Ripa buffer

Name: Ripa buffer
Brand: Thermo Fisher Scientific
SKU: h5oPdZQB1-hLfrUPlUX7
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7 158 citations

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RIPA buffer is a commonly used lysis buffer for the extraction and solubilization of proteins from cells and tissues. It contains a mixture of ionic and non-ionic detergents that help disrupt cell membranes and release cellular contents, including proteins. The buffer also includes salts and buffers to maintain the pH and ionic strength of the solution.

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The RIPA Lysis and Extraction Buffer is commercially available from Thermo Fisher Scientific and can be purchased through authorized distributors. Pricing typically ranges from $115.65 to $242.65, depending on the volume purchased.

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7 158 protocols using «ripa buffer»

Western Blot Analysis of Heme Oxygenase

2025

Protein lysates were prepared using freshly made lysis buffer consisting of 98 % RIPA buffer (Fisher Scientific, Waltham, MA, USA, Cat# PI87787), 1 % protease and phosphatase inhibitor (Fisher Scientific, Waltham, MA, USA, Cat# PI78441), and 1 % EDTA. Protein quantification was performed with a DC Protein Assay Kit (Bio-Rad, Hercules, CA, USA, Cat# 5,000,111) following the manufacturer's protocol and measured using a BioTek Synergy plate reader. Protein lysates (30 μg) were electrophoresed on a 12 % Bis-Tris Gel (BioRad, Hercules, CA, USA, Cat# 4,561,044) at 100 V and transferred to Immobilon-P PVDF membranes (Fisher Scientific, Waltham, MA, USA, Cat# IPVH00010). The membranes were blocked with EveryBlot Blocking buffer (BioRad, Hercules, CA, USA, Cat# 12,010,020). Primary antibodies, including HO-1 pAb (Enzo Life Sciences, Farmingdale, NY, USA, Cat# BML-HC3001–0100, RRID: AB_11,177,779), HO-2 mAb (Cell Signaling Technology, MA, USA, Cat# 32,790, RRID:AB_2,799,030), β- Actin (13E5) rabbit mAb (Cell Signaling Technology, MA, USA, Cat# 4970, RRID:AB_2,223,172), and GAPDH (6C5) (Santa Cruz Biotechnology Dallas, TX, USA, Cat# 32,233, RRID: AB_627,679), were diluted 1:1000 in a 1:1 mixture of EveryBlot blocking buffer and 1 % TBST and incubated overnight at 4 °C. Secondary antibodies, goat anti-rabbit IgG polyclonal (Enzo Life Sciences, Farmingdale, NY, USA, Cat# SAB-300 J, RRID:AB_1,505,668) or mouse IgG HRP-linked (Cell Signaling Technology, MA, USA, Cat# 7076S, RRID:AB_330,924), were diluted 1:3000 in a 1:1 solution of EveryBlot blocking buffer and 1 % TBST, and incubated for 1 hour at room temperature with agitation. Blots were developed using Azure Biosystems Radiance Plus (VWR, Radnor, PA, USA, Cat# 10,147–298) and Azure c600. β-Actin and GAPDH were used as housekeeping genes. Densitometry analysis of western blot bands was performed using ImageJ software.

Salloom R.J., Sahtout D.Z., Ahmad I.M, & Abdalla M.Y. (2025). Synergistic effects of HO-1 inhibition and chemotherapy on tumor proliferation and immune infiltration: An in vitro and in vivo approach to enhancing prostate cancer treatment. Translational Oncology, 54, 102339.

