HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361732, 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
Human, Mouse (Murine), Rabbit, Rat (Rattus)
446
349
319
203
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
345
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
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP)
428
304
292
249
196
179
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 Ah receptor (Aryl hydrocarbon receptor)
Clone 8D3
Isotype IgM
Specificity Detects 90 kDa. Co-immunoprecipitates HSP90 complexes, including HSP70, Hop, Ah receptors, glucocorticoid receptors, heme-regulated eukaryotic initiation factor 2α (eIF-2α) kinase (HRI).
Purification PEG 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). 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
  • ICC/IF (1:100)
  • IP (1:1000)
  • optimal dilutions for assays should be determined by the user.
Comment

Goat anti-mouse IgM was used to bind 25 μl of protein G-Sepharose. SMC-109 IgM from 0.5 ml of high speed supernatant medium was loaded onto the IgG resin and incubated with 100 μl of rabbit reticulocyte lysate for 30 min. at 30C. After washing (4X1 ml), bound proteins were resolved on SDS PAGE, including HSP90, HSP70 and Hop.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS, 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
 image for anti-HSP90 antibody (Heat Shock Protein 90) (ABIN361732) Hsp90 complex (8D3) isolation, IP (rabbit reticulocyte lysate) SDS PAGE Coomassie.
Product cited in: Shimamura, Perera, Foley, Sang, Rodig, Inoue, Chen, Li, Carretero, Li, Sinha, Carey, Borgman, Jimenez, Meyerson, Ying, Barsoum, Wong, Shapiro: "Ganetespib (STA-9090), a nongeldanamycin HSP90 inhibitor, has potent antitumor activity in in vitro and in vivo models of non-small cell lung cancer." in: Clinical cancer research : an official journal of the American Association for Cancer Research, Vol. 18, Issue 18, pp. 4973-85, 2012 (PubMed).

Ardi, Alexander, Johnson, McAlpine: "Macrocycles that inhibit the binding between heat shock protein 90 and TPR-containing proteins." in: ACS chemical biology, Vol. 6, Issue 12, pp. 1357-66, 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).

Uma, Hartson, Chen, Matts: "Hsp90 is obligatory for the heme-regulated eIF-2alpha kinase to acquire and maintain an activable conformation." in: The Journal of biological chemistry, Vol. 272, Issue 17, pp. 11648-56, 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).

Dalman, Bresnick, Patel, Perdew, Watson, Pratt: "Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro." in: The Journal of biological chemistry, Vol. 264, Issue 33, pp. 19815-21, 1989 (PubMed).

Perdew: "Association of the Ah receptor with the 90-kDa heat shock protein." in: The Journal of biological chemistry, Vol. 263, Issue 27, pp. 13802-5, 1988 (PubMed).