Abcam, ab109248, Anti-Hsp90 antibody [EPR3953]

Size: 20µL / 100µL / 1mL
Rabbit Recombinant Monoclonal HS90A antibody. Suitable for IHC-P, WB and reacts with Human, Mouse, Rat samples. Cited in 8 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR3953,
Isotype:IgG,
Carrier free:No,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:The mouse and rat recommendation is based on the WB results. We do not guarantee IHC-P for mouse and rat.

Product details:
Patented technology
Our RabMAb
technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to
RabMAb® patents
What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:
- High batch-to-batch consistency and reproducibility
- Improved sensitivity and specificity
- Long-term security of supply
- Animal-free batch production
For more information, read more on
recombinant antibodies

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Preservative: 0.01% Sodium azideConstituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% BSA, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Storage information-Stable for 12 months at -20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hsp90 also known as heat shock protein 90 is a molecular chaperone with a mass of about 90 kDa. It assists in the proper folding of client proteins stabilization of proteins against heat stress and degradation of misfolded proteins. Hsp90 is present in various cellular compartments including the cytoplasm nucleus and mitochondria. It is highly expressed in most eukaryotic cells reflecting its fundamental role in maintaining cellular protein homeostasis. Additionally Hsp90 serves as a loading control in western blot experiments due to its consistent expression levels across samples.
Biological function summary
Hsp90 interacts with many co-chaperones to form multi-protein complexes that aid its function. This protein is necessary for the maturation and stability of many signaling proteins including steroid hormone receptors and kinases like the tyrosine kinase D7A. Hsp90's chaperone activity is ATP-dependent with its N-terminal domain binding and hydrolyzing ATP leading to conformational changes that promote protein folding and assembly. Its influence extends to regulating cell cycle control and apoptosis highlighting its importance in cellular processes.
Pathways
Hsp90 participates in key biological pathways such as the protein folding response and the MAPK signaling pathway. In the protein folding process Hsp90 collaborates with co-chaperones like Aha1 and p23 to ensure accurate protein synthesis and repair. Its role in the MAPK signaling pathway influences cell growth proliferation and differentiation interacting with proteins like Raf-1 and MEK. These interactions highlight Hsp90's involvement in signal transduction and cellular stress responses.
Hsp90 is implicated in cancer and neurodegenerative diseases. Its overexpression often correlates with tumor progression and poor prognosis in cancers where it stabilizes client proteins like HER2 and AKT that drive oncogenic processes. In neurodegenerative disorders such as Alzheimer's disease altered Hsp90 function affects the degradation of proteins like tau contributing to pathogenic protein aggregation. Understanding Hsp90's role in these conditions offers avenues for therapeutic interventions targeting its chaperone activity.