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Western Blot Analysis of Immune Checkpoint Proteins

2025

T cells were lysed in the RIPA buffer (Thermal Fisher) with protease inhibitor cocktail (Sigma Aldrich). The protein concentration of the lysates was quantified by the Bradford protein assay kit (Bio-Rad). Equal amounts of protein (20 μg) were electrophoresed in 12% sodium dodecyl sulfate-polyacrylamide gel and transferred to polyvinyldifluoride membranes (Millipore). The membranes were blocked for 1 h with 5% non-fat milk, and incubated with primary Abs (TGFBR1, ab235578, Abcam; TGFBR2, ab269279, Abcam; PD-1, AF1021, R&D; ACTIN, 8H10D10, Cell Signaling) diluted by 1:1,000 in 5% non-fat milk at 4 °C overnight. For NFATC1, the membrane was blocked for 1 h with 5% BSA and incubated with primary Ab (NFAT2, #8032, Cell Signaling) diluted by 1:1000 in 5% BSA. After washing, membranes were incubated with the corresponding horseradish peroxidase-conjugated secondary Ab diluted by 1:2000 in 5% non-fat milk. The immune complexes were visualized using SuperSignal™ West Femto Maximum Sensitivity Substrate detection kit according to the manufacturer’s instructions (ThermoFisher). When necessary, membranes were stripped by stripping buffer (Bioland Scientific) for 10 min at room temperature, and re-probed with Abs.

Chen F., Zhao D., Xu Y., Zhang Y., Chen M.H., Pathak K.V., Hansen N., Lovell B., Liang Y., Estrella K., Wang W.L., Ghoda L., Rockne R., Wu X., Ali H., Yu J., Caligiuri M.A., Forman S.J., Trent J.M., Kuo Y.H., Li L., Swiderski P., Zhang J., Kortylewski M., Nguyen L.X., Pirrotte P., Boldin M., Marcucci G, & Zhang B. (2025). miR-142 deficit in T cells during blast crisis promotes chronic myeloid leukemia immune escape. Nature Communications, 16, 1253.

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Protein Extraction and Western Blot

2025

We used RIPA buffer (ThermoFisher Scientific, 89900), supplemented with orthovanadate (New England Biolabs, P0758L) and protease inhibitor cocktail (Sigma-Aldrich, P8340). Protein concentrations were determined using Pierce 660 nm Protein Assay Reagent (ThermoFisher Scientific, 22660). Lysates were diluted in 4x Laemmle buffer (Bio-Rad, 1610747) and β-mercaptoethanol (ThermoFisher Scientific, 21985023), then boiled for 5 min at 95 °C. Samples were subjected to gel electrophoresis in 4–20% Criterion TGX Stain-Free Protein gels (BioRad, 5678095), before being transferred onto PVDF or nitrocellulose membranes using BioRad Transblot Turbr semi-dry transfer system. Gels were then blocked using Blotting grade blocker (Bio-Rad, 170-6404). The following antibodies were used in this study: SARS-CoV-2 nucleocapsid (Abcam, ab271180—1:1000 dilution), β-actin (Abcam, ab8224—1:1000 dilution), GAPDH (Cell signaling technology, 5174S—1:1000 dilution). FABP4 was detected using an in-house antibody produced for the Hotamisligil laboratory by the Dana Farber Antibody Core (HRP-tagged clone 351.4.5E1.H3—1:1000 dilution). This FABP4 antibody was validated using with protein lysates from FABP4-knockout mice as negative controls and recombinant FABP4 as positive control.

Baazim H., Koyuncu E., Tuncman G., Burak M.F., Merkel L., Bahour N., Karabulut E.S., Lee G.Y., Hanifehnezhad A., Karagoz Z.F., Földes K., Engin I., Erman A.G., Oztop S., Filazi N., Gul B., Ceylan A., Cinar O.O., Can F., Kim H., Al-Hakeem A., Li H., Semerci F., Lin X., Yilmaz E., Ergonul O., Ozkul A, & Hotamisligil G.S. (2025). FABP4 as a therapeutic host target controlling SARS-CoV-2 infection. EMBO Molecular Medicine, 17(3), 414-440.

