HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361873, 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
Fish, Human, Salmon (Salmonidae)
447
350
320
204
158
74
73
54
49
38
37
34
34
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25
25
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18
18
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11
9
8
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4
3
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
Host
Rabbit
347
134
11
1
1
Clonality
Polyclonal
Conjugate
This HSP90 antibody is un-conjugated
23
19
19
18
16
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15
15
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15
15
15
10
8
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4
4
4
3
3
3
3
3
3
3
2
2
2
Application
Western Blotting (WB)
428
304
293
249
196
180
156
54
33
2
2
2
2
1
1
1
Options
Supplier
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Immunogen KLH-conjugated synthetic peptide chosen from a highly conserved region of HSP90 found in both the alpha and beta form. The taget peptide is perfectly conserved in animals.
Specificity Detects ~90 kDa. In salmonid fish a cross-reactive band at 40 kDa is observed. Antibody will also detect a Human recombinant HSP90 protein.
Purification Rabbit Antiserum
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). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Gene ID 100136360
NCBI Accession NP_001117004
UniProt Q9W6K6
Pathways M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals
Application Notes
  • WB (1:5000)
  • optimal dilutions for assays should be determined by the user.
Comment

0.2 μl/ml of SPC-316 was sufficient for detection of HSP90 in 10 μg Heat shocked (25°C) rainbow trout nuclear fraction lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Lyophilized
Buffer Lyophilized rabbit Antiserum. For reconstitution add 100 μL of sterile water.
Storage -20 °C
Supplier Images
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361873) Hsp90, rainbow trout.
Product cited in: Ings, Oakes, Vijayan, Servos: "Temporal changes in stress and tissue-specific metabolic responses to municipal wastewater effluent exposure in rainbow trout." in: Comparative biochemistry and physiology. Toxicology & pharmacology : CBP, Vol. 156, Issue 2, pp. 67-74, 2012 (PubMed).

Ings, Servos, Vijayan: "Hepatic transcriptomics and protein expression in rainbow trout exposed to municipal wastewater effluent." in: Environmental science & technology, Vol. 45, Issue 6, pp. 2368-76, 2011 (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).