-7 | sc-3505 sc-3505A sc-3505B | 1 mg 5 mg 20 mg | $66.00 $219.00 $417.00 | 97 | |
Similar to LY294002, Wortmannin inhibits PI3K and could affect the AKT signaling pathway. This inhibitor may indirectly enhance 4.1N’s activity by changing the cytoskeletal dynamics and the interaction of 4.1N with other cellular structural components. | ||||||
Staurosporine | 62996-74-1 | sc-3510 sc-3510A sc-3510B | 100 µg 1 mg 5 mg | $82.00 $150.00 $388.00 | 113 | |
As a broad-spectrum kinase inhibitor, Staurosporine may influence multiple signaling pathways. By inhibiting specific kinases, it could indirectly enhance the function of 4.1N in the context of cytoskeletal stability and protein interactions. | ||||||
Anisomycin | 22862-76-6 | sc-3524 sc-3524A | 5 mg 50 mg | $97.00 $254.00 | 36 | |
This antibiotic interferes with protein synthesis and also activates stress-activated protein kinases. This activation could potentially enhance the role of 4.1N in stress fiber formation and maintenance within cells. | ||||||
Bisindolylmaleimide I (GF 109203X) | 133052-90-1 | sc-24003A sc-24003 | 1 mg 5 mg | $103.00 $237.00 | 36 | |
This compound is a specific inhibitor of PKC, and while it inhibits the kinase, it could paradoxically enhance 4.1N function by shifting the equilibrium of phosphorylation states within the cell, indirectly affecting 4.1N’s role in cytoskeletal organization. | ||||||