Hsp90α ab2928

Manufactured by Abcam

Sourced in United States, United Kingdom

HSP90α (ab2928) is a recombinant protein that corresponds to a portion of the human heat shock protein 90 alpha (HSP90α) sequence. HSP90α is a molecular chaperone involved in the folding and maturation of various client proteins.

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Lab products found in correlation

Trueblot anti rabbit ig ip beads, by Rockland Immunochemicals (1 mentions) γ catenin 2309, by Cell Signaling Technology (1 mentions) Lipofectamine method, by Thermo Fisher Scientific (1 mentions) Hop sra 1500, by Enzo Life Sciences (1 mentions) Cdc37 4793, by Cell Signaling Technology (1 mentions)

Spelling variants of this product

Ab2928 (7 citations) HSP90α (5 citations)

4 protocols using hsp90α ab2928

Immunoprecipitation of Halo Fusion Proteins

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Immunoprecipitation was carried out using HCC1937 and MDA‐MB231 cells expressing Halo fusion proteins. The cell lysates were incubated with each antibody and then TrueBlot anti‐rabbit Ig IP beads (Rockland, Limerick, PA, USA) were added. After incubation, the binding proteins were eluted from the beads with 1× SDS Sample Buffer (62.5 mmol/L Tris pH 6.8, 2% SDS, 10% glycerol, 0.1 mol/L DTT, 0.005% bromophenol blue, 2% 2‐mercaptoethanol). The following antibodies were used for IP: HSP90α (ab2928), and GRP78 (ab21685) from Abcam Inc. (Cambridge, MA, USA), and γ‐catenin (#2309) from Cell Signaling Technology Inc. (Beverly, MA, USA).

Moriya C., Taniguchi H., Nagatoishi S., Igarashi H., Tsumoto K, & Imai K. (2017). PRDM14 directly interacts with heat shock proteins HSP90α and glucose‐regulated protein 78. Cancer Science, 109(2), 373-383.

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Tau Protein Expression and Characterization

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For Fig. 2f, N2a cells were transfected with an eYFP-tau containing plasmid (a kind gift from Dr. Marc Diamond) using the Lipofectamine method (Invitrogen). Single colonies were obtained and selected using media supplemented with G418 (Gibco) and expanded for screening. Stably transfected clones were treated with indicated inhibitors for 24 h, then drug was washed off and new media was added for an additional 24 h. For Fig. 5d, N2a cells with transient overexpression of CMV6-Tau (4R0N) were used. Cells were lysed in 20 mM Tris pH 7.4, 20 mM KCl, 5 mM MgCl₂, 0.01% NP40 buffer containing protease and phosphatase inhibitors. For native gels, the protein extracts were loaded onto 4–10% native gradient gel and resolved at 4 °C. Gels were immunoblotted following a transfer in 0.1% SDS-containing transfer buffer for 1 h. Antibodies used were: HSP110 (SPC-195) (Stressmarq); HSC70 (SPA-815) and HOP (SRA-1500) (Enzo); HSP90α (ab2928) Abcam; and CDC37 (4793) (Cell Signalling Technology).

Inda M.C., Joshi S., Wang T., Bolaender A., Gandu S., Koren III J., Che A.Y., Taldone T., Yan P., Sun W., Uddin M., Panchal P., Riolo M., Shah S., Barlas A., Xu K., Chan L.Y., Gruzinova A., Kishinevsky S., Studer L., Fossati V., Noggle S.A., White J.R., de Stanchina E., Sequeira S., Anthoney K.H., Steele J.W., Manova-Todorova K., Patil S., Dunphy M.P., Pillarsetty N., Pereira A.C., Erdjument-Bromage H., Neubert T.A., Rodina A., Ginsberg S.D., De Marco Garcia N., Luo W, & Chiosis G. (2020). The epichaperome is a mediator of toxic hippocampal stress and leads to protein connectivity-based dysfunction. Nature Communications, 11, 319.

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Native Gel Immunoblotting of Heat Shock Proteins

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Cells were treated for 24 hr with the indicated concentrations of PU-H71. The agent was washed off, new media was added for another 24 hr, and cells were then lysed in 20 mM Tris pH 7.4, 20 mM KCl, 5 mM MgCl₂, 0.01% NP40 buffer containing protease and phosphatase inhibitors. For native gels, the protein extracts were loaded onto 4–10% native gradient gel and resolved at 4 °C. The gels were immunoblotted follo wing a transfer in 0.1% SDS-containing transfer buffer for 1 hr. The antibodies used were: HSC70 (SPA-815; RRID:AB_10617277) from Enzo; HSP90β (SMC-107; RRID:AB_854214) and HSP110 (SPC-195; RRID:AB_2119373) from Stressmarq; HSP90α (ab2928; RRID:AB_303423) from Abcam. Their total protein was determined using the protocol discussed in the later section (Pharmacodynamic Analyses in Mice).

Pillarsetty N., Jhaveri K., Taldone T., Caldas-Lopes E., Punzalan B., Joshi S., Bolaender A., Uddin M.M., Rodina A., Yan P., Ku A., Ku T., Shah S.K., Lyashchenko S., Burnazi E., Wang T., Lecomte N., Janjigian Y., Younes A., Batlevi C.W., Guzman M.L., Roboz G.J., Koziorowski J., Zanzonico P., Alpaugh M.L., Corben A., Modi S., Norton L., Larson S.M., Lewis J.S., Chiosis G., Gerecitano J.F, & Dunphy M.P. (2019). Paradigms for precision medicine in epichaperome cancer therapy. Cancer cell, 36(5), 559-573.e7.

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Epichaperome Analysis in Tumors

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For epichaperome analysis, tumors were cut into small pieces and homogenized in native lysis buffer (20 mM HEPES pH 7.5, 50 mM KCl, 5 mM MgCl₂, 0.01% NP40, 20 mM Na₂MoO₄) containing protease and phosphatase inhibitors using BioMasher^® II Micro Tissue Homogenizers (VWR, Radnor, PA, USA). Samples were left on ice for 30 min and then subjected to native PAGE analysis. Protein concentrations were determined using the BCA kit (Pierce, Waltham, MA, USA) according to the manufacturer’s instructions. Protein lysate (10–60 µg) was loaded onto 5.5% native gel and resolved at 4 °C, transferred to nitrocellulose membrane, and probed with the indicated primary antibodies: HSP90α (AB2928; RRID:AB_303423; 1:8000) from Abcam (Cambridge, UK), HOP (ADI-SRA-1500; RRID:AB_10618972; 1:1000) from Enzo and CDC37 (4793S; RRID:AB_10695539; 1:1000) from Cell Signaling (Danvers, MA, USA). Membranes were then incubated with a 1:5000 dilution of a peroxidase-conjugated corresponding secondary antibody. Detection was performed using the ECL Enhanced Chemiluminescence Detection System (Pierce™ ECL Western Blotting Substrate) according to the manufacturer’s instructions.

Sharma S., Joshi S., Kalidindi T., Digwal C.S., Panchal P., Lee S.G., Zanzonico P., Pillarsetty N, & Chiosis G. (2023). Unraveling the Mechanism of Epichaperome Modulation by Zelavespib: Biochemical Insights on Target Occupancy and Extended Residence Time at the Site of Action. Biomedicines, 11(10), 2599.

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