HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361718, Supplier: Log in to see
Antigen
  • git10
  • swo1
  • HSP90
  • htpG
  • SCBAC25F8.08
  • 23.m06066
  • 17.m07646
  • HSP90-1
  • 143198_at
  • 83
  • 83K HSP
  • DMHSP82
  • E(sev)3A
  • E(sina)2
  • HSP82
  • HSP83
  • ORF1
  • Su(Raf)3A
  • anon-EST:Liang-2.53
  • anon-WO0068693
  • anon-WO0140519.209
  • clone 2.53
  • en(lz)3C/4C
  • hsp84
  • l(3)j5C2
  • ms(3)08445
  • stc
  • DmelCG1242
  • CG1242
  • 86kDa
  • 89kDa
  • AL024080
  • AL024147
  • Hsp86-1
  • Hsp89
  • Hsp90
  • Hspca
  • hsp4
  • Hsp86
  • EL52
  • HSP86
  • HSP89A
  • HSP90A
  • HSP90N
  • HSPC1
  • HSPCA
  • HSPCAL1
  • HSPCAL4
  • HSPN
  • LAP2
  • hsp86
  • hsp89
  • hsp90
  • hsp90a
  • hspc1
  • hspca
  • hspn
  • lap2
  • D6S182
  • HSP84
  • HSP90B
  • HSPC2
  • HSPCB
  • heat shock protein Hsp90
  • Hsp90 chaperone
  • heat shock protein 90
  • Heat Shock Protein 90
  • LOC100384473
  • Heat shock protein 83
  • heat shock protein 90, alpha (cytosolic), class A member 1
  • heat shock protein 90kDa alpha (cytosolic), class A member 1
  • heat shock protein 90kDa alpha (cytosolic), class A member 1, gene 1
  • heat shock protein 90kDa alpha (cytosolic), class B member 1
  • hsp90
  • HSP90
  • htpG
  • SCO7516
  • TP04_0646
  • TP01_0934
  • GbCGDNIH1_0315
  • MAV_2118
  • HSP90C
  • BBOV_IV008400
  • BBOV_III007380
  • ACICU_00312
  • ECL_01244
  • YE105_C1172
  • pco153543(105)
  • Hsp83
  • Hsp90aa1
  • HSP90AA1
  • hsp90aa1.1
  • HSP90AB1
Alternatives
anti-Human HSP90 antibody for Immunofluorescence (fixed cells)
Reactivity
Chicken, Dog (Canine), Fish, Human, Mouse (Murine), Rabbit, Rat (Rattus), Shark
448
350
320
204
158
74
73
54
50
38
37
34
34
30
25
25
20
18
18
16
16
16
11
9
8
6
5
4
4
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
Host
Mouse
347
135
11
1
1
Clonality (Clone)
Monoclonal ()
Conjugate
This HSP90 antibody is un-conjugated
23
19
19
18
16
15
15
15
15
15
15
15
15
15
15
10
8
7
5
4
4
4
4
3
3
3
3
3
3
3
2
2
2
Application
Antibody Array (AA), ELISA, Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blotting (WB)
429
304
293
249
196
180
156
54
33
2
2
2
2
1
1
1
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Immunogen Recombinant human HSP90beta
Clone H9010
Isotype IgG2a
Specificity Detects 90 kDa. Detects HSP90 beta in all reactive species except in Chicken, where it detects both alpha and beta isoforms.
Purification Protein G Purified
Alternative Name HSP90 (HSP90 Antibody Abstract)
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.
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Pathways M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
Application Notes
  • WB (1:2500)
  • IHC (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

1 μg/ml of SMC-107 was sufficient for detection of HSP90beta in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Hsp90 (H9010) Western Blotting, heat shock Hela.
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Hsp90 (H9010), cell lines.
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361718) Rabbit reticulocyte lysate
Product cited in: Jayaprakash, Dong, Zou, Bhatia, OBrien, Chen, Woodley, Li: "Hsp90α and Hsp90β together operate a hypoxia and nutrient paucity stress-response mechanism during wound healing." in: Journal of cell science, Vol. 128, Issue 8, pp. 1475-80, 2015 (PubMed).

Teigen, Orczewska, McLaughlin, OBrien: "Cold acclimation increases levels of some heat shock protein and sirtuin isoforms in threespine stickleback." in: Comparative biochemistry and physiology. Part A, Molecular & integrative physiology, Vol. 188, pp. 139-47, 2015 (PubMed).

Hunter, OHagan, Kenyon, Dhanani, Prinsloo, Edkins: "Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells." in: PLoS ONE, Vol. 9, Issue 1, pp. e86842, 2014 (PubMed).