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Immunoblotting analysis of HCMV protein expression

2025

HF cells were infected with TB40E WT, TB40E Δ1.2, and TB40E Δ1.2 half (MOI = 1). After 24 hpi and 72 hpi, cells were washed with 1X PBS and lysed using RIPA buffer (Thermo Scientific USA, 89901) with protease inhibitor cocktail (Sigma USA, P8340). Cells were scraped and harvested. Samples were then sheared using a probe sonicator at 30 amplitudes for a total of 30 s: 10 s on and 10 s off. Cellular debris was then centrifuged at 13,000 RPM for 10 min at 4 °C. Protein was denatured using Laemmli Buffer (Bio-Rad) with β-mercaptoethanol and boiled at 95 °C for 5 min. The protein was then resolved by SDS-PAGE and transferred to a PVDF membrane (Bio-Rad) for immunoblotting analysis. The membrane was blocked in 5% BSA in Tris-buffered saline, 0.05% Tween-20 (1X TBST) for 30 min. The membrane containing samples from 24 hpi was then probed with antibodies to detect IE1/IE2 1:1000 (Virusys, P1215) and H3 1:5000 (Abcam USA, ab1791). Membrane with samples from 72 hpi was probed with antibodies to detect UL44 1:1000 (Fitzgerald, 10-C50I), pp65 1:150 (Abcam, ab49214), and H3. Protein was detected by incubation with secondary antibody using IRDye 680 anti-mouse Ab 1:10,000 (LI-COR USA, #926-68070) and IRDye 800 anti-rabbit Ab 1:10,000 (LI-COR, #926-32211).

Manska S., Hagemann A., Magana J., Rossetto C.C, & Verma S.C. (2025). Characterization of Human Cytomegalovirus (HCMV) Long Non-Coding RNA1.2 During Lytic Replication. Viruses, 17(2), 149.

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Protein Analysis by Western Blotting

2025

Cell lysis and protein extraction were performed using RIPA buffer (Thermo Fisher Scientific Inc., Tokyo, Japan). Samples were separated by SDS-PAGE and transferred onto a PVDF membrane. After blocking with 5% nonfat dry milk (Cell Signaling Technology, Tokyo, Japan) or 2% bovine serum albumin (Nacalai Tesque, Inc., Tokyo, Japan) in Tween-PBS, each membrane was incubated with the following primary antibodies: anti-GAPDH; 1:10,000; ab181602; Abcam, Cambridge, United Kingdom, anti-DCN; 1:1000; sc-73896; Santa Cruz Biotechnology, Inc., Heidelberg, Germany, anti-BGN; 1:1000; sc-100857; Santa Cruz Biotechnology, Inc., anti-TGFβ1; 1:1000; sc-130348; Santa Cruz Biotechnology, Inc., anti-vinculin; 1:10,000; ab129002; Abcam, or anti-RhoA; 1:5000; #2117; Cell Signaling Technology, Inc. for 12 h at 4 °C. The membrane was then incubated with anti-rabbit IgG horseradish peroxidase-linked whole antibody (from donkey) (1:10,000, NA934V; GE Healthcare, Tokyo, Japan) or anti-mouse IgG HRP peroxidase-linked whole antibody (1:10,000, NXA931V, GE Healthcare), as the secondary antibody for 1 h at room temperature. Antibody reactions were detected using ECL™ Prime Western Blotting Reagent (GE Healthcare) or ECL Select Western Blotting Reagent (GE Healthcare) and a LuminoGraph I system (ATTO Corp., Tokyo, Japan).

Kamio H., Okabe K., Honda M., Kuroda K, & Tsuchiya S. (2025). Knockdown of decorin in human bone marrow mesenchymal stem cells suppresses proteoglycan layer formation and establishes a pro-inflammatory environment on titanium oxide surfaces. Journal of Materials Science. Materials in Medicine, 36(1), 5.

