Description
Key facts
Cell type:Hep G2,
Species or organism:Human,
Tissue:Liver,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp deletion in exon 1,
Disease:Hepatocellular Carcinoma
Product details:
Although we aim to provide customers with a homozygous clone, feasibility will be dependent on the biology of the protein. Should only heterozygous edits be achieved, you will be notified of the outcome and be asked to confirm whether the cell line is acceptable. All clones will be accompanied with DNA sequencing data, and the mutation description.
We will provide viable cells that proliferate on revival.
This product is subject to limited use licenses from The Broad Institute and ERS Genomics Limited, and is developed with patented technology. For full details of the limited use licenses and relevant patents please refer to our
limited use license
patent pages
Properties and Storage Information:
Gene name-AHSA1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--196°C, Appropriate long-term storage conditions--196°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
AHA1 also known as activator of heat shock 90kDa protein ATPase homolog 1 is a co-chaperone protein that plays a role in the regulation of HSP90 ATPase activity. This protein has a molecular weight of approximately 38 kDa. AHA1 expression occurs in various tissues with higher amounts seen in metabolically active tissues. It interacts directly with HSP90 enhancing the chaperone's ability to fold client proteins correctly by stimulating its ATPase activity.
Biological function summary
AHA1 modulates the function of the HSP90 chaperone complex. This complex is important for the stabilization and activation of many client proteins such as steroid hormone receptors and kinases. AHA1 binds to the middle domain of HSP90 contributing to conformational changes necessary for efficient ATP hydrolysis. By influencing these molecular processes AHA1 plays a role in maintaining cellular protein homeostasis under stress conditions.
Pathways
The HSP90-AHA1 interaction is significant in the signaling pathway of cellular stress responses and protein folding. AHA1's upregulating effect on HSP90 ATPase activity facilitates the correct folding and function of client proteins involved in the MAPK/ERK and PI3K/AKT pathways. These pathways commonly involve interactions with proteins such as RAF and PI3K which are important in cell proliferation and survival processes.
AHA1 influences the progression of cancer and neurodegenerative diseases. Altered expression or function of AHA1 is linked to the development and progression of cancer as it affects the stability of oncoproteins through its interaction with HSP90. The protein is also connected to neurodegenerative diseases with disruptions in its function or expression impacting the folding and maintenance of neuronal proteins. In these diseases the AHA1-HSP90 interaction remains a critical component of pathogenic pathways affecting disease manifestation and progression.
