HSP90 Antibody, Clone 4F3.E8: FITC

Monoclonal

Blue Ice or 4ºC. All orders received in North America by 12:00 PM PST Monday to Thursday will usually be shipped out on the same day. North American customers will typically receive their orders within 1-2 business days. All shipments are F.O.B. from point of shipment, pre-paid and added to the invoice. Freight charges include but not limited to: priority service and packaging materials.Products are shipped with “cold packs” in insulated containers. There is a charge for this packaging and for the shipping costs via FedEx. Please inspect packages immediately upon receipt and inform Labscoop Customer Support of any shortage or damage within 48 hours of receipt. We can only accept returns after we have given prior authorization and issued specific shipping instructions. If a customer wishes to use their own FedEx account number please indicate this on the purchase order or during checkout.

Canada

WB, IHC, ICC/IF, IP, ELISA

https://www.ncbi.nlm.nih.gov/gene/3320

4F3.E8

NP_001017963.2

Non-hazardous

Non-hazardous

Not for use in humans. Not for use in diagnostics or therapeutics. For in vitro research use only.

1 mg/ml

WB (1:2000), IHC (1:100), ICC/IF (1:100); optimal dilutions for assays should be determined by the user.

Mouse

IgG2a

Human | Mouse | Rat | Plant | Wheat (Triticum spp.)

FITC

Protein G Purified

ISO 9001:2015

HSP90

Recombinant Human HSP90 purified from E.coli

Detects ~90kDa. This antibody detects both ? and ? forms of HSP90 equally well.

PBS pH7.2, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated

https://antibodyregistry.org/search.php?q=AB_2698392

Cytoplasm | Melanosome

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 its 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.

1. Nemoto T. et al. (1997) J.Biol Chem. 272: 26179-26187. 2. Minami, Y, et al. (1991), J.Biol Chem. 266: 10099-10103. 3. Arlander SJH, et al. (2003) J Biol Chem 278: 52572-52577. 4. Pearl H, et al. (2001) Adv Protein Chem 59: 157-186. 5. Neckers L, et al. (2002) Trends Mol Med 8: S55-S61. 6. Pratt W, Toft D. (2003) Exp Biol Med 228: 111-133. 7. Pratt W, Toft D. (1997) Endocr Rev 18: 306–360. 8. Pratt WB. (1998) Proc Soc Exptl Biol Med 217: 420–434. 9. Whitesell L, et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328. 10. Nemoto, T. (1997) Biochem and Mol. Bio Intl. 42 (5): 881-889.

Cancer | Heat Shock | Cell Signaling | Protein Trafficking | Chaperone Proteins | Cancer | Tumor Biomarkers

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