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Top 5 most cited protocols using «ripa buffer»

Immunoblotting for Protein Analysis

Cited 7 times

Cells were washed three times with phosphate-buffered saline (PBS), scraped from the culture dishes, and solubilized in RIPA buffer (Thermo Scientific, Lafayette, CO, USA) with 10 μM protein inhibitors (Thermo). The samples were then centrifuged at 20,000 g for 15 min, and the supernatants were collected. Protein determination was performed using the BCA assay kit (Pierce, Rockford, IL, USA). Samples were loaded on 4–20% gradient polyacrylamide gel (Bio-Rad) and transferred to PVDF membranes. After blocking in 10 mM Tris-HCl pH 7.4 and 150 mM NaCl (TBS) containing 5% non-fat milk, membranes were incubated with primary antibodies overnight at 4 °C. Primary antibodies for GH (1:500, R&D), PLZF (1:200, Santa Cruz Biotechnology, Santa Cruz, CA, USA), Atp6l (1:500, Abcam, Cambridge, MA, USA) and β-actin (1:1000, Santa Cruz Biotechnology) were used for the study. Polyclonal rabbit anti-human PRR (1:1000, ProteinExpress, Chiba, Japan), which recognizes extracellular domains, has been previously described8 (link). After extensive washing, the membrane was incubated with peroxidase secondary antibody for 1 h at room temperature, and the complexes were detected using an enhanced chemiluminescence (ECLplus) system (GE Healthcare, Tokyo, Japan). The signals of each blot were visualized and quantitatively analyzed by ImageQuant LAS 4000 (GE Healthcare).

Tani Y., Yamada S., Inoshita N., Hirata Y, & Shichiri M. (2015). Regulation of growth hormone secretion by (pro)renin receptor. Scientific Reports, 5, 10878.

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Corresponding organizations : Kitasato University, Toranomon Hospital, Foundation for Biomedical Research and Innovation

Prostate Cancer Cell Protein Expression

Cited 5 times

LNCaP and PC3 human prostate cancer cells (ATCC, Manassas, VA) were grown to 50% confluency and transfected with either microRNA precursor or antisense microRNA inhibitor (Ambion, Austin, TX) at 100 nM final concentration using Lipofectamine 2000 reagent (Invitrogen). After 48 hours, cells were harvested by scraping and protein was extracted with RIPA buffer (Pierce Biotechnology, Rockford, IL). The following primary antibodies were for used to visualize protein expression by Western blot analysis: polyclonal rabbit anti-exportin-6 antibody, 1:200 (ProteinTech Group, Chicago, IL: 11408-1-AP); monoclonal mouse anti-PTK9 antibody, 1:500 (Abnova Corp., Taipei, Taiwan: clone 1E2); monoclonal mouse anti-E2F1 antibody, 1:200 (Santa Cruz Biotechnology, Santa Cruz, CA: sc-251); monoclonal mouse anti-p21/WAF1 antibody, 1:200 (Santa Cruz Biotechnology: sc-6246); and polyclonal rabbit anti-BIM antibody, 1:1000 (Cell Signaling/Santa Cruz Biotechnology: #2819). A quantification of protein expression was obtained with the AIDA Biopackage, 2D–Densitometry (raytest Isotopenmessgeraete GmbH, Straubenhardt, Germany).

Ambs S., Prueitt R.L., Yi M., Hudson R.S., Howe T.M., Petrocca F., Wallace T.A., Liu C.G., Volinia S., Calin G.A., Yfantis H.G., Stephens R.M, & Croce C.M. (2008). Genomic profiling of microRNA and mRNA reveals deregulated microRNA expression in prostate cancer. Cancer research, 68(15), 6162-6170.

