Sds running buffer

Manufactured by Bio-Rad

Sourced in United States

SDS running buffer is a solution used in SDS-PAGE (Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis) to separate proteins based on their molecular weight. It provides the necessary ionic environment for the electrophoretic separation of proteins.

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Lab products found in correlation

Tris glycine gel, by Bio-Rad (3 mentions) Nativepagetm running buffer, by Thermo Fisher Scientific (2 mentions) Transfer buffer, by Bio-Rad (2 mentions) Pvdf membrane, by GE Healthcare (2 mentions) Hrp detection kit, by Thomas Scientific (2 mentions) Coomassie brilliant blue r 250, by Bio-Rad (2 mentions) Nitrocellulose membrane, by Thermo Fisher Scientific (2 mentions) Iblot system, by Thermo Fisher Scientific (2 mentions) Any kd mini protean tgx gel, by Bio-Rad (2 mentions) 300 μl laemmli buffer, by Bio-Rad (2 mentions) Image lab software, by Bio-Rad (2 mentions) Chemidoc xrs system, by Bio-Rad (2 mentions) Nupage bis tris gel, by Thermo Fisher Scientific (1 mentions) Sheep anti mouse hrp, by GE Healthcare (1 mentions) Anti β actin antibody, by Merck Group (1 mentions) Gentlemacs m tube, by Miltenyi Biotec (1 mentions) Nativepage running buffer, by Thermo Fisher Scientific (1 mentions) Nupage 4 to 12 bis tris gel, by Thermo Fisher Scientific (1 mentions) Anti hmgb1 antibody, by Abcam (1 mentions) Goat anti rabbit hrp, by Merck Group (1 mentions)

8 protocols using sds running buffer

Electrophoretic Analysis of HCV Antigens

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HCV antigens were analyzed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS PAGE) and BN PAGE and stained using Coomassie blue. The protein samples were mixed with loading dye and loaded onto a 4–12% Bis-Tris NuPAGE gel (Life Technologies) or a 10% Tris-Glycine Gel (Bio-Rad). The SDS PAGE gels were run for 20 min at 250 V using the SDS running buffer (Bio-Rad). BN PAGE gels were run for 1.5 h at 200 V using NativePAGE^TM running buffer (Life Technologies) according to the manufacturer’s instructions.

He L., Cheng Y., Kong L., Azadnia P., Giang E., Kim J., Wood M.R., Wilson I.A., Law M, & Zhu J. (2015). Approaching rational epitope vaccine design for hepatitis C virus with meta-server and multivalent scaffolding. Scientific Reports, 5, 12501.

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Jurkat Cell Signaling Pathway Analysis

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2×10⁶ Jurkat cells were left untreated or incubated at 37°C for 30 minutes with 20ug/ml CD80-Fc or anti-CD28 mAb. Cells were harvested, resuspended in M-PER Mammalian Protein Extraction Reagent with Halt Protease and Phosphatase Inhibitor Cocktail (ThermoFisher Scientific), and lysed in gentleMACS M tubes (Miltenyi Biotec) using program Protein_01according to the manufacturer’s recommendation. Protein concentration was assed via Bradford Assay, and protein was electrophoresed on 15% SDS-PAGE gels in SDS running buffer (BioRad) at 100 volts for 90 minutes, and transferred overnight in transfer buffer (BioRad) at 30 volts to PVDF membranes (GE Healthcare). Membranes were blocked with 5% milk in TBST. pNF-κB and pMAPK were detected with anti-pNF-KB antibody (clone 93H1; 1:1000 in 10ml of 2.5% milk/TBST) or anti-pMAPK antibody (clone D13.14.4E; 1:2000 in 10ml of 2.5% milk/TBST) (both from Cell Signaling) followed by goat-anti-rabbit-HRP (Biolegend; 1:10000 in 10ml of 2.5% milk/TBST). Beta-actin was detected with anti-β-actin antibody (Sigma-Aldrich; clone AC-15, ascites fluid; 1:10000 in 10ml of 2.5% milk/TBST) followed by sheep-anti-mouse-HRP (GE Healthcare Life Sciences). Protein was visualized using an HRP detection kit (Denville Scientific, Inc).

