PP2A-Cα/β Antibody (0.T.118): sc-56950

PP2A-Cα/β Antibody (0.T.118) is a mouse monoclonal IgG2b antibody that detects PP2A-Cα/β in mouse, rat, human, Xenopus, zebrafish, bovine, porcine, and canine samples through applications such as western blotting (WB), immunoprecipitation (IP), and immunofluorescence (IF). PP2A-Cα/β is a crucial component of the protein phosphatase 2A (PP2A) complex, which plays a vital role in cellular signaling by dephosphorylating serine and threonine residues on target proteins, thereby regulating various cellular processes including cell division, apoptosis, and metabolism. The structure of PP2A consists of a trimeric complex formed by a catalytic subunit, a regulatory subunit, and a variable subunit, allowing for a high degree of specificity and regulation in substrate interactions. This structural arrangement facilitates precise modulation of signaling pathways and enables assembly of distinct PP2A holoenzymes that target specific cellular functions, making PP2A-Cα/β essential for maintaining cellular homeostasis and responding to external stimuli. PP2A-Cα/β′s versatility in forming complexes with various regulatory subunits underscores its significance in diverse biological contexts, highlighting anti-PP2A-Cα/β antibody (0.T.118)′s importance in research focused on cellular signaling and disease mechanisms.

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PP2A-Cα/β Antibody (0.T.118) References:

1. Arctigenin attenuates diabetic kidney disease through the activation of PP2A in podocytes.  |  Zhong, Y., et al. 2019. Nat Commun. 10: 4523. PMID: 31586053
2. Selective PP2A Enhancement through Biased Heterotrimer Stabilization.  |  Leonard, D., et al. 2020. Cell. 181: 688-701.e16. PMID: 32315618
3. PP2A-B55 Holoenzyme Regulation and Cancer.  |  Goguet-Rubio, P., et al. 2020. Biomolecules. 10: PMID: 33266510
4. The PP2A-Integrator-CDK9 axis fine-tunes transcription and can be targeted therapeutically in cancer.  |  Vervoort, SJ., et al. 2021. Cell. 184: 3143-3162.e32. PMID: 34004147
5. Activation of the PP2A-B56α heterocomplex synergizes with venetoclax therapies in AML through BCL2 and MCL1 modulation.  |  Peris, I., et al. 2023. Blood. 141: 1047-1059. PMID: 36455198
6. Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A.  |  Pavic, K., et al. 2023. Nat Commun. 14: 1143. PMID: 36854761
7. Targeting PP2A-dependent autophagy enhances sensitivity to ruxolitinib in JAK2V617F myeloproliferative neoplasms.  |  Courdy, C., et al. 2023. Blood Cancer J. 13: 106. PMID: 37423955
8. Regulation and role of the PP2A-B56 holoenzyme family in cancer.  |  Peris, I., et al. 2023. Biochim Biophys Acta Rev Cancer. 1878: 188953. PMID: 37437699
9. NMDARs activation regulates endothelial ferroptosis via the PP2A-AMPK-HMGB1 axis.  |  Han, WM., et al. 2024. Cell Death Discov. 10: 34. PMID: 38233385
10. PP2A and GSK3 act as modifiers of FUS-ALS by modulating mitochondrial transport.  |  Tziortzouda, P., et al. 2024. Acta Neuropathol. 147: 41. PMID: 38363426

The preferred p-PP2A-Cα/β antibody is p-PP2A-Cα/β Antibody (F-8): sc-271903.