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HSP90 antibody (Heat Shock Protein 90)

Details for Product anti-HSP90 Antibody No. ABIN361682, 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-Plasmodium falciparum HSP90 antibody for Immunocytochemistry
Reactivity
Plasmodium falciparum
447
354
324
204
157
75
70
52
51
40
38
34
34
30
25
25
21
19
19
16
16
16
11
9
9
7
5
4
4
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
Host
Rabbit
346
136
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
7
5
4
4
3
3
3
3
3
3
3
3
3
2
2
2
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
433
304
294
253
197
175
157
54
29
2
2
2
2
1
1
1
Options
Supplier
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Immunogen Recombinant full length PfHSP90
Specificity Detects ~ 86 kDa. Specific to P. falciparum and does not cross-react to HSP90 from Human, yeast, and dictyostelium.
Purification Protein A 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 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 (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 immune adsorption 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). Recently, Prof. Tatu's laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.
Gene ID 811999
NCBI Accession XP_001348591
UniProt Q8IL32
Pathways M Phase
Application Notes
  • WB (1:2000)
  • ICC/IF (1:50)
  • optimal dilutions for assays should be determined by the user.
Comment

0.7 μg/ml of SPC-187 was sufficient for detection of PfHSP90 in 20 μg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1.56 mg/mL
Buffer PBS pH 7.4, 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) (ABIN361682) PfHsp90, malarial parasite lysate.
Product cited in: Shahinas, Folefoc, Taldone, Chiosis, Crandall, Pillai: "A purine analog synergizes with chloroquine (CQ) by targeting Plasmodium falciparum Hsp90 (PfHsp90)." in: PLoS ONE, Vol. 8, Issue 9, pp. e75446, 2013 (PubMed).

Background publications Pavithra, Banumathy, Joy, Singh, Tatu: "Recurrent fever promotes Plasmodium falciparum development in human erythrocytes." in: The Journal of biological chemistry, Vol. 279, Issue 45, pp. 46692-9, 2004 (PubMed).

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).

Banumathy, Singh, Pavithra, Tatu: "Heat shock protein 90 function is essential for Plasmodium falciparum growth in human erythrocytes." in: The Journal of biological chemistry, Vol. 278, Issue 20, pp. 18336-45, 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).

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).

Lowe: "Colipase stabilizes the lid domain of pancreatic triglyceride lipase." in: The Journal of biological chemistry, Vol. 272, Issue 1, pp. 9-12, 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).

Garg, Hassid: "Nitric oxide decreases cytosolic free calcium in Balb/c 3T3 fibroblasts by a cyclic GMP-independent mechanism." in: The Journal of biological chemistry, Vol. 266, Issue 1, pp. 9-12, 1991 (PubMed).