Horn L.A., Long T.M., Atkinson R., Clements V, & Ostrand-Rosenberg S. (2017). Soluble CD80 protein delays tumor growth and promotes tumor infiltrating lymphocytes. Cancer immunology research, 6(1), 59-68.

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Characterizing Designed Antigens by SDS-PAGE and BN-PAGE

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Designed antigens were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and blue native-polyacrylamide gel electrophoresis (BN-PAGE). The protein samples were mixed with loading dye and added to either a 10% Tris-glycine gel (Bio-Rad) or a 4 to 12% bis-Tris NuPAGE gel (Life Technologies, Inc.). For SDS-PAGE under reducing conditions, the antigen samples were first treated with dithiothreitol (DTT) (25 mM) and boiled for 5 min at 100°C. SDS-PAGE gels were run for 20 min at 250 V using SDS running buffer (Bio-Rad), while BN-PAGE gels were run for 2.5 h at 150 V using native PAGE running buffer (Life Technologies, Inc.) according to the manufacturer’s instructions. The gels were stained using Coomassie brilliant blue R-250 (Bio-Rad) and destained using a solution of 6% ethanol and 3% glacial acetic acid.

Morris C.D., Azadnia P., de Val N., Vora N., Honda A., Giang E., Saye-Francisco K., Cheng Y., Lin X., Mann C.J., Tang J., Sok D., Burton D.R., Law M., Ward A.B., He L, & Zhu J. (2017). Differential Antibody Responses to Conserved HIV-1 Neutralizing Epitopes in the Context of Multivalent Scaffolds and Native-Like gp140 Trimers. mBio, 8(1), e00036-17.

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HMGB1 Protein Detection and Quantification

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50 μl of equivalent quantities of concentrated supernatants of cultured tumor cells, in vivo grown tumors, MDSC, macrophages, or 60ug of MEF cell lysates were mixed with 10 μl or the appropriate amount of 6x sample buffer and electrophoresed on 12% SDS-PAGE gels in SDS running buffer (BioRad) at 150 volts for 1 hour, and transferred overnight in transfer buffer (BioRad) at 30 volts to PVDF membranes (GE Healthcare). Membranes were blocked with 5% milk in TBST. HMGB1 was detected with anti-HMGB1 antibody (Epitomics) (5ng/ml in 10ml of 2.5% milk/TBST) followed by goat-anti-rabbit-HRP (Millipore) (40ng/ml in 10ml of 2.5% milk/TBST). Protein was visualized using an HRP detection kit (Denville Scientific, Inc). HMGB1 levels were measured by ELISA according to the manufacturer's directions (IBL International, Hamburg, Germany).

Parker K., Sinha P., Horn L.A., Clements V.K., Yang H., Li J., Tracey K.J, & Ostrand-Rosenberg S. (2014). HMGB1 enhances immune suppression by facilitating the differentiation and suppressive activity of myeloid-derived suppressor cells. Cancer research, 74(20), 5723-5733.

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BG505 Env-NPs Structural Analysis

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BG505 Env-NPs were analyzed by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) and blue native-polyacrylamide gel electrophoresis (BN-PAGE). The proteins were mixed with loading dye and added to either a 10% Tris-Glycine Gel (Bio-Rad) or a 4–12% Bis-Tris NativePAGE^TM gel (Life Technologies). For SDS-PAGE under reducing conditions, the proteins were first treated with dithiothreitol (DTT, 25 mM) and boiled for 5 min at 100 °C. SDS-PAGE gels were run for 20 min at 250 V using SDS running buffer (Bio-Rad), and BN-PAGE gels were run for 2–2.5 h at 150 V using NativePAGE^TM running buffer (Life Technologies) according to the manufacturer’s instructions. The gels were stained using Coomassie Brilliant Blue R-250 (Bio-Rad) and de-stained using a solution of 6% ethanol and 3% glacial acetic acid.

