Anti hsp90

Manufactured by BD

Sourced in United States

Anti-HSP90 is a laboratory equipment product designed for the detection and analysis of the heat shock protein 90 (HSP90). HSP90 is a molecular chaperone that plays a crucial role in the folding, stability, and function of various client proteins. The Anti-HSP90 product facilitates the identification and quantification of HSP90 levels in biological samples, enabling researchers to study its involvement in cellular processes and its potential as a therapeutic target.

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Lab products found in correlation

Anti eif3d, by Fortis Life Sciences (4 mentions) Anti rps19, by Fortis Life Sciences (4 mentions) Dc protein assay, by Bio-Rad (4 mentions) Complete mini inhibitor mixture, by Roche (4 mentions) Anti gapdh, by Santa Cruz Biotechnology (4 mentions) Anti actin, by Abcam (3 mentions) Anti ha, by Roche (3 mentions) Anti parp, by Cell Signaling Technology (3 mentions) Anti mouse igg hrp, by Promega (3 mentions) Anti rabbit igg hrp, by Promega (3 mentions) Anti v5, by Thermo Fisher Scientific (3 mentions) Protease inhibitor cocktail, by Merck Group (3 mentions) Anti β actin, by Santa Cruz Biotechnology (3 mentions) Anti h3, by Abcam (3 mentions) Anti flag, by Merck Group (3 mentions) Bis tris gradient gel, by Thermo Fisher Scientific (3 mentions) Anti flag m2 antibody, by Merck Group (2 mentions) Nitrocellulose membrane, by Bio-Rad (2 mentions) Anti gapdh, by Cell Signaling Technology (2 mentions) Odyssey system, by LI COR (2 mentions)

Close spelling variants of this product

HSP90 (64 citations) Mouse anti-Hsp90 (4 citations) Anti-human Hsp90 (4 citations) Mouse monoclonal anti-HSP90 (4 citations) Anti-Hsp90 (610418, (3 citations) Mouse anti-HSP90 (610419; (2 citations) Anti-HSP90 antibody (2 citations) Monoclonal anti-HSP90 (2 citations)

49 protocols using anti hsp90

Immunoblotting and Immunoprecipitation Protocols

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Anti-GFP (Clonetech, 632381), anti-LAMP-1(Abcam, ab13523), anti-GAPDH (Abcam, ab9485), anti-actin(Abcam, ab8227), anti-α-synuclein (BD Transduction Laboratories, 610786), anti-HA (Roche applied science, 11867431001), monoclonal anti-FLAG M2 antibody (Sigma-Aldrich, F1804-200UG), anti-DAPK1 (Sigma, D1319-200UL), monoclonal anti-phospho-DAPK1 (pSer308, Sigma, D4941), anti-GluN2B (lab generated), anti-LAMP-2A (Abcam, ab18528), anti-Labmin B1(Abcam, ab16048), anti-HSP90 (BD Transduction Laboratories, 610418), anti-VDAC1 (Porin) (MitoSciences,MSA03). Antibodies were validated for their intended purpose (immunoblotting, immunocytochemistry, immunohistochemistry and co-immunoprecipitation) as outlined in the product sheet or in lab. Ammonium chloride (Sigma, A0171), 3-methyladenine (Sigma, M9281), MG132 (Sigma, C2211), Pepstatin A (Sigma), N-Methyl-D-aspartic acid (NMDA, Tocris Asc-052), H₂O₂ (Sigma, 7722-84-1) Catalase (Sigma, C1345), (2R)-amino-5-phosphon-opentanoic acid (APV, Ascent Scientific, Asc-003). GluN2B-CTM and TAT-GluN2B were synthesized by Brain Research Centre peptide synthesis facility at UBC. All other synthetic peptides used were synthesized by GL Biochem.

Fan X., Jin W.Y., Lu J., Wang J, & Wang Y.T. (2014). Rapid and reversible knockdown of endogenous proteins by peptide-directed lysosomal degradation. Nature neuroscience, 17(3), 471-480.

