- Catalog number
- M01692-3
- Size / count
- 200 µg
- Dry ice
- No
- Hazardous
- No
- Discontinued
- Yes
- Background
- HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms α and β, which share 85% sequence amino acid homology. The two isoforms of HSP90, are expressed in the cytosolic compartment (1) . Despite the similarities, HSP90α exists predominantly as a homodimer while HSP90β exists mainly as a monomer (2) . From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6) . Furthermore, HSP90 is highly conserved between species; having 60% and 78% amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. Despite it's label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1–2% of cytosolic protein) . It carries out a number of housekeeping functions – including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (7-8) . The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase (5) . When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (9) . For more information visit our HSP90 Scientific Resource Guide at http://www.HSP90.ca.
- Synonyms
- HSP84, HSP90, HSP90 beta, HSP90B, HSPC2, HSPCB
- Gene Name
- HSP90
- UniProt
- P08238
- Host
- Mouse
- Reactivity
- Human, Mouse, Rat, Rabbit, Chicken, Dog, Fish, Shark, Hamster
- Cross Reactivity
- Detects 90kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.
- Immunogen
- Recombinant human HSP90beta
- Clonality
- Monoclonal
- Clone
- Clone: H9010
- Applications
- WB, IHC, ICC, IF, IP, ELISA, Antibody Microarray
- Field of Research
- Cancer, Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction, Tumor Biomarkers
- Purification
- Protein G Purified
- Concentration
- 1 mg/ml
- Dilution
- WB (1:2500), IHC (1:100) ; optimal dilutions for assays should be determined by the user.
- Form
- Liquid
- Shipping Conditions
- Available
- Storage Conditions
- Store at -20°C for one year. Avoid repeated freeze-thaw cycles.
- Fragment
- IgG2a
- Subcellular Location
- Cytoplasm. Melanosome
- Protein Name
- HSP90