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Corresponding organizations : National Cancer Institute, Center for Cancer Research, The Ohio State University, The University of Texas MD Anderson Cancer Center, Veterans Health Administration

Protein Extraction and Western Blot Analysis

Cited 5 times

Cells were harvested with a radioimmunoprecipitation assay (RIPA) buffer (Thermo Fisher Scientific Inc.) solution with 3.0 g/L protease inhibitor cocktail (Roche Applied Science) solution. Protein concentrations were assessed by the BCA assay kit, using BSA as a standard. Lysates (15 μg protein/lane) were mixed with sodium dodecyl sulfate (SDS) sample buffer (Bio-Rad) and 2-mercaptoethanol (Sigma-Aldrich) and heated at 95 °C for 5 min. They were separated by SDS polyacrylamide gel electrophoresis (SDS-PAGE) with 40-150 g/L gradient polyacrylamide gels (Bio-Rad). Proteins were transferred onto PVDF membranes using the semidry electron transfer system (ATTO Co., Ltd., Tokyo, Japan). The membranes were incubated in 50 g/L SM-PBS-T at room temperature for 30 min (blocking step). Proteins on PVDF membranes were probed with the following primary antibodies at 4 °C overnight: anti-GA-AGE antibody (1:1000), neutralized anti-GA-AGE antibody (1:1000), rabbit monoclonal [ERP3953] anti-HSP90α antibody (Abcam, Cambridge, United Kingdom; 1:2000; ab109248), rabbit polyclonal anti-HSP70 antibody (Abcam; 1:8000; ab94368), rabbit polyclonal anti-HSP27 antibody (Abcam 1:1000; ab1428), rabbit polyclonal anti-cleaved caspase-3 (Asp175) antibody (Cell Signaling Technology Japan K.K.; 1:1000; #9661), and mouse monoclonal [6C5] anti-GA-3 phosphate dehydrogenase (anti-GAPDH) antibody (Abcam; 1:10000; ab8245). PVDF membranes were washed four times with 5.0 g/L SM-PBS-T and incubated with secondary antibody at room temperature for 1 h. The secondary antibodies were the following: HRP-conjugated goat anti-rabbit IgG antibody (Dako; 1:2000; REF0448), which was used to analyze GA-AGEs, HRP-conjugated goat anti-mouse IgG antibody (Thermo Fisher Scientific Inc.; 1:5000; Product Number 31458), and HRP-conjugated donkey anti-rabbit IgG antibody (Thermo Fisher Scientific Inc.; 1:2000; Product Number 31432). Band densities were measured as well as SB. When the detection of HSP90β was performed, proteins on PVDF membranes were probed with a mouse monoclonal [5G4] anti-HSP90β antibody (Abcam; 1:20000; ab119833) and incubated at room temperature for 2 h. Then, proteins on PVDF were incubated in the secondary antibody at room temperature for 1 h. The anti-GAPDH antibody was used after the target antibody was removed by the Western re-probe kit.

Takata T., Ueda T., Sakasai-Sakai A, & Takeuchi M. (2017). Generation of glyceraldehyde-derived advanced glycation end-products in pancreatic cancer cells and the potential of tumor promotion. World Journal of Gastroenterology, 23(27), 4910-4919.

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Corresponding organizations : Kanazawa Medical University

Quantifying Stem Cell Lineage Markers

Cited 4 times

To investigate protein levels related to osteogenic, chondrogenic, and adipogenic differentiation or to autophagy in in vitro experiments, we performed Western blot analyses. Protein extraction was performed using RIPA buffer (Thermo Fisher Scientific, Waltham, MA, USA) according to the manufacturer's protocol. A BCA assay (Thermo Fisher Scientific, Waltham, MA, USA) was used to determine protein concentrations. Protein samples were diluted in 4x Laemmli's sample buffer (Bio-Rad, CA, US), heated for 5 min at 95°C, and separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS PAGE), using a mini-PROTEAN® TGX™ Precast gradient 4-20% gel (Bio-Rad, CA, US), followed by transfer onto polyvinylidene difluoride (PVDF) membranes (Thermo Fisher Scientific, Waltham, MA, USA). PVDF membranes were probed with the primary and secondary antibodies reported in Table 1. Signals were detected using a chemiluminescence reagent (ECL, Millipore, Burlington, MA, USA) according to the manufacturer's instructions. Images were acquired by a LAS4000 Digital Image Scanning System (GE Healthcare, Little Chalfont, UK). Densitometric analysis was performed by using ImageQuant software (GE Healthcare, Little Chalfont, UK), and the relative protein band intensity was normalized to β-actin.