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Western Blot Analysis of Heat Stress

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For western blot analysis, solei were homogenized in reducing sample buffer (80 mM Tris-HCl, pH6.8, 2% sodium dodecyl sulfate, 10% glycerol and 0.1 M dithiothreitol) supplemented with Halt protease and phosphatase inhibitor cocktail (ThermoFisher Scientific). The following antibodies were used for western blot analysis: anti-HSF-1 (Santa Cruz Biotechnology), anti-hsp70 (StressMarq), anti-hsp90 (BD Transduction Laboratories), anti-P-CaMKII (ThermoFisher Scientific), anti-CaMKIIβ (Invitrogen). The quantitative analysis was performed using ImageJ software.

Kramerova I., Torres J.A., Eskin A., Nelson S.F, & Spencer M.J. (2018). Calpain 3 and CaMKIIβ signaling are required to induce HSP70 necessary for adaptive muscle growth after atrophy. Human Molecular Genetics, 27(9), 1642-1653.

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Quantification of Myc Protein Levels

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Cells were collected, counted, and lysed in 2×Laemmli buffer (100 mM Tris-HCl pH6.8, 200 mM DTT, 3% SDS, 20% glycerol) at 0.5-1x10⁴ cells/μl. Samples were heated at 95°C for 7 minutes and passed through an insulin syringe. Protein from 1x10⁵ cells was separated on 10% SDS-polyacrylamide gels and transferred to nitrocellulose membranes (Bio-Rad). After blocking (5% milk, PBST), membranes were incubated overnight at 4°C in primary antibody, then 1hr at RT in secondary antibody. The following antibodies were used: anti-c-Myc (1:1000, clone Y69, ab32072, Abcam), anti-Hsp90 (1:2500, 610419, BD Transduction Laboratories), anti-Hsp90 (1:1000, 4877S, Cell Signaling Technology), goat anti-mouse secondary antibody (1:50000, 1706516, Bio-Rad), and donkey anti-rabbit secondary antibody (1:50000, 711-035-152, Jackson ImmunoResearch). Protein bands were visualized using Amersham ECL Prime Western Blotting Detection Reagent (GE Healthcare). Quantification of Myc and Hsp90 protein levels was performed using the rectangle selection and measure tools in FIJI and Myc levels plotted relative to Hsp90 levels and normalized to negative control in relevant graphs. For cycloheximide experiments, Myc levels were normalized to negative control and half-life of Myc protein was determined using Prism8 software.

Olivero C., Martínez-Terroba E., Zimmer J., Liao C., Tesfaye E., Hooshdaran N., Schofield J., Bendor J., Fang D., Simon M., Zamudio J, & Dimitrova N. (2020). p53 activates the long noncoding RNA Pvt1b to inhibit Myc and suppress tumorigenesis. Molecular cell, 77(4), 761-774.e8.

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Western Blot Analysis of Cellular Proteins

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Cellular proteins were extracted using RIPA lysis buffer (50 mM HEPES, 150 mM NaCl, 1% Triton X-100, 0.1% SDS, 1% sodium deoxycholate) containing protease and phosphatase inhibitors (Roche Diagnostics) and quantified using BCA Protein Assay Kit (Thermo Fisher Scientific). Protein extracts were resolved by SDS-PAGE, transferred to PVDF membranes, and immunoblotted with anti-BRCA1 (1:500; sc-6954, Santa Cruz Biotechnology, Dallas, TX), anti-ISG15 (1:2000, a gift from Dr. Arthur Haas, Louisiana State University) [20] (link), anti-EGFR (1:1000, #2232), anti-pERK1/2 (1:2000, #9101), anti-ERK1/2 (1:2000, #4696), anti-USP18 (1:1000, #4813) (Cell Signaling Technology, Danvers, MA), anti-tubulin (1:3000, #T6199, Sigma), or anti-HSP90 (1:5000, #610418, BD Transduction Laboratories, Mississauga, Canada) antibodies. Immunoblots were then incubated with horseradish peroxidase–conjugated goat anti-rabbit (1:1000, sc-2004, Santa Cruz Biotechnology) or horse anti-mouse antibodies (1:1000, #7076, Cell Signaling Technology). Immunoreactive bands were visualized by enhanced chemiluminescence (Santa Cruz Biotechnology) and quantified using ImageJ software.

Hollingsworth J., Lau A., Tone A., Kollara A., Allen L., Colgan T.J., Dube V., Rosen B., Murphy K.J., Greenblatt E.M., Feigenberg T., Virtanen C, & Brown T.J. (2018). BRCA1 Mutation Status and Follicular Fluid Exposure Alters NFκB Signaling and ISGylation in Human Fallopian Tube Epithelial Cells. Neoplasia (New York, N.Y.), 20(7), 697-709.

