PP2A-Cα Inhibitors
PP2A-Cα, a catalytic subunit of protein phosphatase 2A (PP2A), is a crucial regulator of cellular signaling pathways, exerting profound effects on various cellular processes, including cell cycle progression, proliferation, apoptosis, and metabolism. Functionally, PP2A-Cα serves as a serine/threonine phosphatase, catalyzing the dephosphorylation of target proteins and thereby counterbalancing the actions of protein kinases. By dephosphorylating key regulatory proteins, PP2A-Cα modulates their activity and function, influencing downstream signaling cascades and cellular responses. Additionally, PP2A-Cα interacts with a diverse array of regulatory subunits and scaffold proteins, forming holoenzymes with distinct substrate specificities and subcellular localization patterns, thereby imparting specificity and versatility to PP2A-mediated dephosphorylation events.
Inhibition of PP2A-Cα activity represents a significant regulatory mechanism that impacts cellular signaling and function. Several mechanisms of PP2A-Cα inhibition have been elucidated, including post-translational modifications, endogenous inhibitors, and pharmacological agents. Post-translational modifications such as phosphorylation, methylation, and oxidation can regulate PP2A-Cα activity by altering its catalytic efficiency, substrate specificity, and subcellular localization. Additionally, endogenous inhibitors, such as the cellular inhibitor of PP2A (CIP2A) protein, directly bind to PP2A-Cα and prevent its association with regulatory subunits and substrates, thereby inhibiting its phosphatase activity. Moreover, pharmacological agents, including small molecule inhibitors and natural compounds, have been identified as potent inhibitors of PP2A-Cα activity. These inhibitors function by disrupting the catalytic activity of PP2A-Cα or interfering with its interactions with regulatory subunits, leading to dysregulation of cellular signaling pathways and perturbation of cellular homeostasis. Overall, the inhibition of PP2A-Cα represents a crucial mechanism for regulating cellular signaling pathways and physiological processes, highlighting its importance as a target for intervention in various diseases and pathological conditions.
SEE ALSO...
| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
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, a marine toxin, is a potent and selective inhibitor of PP2A. By binding to the catalytic subunit of PP2A, Okadaic Acid disrupts its phosphatase activity, leading to the accumulation of phosphorylated substrates. This inhibition provides a valuable tool for studying PP2A-dependent cellular processes and signaling pathways. | ||||||
Cantharidin | 56-25-7 | sc-201321 sc-201321A | 25 mg 100 mg | $81.00 $260.00 | 6 | |
Cantharidin is a natural toxin that acts as an inhibitor of PP2A. Through the formation of a complex with the catalytic subunit of PP2A, Cantharidin disrupts its phosphatase activity, leading to the hyperphosphorylation of substrates. The inhibition by Cantharidin offers insights into the regulatory roles of PP2A in cellular processes and provides a basis for further investigations into its molecular mechanisms. | ||||||
LB-100 | 1632032-53-1 | sc-507368 | 10 mg | $330.00 | ||
LB-100 is a synthetic small molecule that selectively inhibits PP2A. By binding to the catalytic subunit of PP2A, LB-100 disrupts its phosphatase activity, leading to the accumulation of phosphorylated proteins. This targeted inhibition of PP2A by LB-100 offers a precise means to investigate PP2A-dependent cellular processes and pathways, contributing to the understanding of its role in cellular regulation. | ||||||
Perphenazine | 58-39-9 | sc-208161 | 100 mg | $190.00 | ||
Perphenazine, an antipsychotic drug, indirectly influences PP2A activity. By increasing the expression of the PP2A subunit B55α, Perphenazine promotes the assembly of active PP2A holoenzymes. This indirect modulation offers insights into the regulatory mechanisms governing PP2A function and its impact on cellular processes and signaling events. | ||||||
Oleic Acid | 112-80-1 | sc-200797C sc-200797 sc-200797A sc-200797B | 1 g 10 g 100 g 250 g | $36.00 $102.00 $569.00 $1173.00 | 10 | |
OA-NO2, a nitroderivative of Okadaic Acid, is a selective inhibitor of PP2A. Similar to Okadaic Acid, OA-NO2 binds to the catalytic subunit of PP2A, disrupting its phosphatase activity. This selective inhibition by OA-NO2 provides a tool for investigating the specific roles of PP2A in cellular processes and signaling pathways, contributing to a deeper understanding of its regulatory functions. | ||||||
GW 5074 | 220904-83-6 | sc-200639 sc-200639A | 5 mg 25 mg | $106.00 $417.00 | 10 | |
GW5074 is a selective inhibitor of mitogen-activated protein kinase kinase kinase MEKK1, and it indirectly influences PP2A. By inhibiting MEKK1, GW5074 modulates the activation of downstream signaling pathways, potentially impacting PP2A-regulated cellular processes. This indirect regulation provides a tool for exploring the crosstalk between signaling cascades and PP2A-mediated cellular responses. | ||||||
FTY720 | 162359-56-0 | sc-202161 sc-202161A sc-202161B | 1 mg 5 mg 25 mg | $32.00 $75.00 $118.00 | 14 | |
FTY720 Phosphate is the phosphorylated form of FTY720 (Fingolimod) and indirectly modulates PP2A activity. By regulating the expression of endogenous PP2A inhibitors, FTY720 Phosphate promotes the activation of PP2A. This indirect regulation offers insights into the intricate mechanisms controlling PP2A activity and its impact on cellular processes and signaling cascades. | ||||||