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HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361822, 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 Western Blotting
Reactivity
Human, Mouse (Murine), Rat (Rattus)
442
350
320
202
156
74
69
51
50
40
38
33
33
30
25
25
21
19
19
16
16
16
10
8
8
6
5
4
4
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
Host
Rabbit
344
133
11
1
1
Clonality
Polyclonal
Conjugate
This HSP90 antibody is un-conjugated
22
19
18
17
15
15
15
15
15
15
15
15
15
15
15
10
8
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5
4
4
3
3
3
3
3
3
3
3
3
2
2
2
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
428
302
294
253
197
174
157
54
29
2
2
2
2
1
1
1
Options
Supplier
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Available images

Immunogen Full length protein HSP90
Specificity Detects ~90 kDa.
Purification Protein A Purified
Alternative Name HSP90 (HSP90 Antibody Abstract)
Background HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). 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 (5-6). 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 (7). Looking for more information on HSP90? Visit our new 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
Application Notes
  • WB (1:500)
  • IHC (1:100)
  • ICC/IF (1:100)
  • optimal dilutions for assays should be determined by the user.
Comment

A 1:500 dilution of SPC-104 was sufficient for detection of 0.2 mg of purified HSP90 by ECL immunoblot analysis.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Storage -20 °C
Supplier Images
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361822) Hsp90, Mouse backskin
Product cited in: Zhang, Pruitt, Tran, Du Bois, Zhang, Patel, Hoover, Simpson, Simmons, Gary, Snapper, Casellas, Mock: "B cell-specific deficiencies in mTOR limit humoral immune responses." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 191, Issue 4, pp. 1692-703, 2013 (PubMed).

Verheyen, Peeraer, Nuydens, Dhondt, Poesen, Pintelon, Daniels, Timmermans, Meert, Carmeliet, Lambrechts: "Systemic anti-vascular endothelial growth factor therapies induce a painful sensory neuropathy." in: Brain : a journal of neurology, Vol. 135, Issue Pt 9, pp. 2629-41, 2012 (PubMed).

Wagatsuma, Shiozuka, Kotake, Takayuki, Yusuke, Mabuchi, Matsuda, Yamada: "Pharmacological inhibition of HSP90 activity negatively modulates myogenic differentiation and cell survival in C2C12 cells." in: Molecular and cellular biochemistry, Vol. 358, Issue 1-2, pp. 265-80, 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).

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).

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).