Description
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, 10 bp insertion in exon 2 and 1 bp insertion in exon 2.
Product details:
Knockout cell lysate achieved by CRISPR/Cas9.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Lysate preparation:
Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10).
This means that the protein of interest is denatured.
If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions:
Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
This product is subject to limited use licenses from The Broad Institute, ERS Genomics Limited and Sigma-Aldrich Co. LLC, and is developed with patented technology. For full details of the licenses and patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-PTGES3, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Ambient - Can Ship with Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C
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.
