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HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361822, Supplier: Log in to see
Antigen
  • 17.m07646
  • 23.m06066
  • 83
  • 83K HSP
  • 86kDa
  • 89kDa
  • 143198_at
  • AL024080
  • AL024147
  • anon-EST:Liang-2.53
  • anon-WO0068693
  • anon-WO0140519.209
  • CG1242
  • clone 2.53
  • D6S182
  • DmelCG1242
  • DMHSP82
  • E(sev)3A
  • E(sina)2
  • EL52
  • en(lz)3C/4C
  • git10
  • hsp4
  • HSP82
  • HSP83
  • HSP84
  • hsp84
  • Hsp86
  • hsp86
  • HSP86
  • Hsp86-1
  • Hsp89
  • hsp89
  • HSP89A
  • hsp90
  • Hsp90
  • HSP90
  • HSP90-1
  • HSP90A
  • hsp90a
  • HSP90B
  • HSP90N
  • hspc1
  • HSPC1
  • HSPC2
  • hspca
  • Hspca
  • HSPCA
  • HSPCAL1
  • HSPCAL4
  • HSPCB
  • hspn
  • HSPN
  • htpG
  • l(3)j5C2
  • lap2
  • LAP2
  • ms(3)08445
  • ORF1
  • SCBAC25F8.08
  • stc
  • Su(Raf)3A
  • swo1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
314
194
187
105
82
38
35
31
29
25
21
20
18
18
13
13
13
10
9
5
5
5
4
3
3
3
2
2
2
2
2
2
2
1
1
Host
Rabbit
235
110
11
1
Clonality
Polyclonal
Conjugate
This HSP90 antibody is un-conjugated
15
12
11
10
9
9
9
9
9
9
9
9
9
9
9
9
9
4
3
3
3
3
2
2
2
2
2
2
2
2
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
317
213
200
198
140
132
75
10
2
2
2
2
Supplier
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Immunogen Full length protein HSP90
Specificity Detects ~90 kDa.
Purification Rabbit Antiserum
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).
Cellular Localization: Cytoplasm | Melanosome
Gene ID 3326
NCBI Accession NP_031381
UniProt P08238
Application Notes Recommended Dilution: WB (1:40000), IHC (1:100), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Buffer Rabbit Antiserum
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).