CEP70 Activators encompass a diverse array of compounds that exert their effects through distinct cellular pathways, all converging on the functional enhancement of CEP70. Forskolin, through its elevation of cAMP levels, activates PKA, which may phosphorylate proteins involved in regulating microtubule dynamics, thus potentially enhancing CEP70's role in microtubule organization. Similarly, PMA activates PKC, which could phosphorylate substrates that modulate CEP70's interactions with microtubules. EGF, by activating the MAPK/ERK pathway, influences cell proliferation and differentiation processes that are closely tied to centrosome dynamics and could enhance CEP70's activity. Ionomycin, by increasing intracellular calcium, triggers a cascade that activates calmodulin-dependent kinases, which could lead to the phosphorylation of proteins associated with CEP70's microtubule-stabilizing functions.
Further, the modulation of protein phosphorylation states by okadaic acid and Calyculin A, through the inhibition of protein phosphatases, could result in a hyperphosphorylated cellular milieu that indirectly promotes CEP70's activity. Taxol, by modulating microtubule stability, creates a cellular context that may necessitate the stabilizing presence of CEP70, hence indirectly enhancing its function. Lithium chloride, by inhibiting GSK-3, could stabilize microtubules and enhance Wnt signaling, pathways where CEP70's activity would be crucial.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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 | |
Forskolin is a diterpene that directly activates adenylyl cyclase, resulting in an increase in cyclic AMP (cAMP) levels. Elevated cAMP activates protein kinase A (PKA), which can phosphorylate a myriad of cellular targets. CEP70's function is dependent on proper microtubule organization, which could be influenced by PKA-mediated phosphorylation events. | ||||||
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 | |
PMA is a potent activator of protein kinase C (PKC). PKC is known to phosphorylate a variety of proteins, thus affecting numerous signaling pathways. Activation of PKC could lead to phosphorylation of proteins that interact directly with CEP70 or modulate microtubule dynamics, indirectly affecting CEP70's role in microtubule stabilization. | ||||||
Okadaic Acid | 78111-17-8 | sc-3513 sc-3513A sc-3513B | 25 µg 100 µg 1 mg | $285.00 $520.00 $1300.00 | 78 | |
Okadaic acid is a potent inhibitor of protein phosphatases PP1 and PP2A, leading to increased phosphorylation levels of many cellular proteins. The inhibition of phosphatases and subsequent protein hyperphosphorylation can affect microtubule dynamics and centrosome function, possibly impacting CEP70's activity in the centrosome. | ||||||
Taxol | 33069-62-4 | sc-201439D sc-201439 sc-201439A sc-201439E sc-201439B sc-201439C | 1 mg 5 mg 25 mg 100 mg 250 mg 1 g | $40.00 $73.00 $217.00 $242.00 $724.00 $1196.00 | 39 | |
Taxol stabilizes microtubules by binding to β-tubulin and promoting polymerization. As CEP70 is involved in microtubule organization, the stabilization of microtubules by Taxol could enhance CEP70's functional activity by providing a more robust structural framework for its action. | ||||||
Lithium | 7439-93-2 | sc-252954 | 50 g | $214.00 | ||
Lithium chloride inhibits glycogen synthase kinase-3 (GSK-3). Inhibition of GSK-3 can lead to the stabilization of microtubules and may affect Wnt signaling pathways. As CEP70 is involved in microtubule organization, the inhibition of GSK-3 could potentially enhance the role of CEP70 in microtubule stabilization and centrosome cohesion. | ||||||
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 | |
Calyculin A, similar to okadaic acid, is an inhibitor of protein phosphatases PP1 and PP2A. It leads to hyperphosphorylation of cellular proteins, potentially altering microtubule dynamics and centrosome function. This hyperphosphorylation can modify the activity of proteins that interact with or regulate CEP70, thereby indirectly enhancing its function in the centrosome. | ||||||