Anti-PPP2R1B antibody [EPR10159]

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

The protein PPP2R1B also known as Protein Phosphatase 2 Scaffold Subunit A beta isoform acts as a scaffold for the assembly of PP2A complexes. PPP2R1B has a molecular mass of approximately 66 kDa. The protein expresses widely across various tissues with notable presence in the brain heart and skeletal muscle. As a scaffold subunit PPP2R1B coordinates the structural integrity necessary for phosphatase activity by recruiting regulatory and catalytic subunits important to its function.

Biological function summary

PPP2R1B integrates into the PP2A holoenzyme complex a major serine/threonine phosphatase. This complex regulates numerous cellular processes including cell growth division and signal transduction. PPP2R1B plays a role in maintaining cellular homeostasis through its regulatory activities. By doing so it links to various signaling events some of which control oncogenes and tumor suppressors demonstrating the protein's influence over cell cycle regulation and apoptosis.

Pathways

PPP2R1B plays a significant role in the Raf/MEK/ERK signaling pathway and the PI3K/AKT pathway. Through these pathways PPP2R1B interacts with PDPK1 and AKT1 modulating their phosphorylation status and thereby affecting cell proliferation and survival. By influencing such pathways PPP2R1B helps determine cellular responses to external stimuli impacting processes like differentiation and metabolism that are vital for organismal function.

Associated diseases and disorders

PPP2R1B links to cancer and Alzheimer's disease. Mutations or downregulation in PPP2R1B have been implicated in colorectal cancer where it alters the PP2A activity and allows unregulated cellular proliferation. In Alzheimer's disease PPP2R1B's interaction with tau protein goes awry contributing to neurofibrillary tangle formation. These connections highlight the importance of PPP2R1B in understanding the molecular basis of these diseases and potential therapeutic targets.