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Protein Expression Analysis via Western Blotting

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Frozen tissues were lysed in radioimmunoprecipitation assay (RIPA) buffer (50 mM Tris pH 8.0, 1% Nonidet P-40, 0.5% sodium deoxycholate, 0.1% SDS, 150 mM NaCl, 2X protease inhibitors [20 μg/mL each of leupeptin, chymostatin, and pepstatin; Chemicon, EI8, EI6, and EI10, respectively]) for 20 min on ice and clarified by centrifugation. Protein concentration was assessed using the BCA assay (Thermo Scientific, #23225). The protein extracts were separated by SDS-PAGE and transferred onto PDVF membrane (Millipore, IPVH0010) using a semi-dry trans-blot system. Buffer containing TBS with 0.1% Tween 20 (TBS-T) and 4% milk (Biorad, 1706404) was used as a blocking agent. The following primary antibodies were used: anti-C7ORF10 (Proteintech Group, #21589-1-AP) and anti-Hsp90 (BD Transduction Laboratories, #610419).

Niska-Blakie J., Gopinathan L., Low K.N., Kien Y.L., Goh C.M., Caldez M.J., Pfeiffenberger E., Jones O.S., Ong C.B., Kurochkin I.V., Coppola V., Tessarollo L., Choi H., Kanagasundaram Y., Eisenhaber F., Maurer-Stroh S, & Kaldis P. (2019). Knockout of the non-essential gene SUGCT creates diet-linked, age-related microbiome disbalance with a diabetes-like metabolic syndrome phenotype. Cellular and Molecular Life Sciences, 77(17), 3423-3439.

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Immunoblot Analysis of Iron Metabolism Proteins

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Immunoblotting was performed using anti-FTH1 (MA5-32244; Thermo Fisher Scientific), anti-FTL (MA5-32755; Thermo Fisher Scientific), anti-NCOA4 (SAB1409837; Sigma-Aldrich), anti-TAX1BP1 (HPA024432; Sigma-Aldrich), anti-FIP200 (17250-1-AP; Proteintech), anti-HSP90 (610419; BD Transduction Laboratories), anti-GFP (A-6455; Thermo Fisher Scientific), and HRP-conjugated anti-DYKDDDDK/FLAG (015-22391; Fujifilm Wako Pure Chemical Corporation) as primary antibodies, and HRP-conjugated anti-rabbit IgG (111-035-144; Jackson ImmunoResearch) and HRP-conjugated anti-mouse IgG (315-035-003; Jackson ImmunoResearch) as secondary antibodies. Proteins were transferred to Immobilon-P PVDF membrane (IPVH00010; Millipore) with Trans-Blot Turbo Transfer System (Bio-Rad Laboratories). SuperSignal West Pico Chemiluminescent Substrate (1856135; Thermo Fisher Scientific) and Immobilon Western Chemiluminescent HRP Substrate (P90715; Millipore) were used to visualize the signals, which were detected by an image analyzer (FUSION SOLO.7S.EDGE; Vilber-Lourmat). Contrast and brightness adjustments were performed using the ImageJ (National Institutes of Health) or Photoshop CC 2019/2020 (Adobe) software.

Ohshima T., Yamamoto H., Sakamaki Y., Saito C, & Mizushima N. (2022). NCOA4 drives ferritin phase separation to facilitate macroferritinophagy and microferritinophagy. The Journal of Cell Biology, 221(10), e202203102.

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Purification of Mouse VDAC1 and RNF207 Proteins

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GST-fused protein of mouse VDAC1 was expressed in XL-10 cells using the pGEX6P-1 plasmid vector (GE Healthcare) and then purified by reduced glutathione-sepharose beads (GE Healthcare). His 6 -Flag-tagged mouse RNF207 proteins including deletion mutants were expressed in Rosetta blue cells with the use of the pET30 plasmid vector (Novagen, Madison, WI) and then purified with the use of ProBond metal affinity beads (Invitrogen).
For the production of recombinant proteins in Sf9 cells, we subcloned full-length mouse Rnf207 cDNAs into pFastBac HTc with epitope tags and expressed epitope-tagged full-length mouse Rnf207 with the BAC-to-BAC system (Clontech Laboratories, Mountain View, CA). Baculovirus infections, culture and affinity purifications were performed as described previously [29] . In vitro binding assays were performed as described previously [30] 2.9. Antibodies
We used anti-FLAG M2 antibodies (Sigma), anti-HA antibodies (Covance, Princeton, NJ), anti-VDAC1 antibodies (ab14734, Abcam, Cambridge, UK), anti-GST (B-14, Santa Cruz Biotechnology, Santa Cruz, CA), anti-PARP, anti-GAPDH (Cell Signaling Technology [CST], Danvers, MA) and anti-HSP90 (BD Transduction Laboratories, San Diego, CA).

