PP2A-Cα, a catalytic subunit of protein phosphatase 2A (PP2A), plays a pivotal role in cellular signaling by regulating the phosphorylation status of target proteins. Functionally, PP2A-Cα acts as a serine/threonine phosphatase, catalyzing the removal of phosphate groups from substrate proteins. Through its phosphatase activity, PP2A-Cα counterbalances the actions of protein kinases, contributing to the dynamic regulation of cellular processes such as cell cycle progression, proliferation, apoptosis, and metabolism. PP2A-Cα functions as part of a heterotrimeric complex consisting of a catalytic subunit (C), a structural scaffold subunit (A), and a regulatory subunit (B), with various isoforms and splice variants providing diversity and specificity to PP2A-mediated dephosphorylation events.
The activation of PP2A-Cα involves complex regulatory mechanisms that modulate its catalytic activity and substrate specificity. One major mechanism of PP2A-Cα activation is through the formation of active holoenzyme complexes, wherein the catalytic subunit associates with specific regulatory and scaffold subunits. Binding of regulatory subunits to PP2A-Cα can modulate its activity by altering its substrate specificity or subcellular localization. Additionally, post-translational modifications such as phosphorylation and methylation can regulate PP2A-Cα activity, with phosphorylation at specific sites enhancing or inhibiting its phosphatase activity. Moreover, cellular cues such as changes in intracellular calcium levels or oxidative stress can activate PP2A-Cα by promoting its association with regulatory subunits or altering its conformation. Overall, the activation of PP2A-Cα is a tightly regulated process essential for maintaining cellular homeostasis and proper functioning of signaling pathways implicated in various physiological and pathological processes.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
FTY720 | 162359-56-0 | sc-202161 sc-202161A sc-202161B | 1 mg 5 mg 25 mg | $33.00 $77.00 $120.00 | 14 | |
FTY720, also known as Fingolimod, activates PP2A-Cα by inhibiting sphingosine kinase and promoting PP2A-mediated dephosphorylation of its substrates. This leads to increased phosphatase activity and contributes to the regulation of various cellular processes, including cell cycle progression and apoptosis. The direct activation of PP2A-Cα by FTY720 highlights its role in sphingolipid signaling and cellular homeostasis. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $163.00 $800.00 | 59 | |
Calyculin A, a marine toxin, indirectly activates PP2A-Cα by inhibiting its endogenous inhibitor, protein phosphatase 1 (PP1). Similar to Okadaic Acid, Calyculin A disrupts the PP2A-PP1 equilibrium, leading to enhanced PP2A activity and subsequent dephosphorylation of cellular substrates. This indirect activation emphasizes the delicate balance between phosphatases and their impact on PP2A-Cα function. | ||||||
Oleic Acid | 112-80-1 | sc-200797C sc-200797 sc-200797A sc-200797B | 1 g 10 g 100 g 250 g | $37.00 $104.00 $580.00 $1196.00 | 10 | |
OA-NO2, a nitric oxide-releasing derivative of Okadaic Acid, indirectly activates PP2A-Cα by inhibiting its endogenous inhibitor, protein phosphatase 1 (PP1). Through disruption of the PP2A-PP1 equilibrium, OA-NO2 promotes increased PP2A activity, leading to enhanced dephosphorylation of critical cellular substrates. | ||||||
Tunicamycin | 11089-65-9 | sc-3506A sc-3506 | 5 mg 10 mg | $172.00 $305.00 | 66 | |
Tautomycetin directly activates PP2A-Cα by binding to its catalytic subunit, promoting phosphatase activity. This direct activation results in the dephosphorylation of specific cellular substrates, influencing various cellular processes. The unique mechanism of direct activation by Tautomycetin underscores its potential as a tool for studying the intricacies of PP2A-Cα function and regulation. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $80.00 $220.00 $460.00 | 64 | |
Resveratrol indirectly activates PP2A-Cα by inhibiting its endogenous inhibitor, protein phosphatase 1 (PP1). Through disruption of the PP2A-PP1 equilibrium, Resveratrol promotes increased PP2A activity, leading to enhanced dephosphorylation of critical cellular substrates. This indirect activation underscores the potential of dietary compounds in modulating phosphatase balance and influencing PP2A-Cα-mediated cellular processes. | ||||||
Methotrexate | 59-05-2 | sc-3507 sc-3507A | 100 mg 500 mg | $94.00 $213.00 | 33 | |
Methotrexate indirectly activates PP2A-Cα by inhibiting dihydrofolate reductase (DHFR), leading to enhanced PP2A activity. The disruption of folate metabolism by Methotrexate contributes to increased phosphatase activity, resulting in the dephosphorylation of critical cellular substrates. | ||||||