| 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 is a potent inhibitor of protein phosphatase 2A (PP2A), a critical regulator of cellular signaling pathways. Its unique structure allows for specific interactions with the catalytic subunit of PP2A, leading to altered phosphorylation states of target proteins. This modulation can significantly impact cell cycle regulation and apoptosis. The compound's affinity for PP2A is influenced by its stereochemistry, affecting reaction kinetics and cellular outcomes in various biological systems. | ||||||
Calyculin A | 101932-71-2 | sc-24000 sc-24000A | 10 µg 100 µg | $160.00 $750.00 | 59 | |
Calyculin A is a potent inhibitor of protein phosphatase 2A (PP2A), showcasing remarkable specificity in its interactions with the enzyme's active site. This compound stabilizes the phosphorylated state of target proteins, thereby modulating critical signaling pathways. Its unique structure allows for tight binding, influencing reaction kinetics and promoting prolonged phospho-regulation. The compound's selectivity and binding affinity contribute to its role in cellular processes, impacting various regulatory mechanisms. | ||||||
Cytostatin | 156856-30-3 | sc-394496 | 250 µg | $450.00 | ||
Cytostatin functions as a potent inhibitor of protein phosphatase 2A (PP2A-C), showcasing a remarkable affinity for the enzyme's active site. This interaction disrupts the dephosphorylation of key substrates, thereby modulating critical signaling pathways. Its unique structural features enable specific binding, influencing reaction kinetics and stability. The compound's hydrophobic regions enhance membrane permeability, facilitating its engagement in cellular processes and interactions with other biomolecules. | ||||||
Fostriecin | 87860-39-7 | sc-202160 | 50 µg | $260.00 | 9 | |
Fostriecin is a potent inhibitor of protein phosphatase 2A (PP2A), characterized by its ability to form stable complexes with the enzyme's catalytic subunit. This interaction disrupts PP2A's regulatory functions, leading to altered phosphorylation states of target proteins. The compound's unique structure allows for specific binding, influencing cellular signaling pathways and modulating various cellular processes. Its kinetic profile reveals a rapid onset of inhibition, making it a valuable tool for studying PP2A-related mechanisms. | ||||||