Dalle Carbonare L., Mottes M., Cheri S., Deiana M., Zamboni F., Gabbiani D., Schena F., Salvagno G.L., Lippi G, & Valenti M.T. (2019). Increased Gene Expression of RUNX2 and SOX9 in Mesenchymal Circulating Progenitors Is Associated with Autophagy during Physical Activity. Oxidative Medicine and Cellular Longevity, 2019, 8426259.

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Corresponding organizations : University of Verona

Cardiac Fibroblast Isolation and Characterization

Cited 4 times

Cultured MEFs were fixed in 4% paraformaldehyde and stained with αSMA antibody (1:1000, mouse monoclonal, Clone 1A4, Sigma) to detect actin stress fibers and 4′,6-diamidino-2-phenylindole (DAPI, 1:1000, Invitrogen) to visualize the nucleus. Alexa 488 or Alexa 568 conjugated secondary antibody directed against mouse IgG was used to detect αSMA. In cardiac tissue sections myofibroblasts were identified in infarcted hearts 28 days after injury and in MKK6-Tg mice 4 months after tamoxifen induction. Hearts were dissected, fixed overnight in 10% formalin, and paraffin embedded. Five micron sections were subjected to antigen retrieval and subsequently stained with the combination of αSMA antibody and isolectin-B4 (Vector Biolabs) for endothelial cell identification, or for vimentin (1:250, rabbit monoclonal, Abcam).
For Western blotting of purified cardiac fibroblasts isolated from genetically modified hearts, a Langendorff apparatus was used to perfuse the heart with type II collagenase (2mg/ml) and liberase blendzyme (0.4mg/ml) in Krebs-Henseleit buffer. Hearts were processed and cells collected and prepared for flow cytometry as described previously ^{29 (link)}. Cells were incubated for 1 hour with the fibroblast allophycocyanin (APC)-conjugated antibody MEFSK4 (1:10, Miltenyi Biotec), washed 3 times in blocking buffer, and incubated with 4′,6-diamidino-2-phenylindole (DAPI) to identify live cells. The isolated fibroblast fraction was lysed in RIPA buffer (Thermo Fisher Scientific) and prepared in Laemmli buffer (Sigma Aldrich) for SDS-PAGE gel and western blot. For each group, protein extract from 125,000 fibroblasts were loaded per lane and the following antibodies used: total p38α (1:1000, rabbit polyclonal, Cell Signaling), phosphorylated p38 (1:1000, rabbit polyclonal, Cell Signaling), MKK6 (1:500, rabbit polyclonal, Genetex), phosphorylated MK2 (1:100, rabbit polyclonal, Cell Signaling), αSMA (1:1000, mouse monoclonal, Sigma), vimentin (1:1000, rabbit monoclonal, Abcam), and glyceraldehyde 3-phosphate dehydrogenase (GAPDH, 1:10,000, mouse monoclonal, Fitzgerald Industries).

Molkentin J.D., Bugg D., Ghearing N., Dorn L.E., Kim P., Sargent M.A., Gunaje J., Otsu K, & Davis J. (2017). Fibroblast-specific genetic manipulation of p38 MAPK in vivo reveals its central regulatory role in fibrosis. Circulation, 136(6), 549-561.

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Corresponding organizations : Howard Hughes Medical Institute, Cincinnati Children's Hospital Medical Center, University of Washington, University of Cincinnati, British Heart Foundation, King's College London

Spelling variants (same manufacturer)

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