Mouse Hsp90 alpha Monoclonal Antibody | anti-HSP90AA1 antibody
Hsp90 alpha Antibody: ATTO 390
Immunocytochemistry/Immunofluorescence (ICC/IF)
(Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone 2G5.G3. Tissue: HaCaT cells. Species: Human. Fixation: Cold 100% methanol for 10 minutes at -20 degree C. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT.)
Western Blot (WB)
(Western Blot analysis of Rat tissue lysate showing detection of Hsp90 alpha protein using Mouse Anti-Hsp90 alpha Monoclonal Antibody, Clone 2G5.G3. Load: 15 ug. Block: 1.5% BSA for 30 minutes at RT. Primary Antibody: Mouse Anti-Hsp90 alpha Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Sheep Anti-Mouse IgG: HRP for 1 hour at RT.)
Scientific Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85% sequence amino acid homology. The two isoforms of Hsp90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta 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).
1. Orthwein, A. et al. (2010). Regulation of activation-induced deaminase stability and antibody gene diversification by Hsp90. JEM. 207 (12). 2751-2765. doi: 10.1084/jem.20101321
2. Di Noia, J.M. and Orthwein, A. (2011). Modulating and/or detecting activation induced deaminase and methods of use thereof. United States Patent Application. US 20110237560 A1
3. O'Neill, A.J. et al. (2011). Characterisation and manipulation of docetaxel resistant prostate cancer cell lines. Mol Cancer. 10 (126). doi:10.1186/1476-4598-10-126
4. Quanz, M. et al. (2012). Heat Shock Protein 90α (Hsp90α) Is Phosphorylated in Response to DNA Damage and Accumulates in Repair Foci. J Biol Chem. 287, 8803-8815. doi:10.1074/jbc.M111.320887
NCBI and Uniprot Product Information
NCBI Description
The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]
Uniprot Description
HSP90A: a molecular chaperone of the heat shock protein 90 family. Has ATPase activity. Known to interact with a wide variety of proteins including steroid hormone receptors, neuropeptide Y, FKBP51/54, and FKBP52. G protein-coupled receptor kinases are stabilized by interacting with HSP 90. Hsp70 and Hsp90 promote tau solubility and tau binding to microtubules, reducing insoluble tau phosphorylation of tau.
Protein type: Heat shock protein; Chaperone
Chromosomal Location of Human Ortholog: 14q32.33
Cellular Component: nucleoplasm; mitochondrion; membrane; cytoplasm; plasma membrane; extracellular region; melanosome; cytosol; nucleus
Molecular Function: identical protein binding; protein binding; protein homodimerization activity; TPR domain binding; ATPase activity; nitric-oxide synthase regulator activity; unfolded protein binding; nucleotide binding; ATP binding
Biological Process: axon guidance; receptor-mediated endocytosis; positive regulation of nitric oxide biosynthetic process; organelle organization and biogenesis; signal transduction; nitric oxide metabolic process; protein import into mitochondrial outer membrane; response to unfolded protein; mitochondrial transport; innate immune response; protein refolding; regulation of nitric-oxide synthase activity; mitotic cell cycle; G2/M transition of mitotic cell cycle; vascular endothelial growth factor receptor signaling pathway; chaperone-mediated protein complex assembly
