Abcam, ab59459, Anti-Hsp90 antibody [D7a]

Size: 100µg
Anti-Hsp90 antibody [D7a] (ab59459) is a mouse monoclonal antibody detecting Hsp90 in Western Blot, Flow Cytometry, IP, IHC-P, IHC-Fr, ICC/IF . Suitable for Chicken, Cow, Human, Mouse, Pig, Rabbit, Rat . - KO validated for confirmed specificity - Over 20 publications - Trusted since 2007
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:D7a,
Isotype:IgG1,
Carrier free:No,
Reacts with:Mouse, Human, Pig, Chicken, Rat, Rabbit, Cow,
Applications:Flow Cyt, IP, ICC/IF, IHC-Fr, WB, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Native Full Length Protein corresponding to Human HSP90AA1.P07900,
Specificity:Can isolate complexes of HSP90, Src kinase and cec37

Product details:
What is this antibody validated in?
Anti-Hsp90 antibody [D7a] (ab59459) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Flow Cytometry (Flow Cyt), Immunoprecipitation (IP), Immunohistochemistry (IHC-P), Immunohistochemistry (IHC-Fr), Immunocytochemistry/immunofluorescence (ICC/IF) in Chicken, Cow, Human, Mouse, Pig, Rabbit, Rat samples.
What is the molecular weight of Hsp90?
Anti-Hsp90 [D7a] (ab59459) specifically detects a band for Hsp90 (UniProt: P11501) at a molecular weight of 95kDa.
Trusted by the scientific community
Anti-Hsp90 [D7a] (ab59459) was first used in a scientific publication in 2007 and has been cited over 20 times in peer-reviewed journals.
Reviewed by scientists
Anti-Hsp90 [D7a] (ab59459) has over 5 independent reviews from customers.
Specificity confirmed
The specificity of Anti-Hsp90 antibody [D7a] (ab59459) has been confirmed by Western blot testing in HSP90AA1 Knockout HAP1 cells.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Storage buffer-pH: 7.2Preservative: 0.09% Sodium azideConstituents: PBS, 50% Glycerol (glycerin, glycerine), 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--20°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.
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.