Mizushima W., Takahashi H., Watanabe M., Kinugawa S., Matsushima S., Takada S., Yokota T., Furihata T., Matsumoto J., Tsuda M., Chiba I., Nagashima S., Yanagi S., Matsumoto M., Nakayama K.I., Tsutsui H, & Hatakeyama S. (2016). The novel heart-specific RING finger protein 207 is involved in energy metabolism in cardiomyocytes. Journal of molecular and cellular cardiology, 100.

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Western Blot Analysis of Cell Lysates

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Protein lysates from culture cells were harvested with RIPA buffer including proteinase and phosphatase inhibitors. Proteins were separated on 4-12% NuPage Bis-Tris gels (Life Technologies, NP0321), transferred to nitrocellulose membrane, and probed with antibodies. Blots were imaged using an Odyssey system (LICOR). The following antibodies and dilutions were used: 1:1000 anti-Hmga2 (Biocheck); 1:1000 anti-Sox9 (Millipore); 1:10,000 anti-Hsp90 (BD Biosciences); 1:1000 anti-Ck19 (Troma); 1:1000 anti-pErk (Cell Signaling).

Song C.Q., Li Y., Mou H., Moore J., Park A., Pomyen Y., Hough S., Kennedy Z., Fischer A., Yin H., Anderson D.G., Conte D J.r., Zender L., Wang X.W., Thorgeirsson S., Weng Z, & Xue W. (2016). Genome-wide CRISPR Screen Identifies Regulators of MAPK as Suppressors of Liver Tumors in Mice. Gastroenterology, 152(5), 1161-1173.e1.

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Comprehensive Protein Expression Analysis Using Western Blotting

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Western blot analysis was performed using the following antibodies: anti-eIF3a (Novus NBP1-18891); anti-eIF3b (Bethyl A301-761A); anti-eIF3c (Bethyl A300-376A); anti-eIF3d (Bethyl A301-758A); anti-eIF3e (Bethyl A302-985A); anti-eIF3f (Bethyl A303-005A); anti-eIF3g antibody (Bethyl A301-757A); anti-eIF3h antibody (Bethyl A301-754A); anti-eIF3i (Biolegend 646701); anti-eIF3k (Novus NB100-93304); anti-eIF3l antibody (Genetex GTX120119); anti-eIF3m (Novus NBP1-56654); anti-rpS19 (Bethyl A304-002A); anti-eIF4G1 (Bethyl A301-775A); anti-c-Jun (Bethyl A302-959A); anti-BTG1 (Abcam ab151740). anti-GAPDH (Bethyl A300-640A); anti-HSP90 (BD 610418).

Lee A.S., Kranzusch P.J, & Cate J.H. (2015). eIF3 targets cell proliferation mRNAs for translational activation or repression. Nature, 522(7554), 111-114.

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Western Blot Analysis of Cell Signaling Proteins

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Whole-cell extracts were prepared from cells using RIPA lysis buffer. Western blotting analysis was performed using anti-RIPK1 (BD Biosciences, San Jose, CA, USA), RIPK3, p21 (Santa Cruz), cIAP1/2 (R&D Systems, Minneapolis, MN, USA), PARP-1 (BD Biosciences) and cleaved PARP-1 (Cell Signaling Technology, Danvers, MA, USA) antibodies. Anti-HSP90 (BD Biosciences) and β-actin (Prosci, Poway, CA, USA) antibodies were used as a loading control.

Moriwaki K., Bertin J., Gough P.J., Orlowski G.M, & Chan F.K. (2015). Differential roles of RIPK1 and RIPK3 in TNF-induced necroptosis and chemotherapeutic agent-induced cell death. Cell Death & Disease, 6(2), e1636-.

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