Bessemer, Butler, Tunnah, Callaghan, Rundle, Currie, Dieni, MacCormack: "Cardiorespiratory toxicity of environmentally relevant zinc oxide nanoparticles in the freshwater fish Catostomus commersonii." in: Nanotoxicology, pp. 1-10, 2014 (PubMed).

Patel, Yan, Seidler, Patel, Sun, Yang, Que, Taldone, Finotti, Stephani, Gewirth, Chiosis: "Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2." in: Nature chemical biology, Vol. 9, Issue 11, pp. 677-84, 2013 (PubMed).

Espallergues, Teegarden, Veerakumar, Boulden, Challis, Jochems, Chan, Petersen, Deneris, Matthias, Hahn, Lucki, Beck, Berton: "HDAC6 regulates glucocorticoid receptor signaling in serotonin pathways with critical impact on stress resilience." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 32, Issue 13, pp. 4400-16, 2012 (PubMed).

Taldone, Zatorska, Patel, Zong, Rodina, Ahn, Moulick, Guzman, Chiosis: "Design, synthesis, and evaluation of small molecule Hsp90 probes." in: Bioorganic & medicinal chemistry, Vol. 19, Issue 8, pp. 2603-14, 2011 (PubMed).

Chen, Prior, Dargusch, Roberts, Riek, Eichmann, Chiruta, Akaishi, Abe, Maher, Schubert: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." in: PLoS ONE, Vol. 6, Issue 12, pp. e27865, 2011 (PubMed).

Gershburg, Murphy, Marschall, Gershburg: "Key motifs in EBV (Epstein-Barr virus)-encoded protein kinase for phosphorylation activity and nuclear localization." in: The Biochemical journal, Vol. 431, Issue 2, pp. 227-35, 2010 (PubMed).

Background publications Arlander, Eapen, Vroman, McDonald, Toft, Karnitz: "Hsp90 inhibition depletes Chk1 and sensitizes tumor cells to replication stress." in: The Journal of biological chemistry, Vol. 278, Issue 52, pp. 52572-7, 2003 (PubMed).

Pratt, Toft: "Regulation of signaling protein function and trafficking by the hsp90/hsp70-based chaperone machinery." in: Experimental biology and medicine (Maywood, N.J.), Vol. 228, Issue 2, pp. 111-33, 2003 (PubMed).

Neckers: "Hsp90 inhibitors as novel cancer chemotherapeutic agents." in: Trends in molecular medicine, Vol. 8, Issue 4 Suppl, pp. S55-61, 2002 (PubMed).

Pearl, Prodromou: "Structure, function, and mechanism of the Hsp90 molecular chaperone." in: Advances in protein chemistry, Vol. 59, pp. 157-86, 2002 (PubMed).

Loo, Jensen, Cui, Hou, Chang, Riordan: "Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome." in: The EMBO journal, Vol. 17, Issue 23, pp. 6879-87, 1999 (PubMed).

Pratt: "The hsp90-based chaperone system: involvement in signal transduction from a variety of hormone and growth factor receptors." in: Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.), Vol. 217, Issue 4, pp. 420-34, 1998 (PubMed).

Barent, Nair, Carr, Ruan, Rimerman, Fulton, Zhang, Smith: "Analysis of FKBP51/FKBP52 chimeras and mutants for Hsp90 binding and association with progesterone receptor complexes." in: Molecular endocrinology (Baltimore, Md.), Vol. 12, Issue 3, pp. 342-54, 1998 (PubMed).

Nemoto, Sato, Iwanari, Yamashita, Takagi: "Domain structures and immunogenic regions of the 90-kDa heat-shock protein (HSP90). Probing with a library of anti-HSP90 monoclonal antibodies and limited proteolysis." in: The Journal of biological chemistry, Vol. 272, Issue 42, pp. 26179-87, 1997 (PubMed).

Pratt, Toft: "Steroid receptor interactions with heat shock protein and immunophilin chaperones." in: Endocrine reviews, Vol. 18, Issue 3, pp. 306-60, 1997 (PubMed).

Whitesell, Mimnaugh, De Costa, Myers, Neckers: "Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 91, Issue 18, pp. 8324-8, 1994 (PubMed).

Minami, Kawasaki, Miyata, Suzuki, Yahara: "Analysis of native forms and isoform compositions of the mouse 90-kDa heat shock protein, HSP90." in: The Journal of biological chemistry, Vol. 266, Issue 16, pp. 10099-103, 1991 (PubMed).