Overview: Product Name HSP90 beta Antibody (Ser254) DescriptionRabbit Anti-Human HSP90 beta (Ser254) Polyclonal Species Reactivity Human, Mouse, Rat Applications WB, IHC, IP, ICC/IF, ELISA Antibody Dilution WB (1:1000), IHC (1:100), ICC/IF (1:500), ELISA (1:40000); optimal dilutions for assays should be determined by the user. Host Species Rabbit Immunogen Species Human Immunogen Synthesized unphosphorylated peptide derived from human HSP90B around the phosphorylation site of serine 254 (V-G-SP-D-E). Conjugates Alkaline Phosphatase, APC, ATTO 390, ATTO 488, ATTO 565, ATTO 594, ATTO 633, ATTO 655, ATTO 680, ATTO 700, Biotin, FITC, HRP, PE/ATTO 594, PerCP, RPE, Streptavidin, Unconjugated Properties Storage Buffer PBS pH 7.4, 50% glycerol, 150mM NaCl, 0.02% sodium azide Storage Temperature -20ºC Shipping Temperature Blue Ice or 4ºC Purification Affinity Purified Clonality Polyclonal Isotype IgG Specificity Detects endogenous levels of total HSP90B protein. Cite This Product StressMarq Biosciences Cat# SPC-1266, RRID: AB_2712593 Certificate of Analysis A 1:1000 dilution of SPC-1266 was sufficient for detection of Hsp90 beta in 10 µg of HeLa cell lysates by ECL immunoblot analysis using Goat Anti-Rabbit IgG:HRP as the secondary antibody. Biological Description Alternative Names HSP84 Antibody, HSP90 Antibody, HSP86 Antibody, HSP89 Antibody, HSP90B Antibody, HSP90BETA Antibody, HSP90N Antibody, HSPC2 Antibody, HSPCA Antibody, HSPCAL1 Antibody, HSPCB Antibody, HSPN Antibody, LAP2 Antibody, NY REN 38 antigen Antibody Research Areas Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Chaperones, Protein Trafficking, Trafficking Cellular Localization Cytoplasm, Melanosome Accession Number NP_031381.2 Gene ID 3326 Swiss Prot P08238 Scientific 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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca. References 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 S.J.H., 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 W.B. (1998) Proc Soc Exptl Biol Med 217: 420–434. 9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA 91: 8324–8328. 10. Barent R. L. (1998) Mol. Endocrinol. 12: 342-354 11. Lo. M.A. (1998) EMBO J. 17: 6879-6887. Product Images Immunohistochemistry analysis using Rabbit Anti-Hsp90 beta Polyclonal Antibody (SPC-1266). Tissue: Breast Carcinoma Tissue. Species: Human. Fixation: Formalin fixed paraffin-embedded. Primary Antibody: Rabbit Anti-Hsp90 beta Polyclonal Antibody (SPC-1266) at 1:1000. The image on the right is treated with the synthesized phosphorylated peptide. Western blot analysis of Human HeLa cell lysates showing detection of ~90kDa Hsp90 beta protein using Rabbit Anti-Hsp90 beta Polyclonal Antibody (SPC-1266). Lane 1: Human HeLa cells treated with TNF-? (20ng/ml, 30mins). Lane 2: Untreated. Primary Antibody: Rabbit Anti-Hsp90 beta Polyclonal Antibody (SPC-1266) at 1:1000. Predicted/Observed Size: ~90kDa. Product Citations (0) Currently there are no citations for this product. ATTO 700Overview:High fluorescence yieldExcellent thermal and photostabilityQuenched by electron donorsVery hydrophilicGood solubility in polar solventsZwitterionic dyeMolar Mass: 575 g/molATTO 700 Datasheet Optical Properties:λex = 700 nmλem = 719 nmεmax = 1.25×105Φf = 0.25τfl = 1.6 nsBrightness = 31.3Laser = 676 nmFilter set = Cy®5.5