Abcam, ab226295, Anti-p23 antibody

Size: 100µL
Rabbit Polyclonal p23 antibody. Suitable for IP, WB, IHC-P and reacts with Human, Mouse samples. Cited in 2 publications. Immunogen corresponding to Synthetic Peptide within Human PTGES3 aa 100 to C-terminus.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Human,
Applications:IHC-P, IP, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Synthetic Peptide within Human PTGES3 aa 100 to C-terminus. The exact immunogen used to generate this antibody is proprietary information.Q15185

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Purification notes-ab226295 was affinity purified using an epitope specific to p23 immobilized on solid support., Storage buffer-pH: 7 - 8Preservative: 0.09% Sodium azideConstituents: Tris citrate/phosphate, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The p23 protein also known as prostaglandin E synthase 3 weighs about 18 kDa. It functions as a co-chaperone for the heat shock protein 90 (Hsp90) complex. P23 is found in the cytoplasm and nucleus of cells and shows expression across various tissues including the brain liver and kidney. It plays a role in stabilizing the ATP-bound state of Hsp90 assisting in client protein stabilization and maturation. P23 binding to the Hsp90 complex influences its chaperone activity.
Biological function summary
P23 assists Hsp90 in protein-folding processes. As part of the Hsp90 chaperone complex p23 contributes to the correct folding and functioning of several essential client proteins. This chaperone activity is important for cellular processes like signal transduction and protein degradation. Without p23 Hsp90's efficiency in maintaining protein homeostasis can decrease highlighting the importance of their interaction in the cell.
Pathways
The chaperone actions of p23 extensively impact protein signaling pathways and stress response mechanisms. P23 and Hsp90 are important in the Akt/PI3K signaling pathway which regulates cell proliferation and survival. The complex formed by p23 and Hsp90 also involves heat shock proteins like Hsp70 which collaborates in broader cellular stress responses. These connections demonstrate how p23 integrates into cellular regulation and signal transduction networks.
P23's interaction with Hsp90 relates to cancer development and progression. Dysregulation in the p23-Hsp90 interaction can lead to increased stabilization of oncogenic client proteins contributing to tumorigenesis. Additionally p23 implication has been noted in neurodegenerative diseases like Alzheimer's where protein misfolding plays a critical role. Here p23 involvement with proteins like Tau may link its chaperone activity to the pathological protein aggregation seen in such disorders.