Purified Hsp90 isolated from human therapeutic orchiectomy specimens.
UniProt ID:
P07900
Source:
Purified from mouse ascites.
Species reactivity:
Human Chicken
Applications:
Flow Cytometry, ICC, IHC, IP, WB
Recommended Dilutions/Conditions:
Flow Cytometry (1:100) Western Blot (1:1,000, colorimetric) Suggested dilutions/conditions may not be available for all applications. Optimal conditions must be determined individually for each application.
Application Notes:
Detects a band of ~90kDa by Western blot.
Purity Detail:
Protein G affinity purified.
Formulation:
Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
Handling:
Avoid freeze/thaw cycles.
Shipping:
Blue Ice
Long Term Storage:
-20°C
Scientific Background:
The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.
Regulatory Status:
RUO - Research Use Only
Western blot analysis of HSP90α, mAb (9D2) (Prod. No. ADI-SPA-840): Lane 1: MW marker, Lane 2: HSP90 native protein (Prod. No. ADI-SPP-770), Lane 3: HSP90 alpha recombinant protein (Prod. No. ADI-SPP-776), Lane 4: HSP90 beta recombinant protein (Prod. No. ADI-SPP-777), Lane 5: HeLa Cell Lysate (heat shocked) (Prod. No. ADI-LYC-HL101), Lane 6: PC-12 Cell Lysate (heat shocked) (Prod. No. ADI-LYC-PC101), Lane 7: 3T3 Cell Lysate (heat shocked) (Prod. No. ADI-LYC-3T101).
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Product Literature References
Phosphorylation of the Hsp90 Co-Chaperone Hop Changes its Conformational Dynamics and Biological Function: M. Castelli, et al.; J. Mol. Biol. 435, 167931 (2023), Abstract;
Secreted heat shock protein 90 promotes prostate cancer stem cell heterogeneity: K.D. Nolan, et al.; Oncotarget 8, 19323 (2017), Abstract; Full Text
4-hydroxybenzoic acid derivatives as HDAC6-specific inhibitors modulating microtubular structure and HSP90α chaperone activity against prostate cancer: C. Seidel, et al.; Biochem. Pharmacol. 99, 31 (2016), Application(s): Western blot, Immunoprecipitation, Abstract;
The association of Hsp90 expression induced by aspirin with anti-stress damage in chicken myocardial cells: X.H. Zhang, et al.; J. Vet. Sci. 17, 35 (2016), Application(s): Immunohistochemistry on heart tissue, Abstract; Full Text
KU675, a Concomitant Heat Shock Protein Inhibitor of Hsp90 and Hsc70 that Manifests Isoform Selectivity for Hsp90α in Prostate Cancer Cells: W. Liu, et al.; Mol. Pharmacol. 88, 121 (2015), Application(s): Western Blot, Abstract; Full Text
Phosphorylated and Unphosphorylated Serine 13 of CDC37 Stabilize Distinct Interactions Between its Client and HSP90 Binding Domains: W. Liu & R. Landgraf; Biochemistry 54, 1493 (2015), Application(s): Western blot using human BT474 breast cancer cell lysates, Abstract; Full Text
Expression of Hsp90α and cyclin B1 were related to prognosis of esophageal squamous cell carcinoma and keratin pearl formation: T. Huang, et al.; Int. J. Clin. Exp. Pathol. 7, 1544 (2014), Application(s): IHC of human esophageal squamous cell carcinoma, Abstract; Full Text
Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells: M. Hunter, et al.; PLoS One 9, e86842 (2014), Application(s): WB, IP of human breast cancer cells, Abstract; Full Text
Human TRiC complex purified from HeLa cells contains all eight CCT subunits and is active in vitro: K. Knee, et al.; Cell Stress Chaperones 18, 137 (2013), Application(s): WB of human TRiC from HeLa cell lysate, Abstract; Full Text
A potentially common peptide target in secreted heat shock protein-90α for hypoxia-inducible factor-1α-positive tumors: D. Sahu, et al.; Mol. Biol. Cell 23, 602 (2012), Application(s): Western blot using human HBL-100, HKC, MC, HDF, SCC-12, M-24, A431 and MDA-MB-231 cell lysates, Abstract; Full Text
Differential proteomic analysis of human erythroblasts undergoing apoptosis induced by epo-withdrawal: S. Pellegrin, et al.; PLoS One 7, e38356 (2012), Application(s): WB of human erythroblasts, Abstract; Full Text
Heat shock protein 90α (HSP90α), a substrate and chaperone of DNA-PK necessary for the apoptotic response: S. Solier, et al.; Proc. Natl. Acad. Sci. 109, 12866 (2012), Application(s): WB, IF of human colon, cervical, and leukemic carcinomas, Abstract; Full Text
HSP90 and HSP70 proteins are essential for stabilization and activation of WASF3 metastasis-promoting protein: Y. Teng, et al.; J. Biol. Chem. 287, 10051 (2012), Application(s): Western blot using human immunoprecipitated PC-3 cell lysates, Abstract; Full Text
Association of hsp90 to the hTERT promoter is necessary for hTERT expression in human oral cancer cells: M. Kang, et al. ; Carcinogenesis 29, 2425 (2008), Application(s): WB, IP, ChIP using human cell lysates, Abstract;
Expression of hsp90 in the human kidney and in proximal tubule cells exposed to heat, sodium arsenite and cadmium chloride: S. Somji, et al. ; Toxicol. Lett. 133, 241 (2002), Application(s): IHC, WB using human samples, Abstract;
Nucleophosmin-anaplastic lymphoma kinase (NPM-ALK), a novel Hsp90-client tyrosine kinase: down-regulation of NPM-ALK expression and tyrosine phosphorylation in ALK+ CD30+ lymphoma cells by the Hsp90 antagonist 17-allylamino,17-demethoxygeldanamycin: P. Bonvini, et al. ; Cancer Res. 62, 1559 (2002), Application(s): IP, WB using human samples, Abstract;
A role for the integrin alphavbeta8 in the negative regulation of epithelial cell growth: S.L. Nishimura, et al. ; Cancer Res. 60, 7084 (2000), Application(s): WB using human samples, Abstract;
Quantitation and intracellular localization of the 85K heat shock protein by using monoclonal and polyclonal antibodies: B.T. Lai, et al.; Mol. Cell. Biol. 4, 2802 (1984), Application(s): IP, ICC using human samples, Abstract;
