Abcam, ab266591, Human HSP90AA1 (Hsp90 alpha) knockout HEK-293T cell line

Size: 2 x 1000000Cells / vial / 1000000Cells / vial
HSP90AA1 KO cell line available to order. KO validated by Western blot. Free of charge wild type control available. Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 3. To order both knockout and wild-type control cells: select 2 x 1000000Cells/vial. To order only knockout cells: select 1000000Cells/vial.
Key facts
Cell type:HEK-293T,
Species or organism:Human,
Tissue:Kidney,
Form:LiquidSee storage information,
Knockout validation:Sanger Sequencing,Western blot,
Mutation description:Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp insertion in exon 3

Product details:
We will provide viable cells that proliferate on revival.
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-HSP90AA1, Gene editing type-Knockout, Gene editing method-CRISPR technology, Knockout validation-Sanger Sequencing, Western blot, Zygosity-Homozygous, 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.
Hsp90 alpha also known as Hsp90AA1 or 5G5 is a molecular chaperone with an approximate molecular weight of 90 kDa. It plays an important role in the folding stability and function of many client proteins. This protein is expressed ubiquitously in eukaryotic cells with high levels in the cytoplasm and the endoplasmic reticulum. Hsp90 alpha operates through a unique ATPase-driven chaperone cycle that modulates protein conformations helping in the assembly and disassembly of protein complexes.
Biological function summary
Hsp90 alpha assists in maintaining protein homeostasis and is part of a larger chaperome complex including co-chaperones and other chaperones such as Hsp70. It plays an important role in stress response by stabilizing proteins and preventing aggregation. Hsp90 alpha is essential for the normal function of several kinases and transcription factors which are important for cell signaling and regulation processes. It functions as a mediator for cellular response to environmental cues.
Pathways
Hsp90 alpha is an integral component in the signal transduction and cell cycle control pathways. It interacts with various signaling proteins and receptors like AKT and steroid hormone receptors to facilitate their proper folding and activation. Furthermore Hsp90 alpha influences the MAPK/ERK pathway playing a role in cell proliferation and differentiation. Its interaction with Hsp90 protein clients creates a regulatory framework across multiple pathways allowing precise control over cellular function.
Hsp90 alpha is linked to cancer and neurodegenerative diseases. Its enhanced expression in tumors correlates with the stabilization of oncogenic client proteins such as HER2 contributing to cancer progression. Additionally Hsp90 alpha relates to disorders like Alzheimer's disease due to its role in handling misfolded proteins. The protein interacts with co-chaperones like H1L1 which may influence its impact on disease outcomes highlighting the therapeutic potential of targeting Hsp90 alpha in these conditions.