Zhang Y.N., Paynter J., Antanasijevic A., Allen J.D., Eldad M., Lee Y.Z., Copps J., Newby M.L., He L., Chavez D., Frost P., Goodroe A., Dutton J., Lanford R., Chen C., Wilson I.A., Crispin M., Ward A.B, & Zhu J. (2023). Single-component multilayered self-assembling protein nanoparticles presenting glycan-trimmed uncleaved prefusion optimized envelope trimers as HIV-1 vaccine candidates. Nature Communications, 14, 1985.

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Whole-Cell Protein Extraction from hESC-Derived Cells

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To extract whole-cell protein from hESC-derived cells, cells were washed with ice-cold PBS and lysed with 300 μL Laemmli buffer (Bio-Rad Laboratories) for 10 min on ice. The cells were then sonicated (three times for 15 s each) and the homogenate centrifuged at 1,000 relative centrifugal force for 10 min at 4°C and heated at 95°C for 5 min. Equal amounts of supernatant were run on Any kD Mini-PROTEAN TGX gel (Bio-Rad Laboratories) at 100 V for 1 h in SDS running buffer (Bio-Rad Laboratories). Proteins were then transferred to a nitrocellulose membrane (Invitrogen) using the iBlot system (Invitrogen) for 5 min. The membrane was blocked in Tris-buffered saline containing 0.05% Tween and 5% low-fat dried milk for 90 min at 4°C. The membrane was then probed with the primary antibody overnight at 4°C, washed twice with Tris-buffered saline containing 0.05% Tween, and incubated with the corresponding secondary antibody for 1 h at room temperature. Chemiluminescence detection was performed following Amersham ECL (RPN2235; Cytiva) exposure using the ChemiDoc XRS+ System and Image Lab Software (Bio-Rad Laboratories). Details on the antibodies used are given in Supplementary Table 3.

Montaser H., Patel K.A., Balboa D., Ibrahim H., Lithovius V., Näätänen A., Chandra V., Demir K., Acar S., Ben-Omran T., Colclough K., Locke J.M., Wakeling M., Lindahl M., Hattersley A.T., Saarimäki-Vire J, & Otonkoski T. (2021). Loss of MANF Causes Childhood-Onset Syndromic Diabetes Due to Increased Endoplasmic Reticulum Stress. Diabetes, 70(4), 1006-1018.

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Whole Cell Protein Extraction from hESC-Derived Cells

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To extract whole cell protein from hESC-derived cells, cells were washed with ice-cold PBS and lysed with 300 μL Laemmli buffer (Bio-Rad) for 10 min on ice. The cells were then sonicated (3 x 15 s) and the homogenate centrifuged at 1000 rcf for 10 min at 4°C, heated at 95°C for 5 min. Equal amounts of supernatant were run on Any kD Mini-PROTEAN TGX gel (Bio-Rad, Hercules, CA, USA) at 100 V for 1 h in SDS running buffer (Bio-Rad). Proteins were then transferred to a nitrocellulose membrane (Invitrogen) using iBlot system (Invitrogen) for 5 min. The membrane was blocked in Tris-buffered saline containing 0.05% Tween (TBS-T) and 5% low fat dried milk for 90 min at 4°C. The membrane was then probed the primary antibody overnight at 4°C, washed twice with TBS-T, and incubated with the corresponding secondary antibody for 1 h at room temperature. Chemiluminescence detection was performed following Amersham ECL (Cytiva, RPN2235) exposure using Chemidoc XRS+ system and Image Lab Software (BioRad). Details of the used antibodies are listed in supplementary table 2.

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CD13 Expression in HT-1080 Tumor Cells and Xenograft

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CD13 expression in HT-1080 tumor cells and the HT-1080 xenograft tumor was determined by Western blot. The tumor was homogenized using a manual pestle homogenizer (Duran, Wertheim, Germany). The homogenates were centrifuged (10,000 rpm, 10 min), and the supernatant was collected. Protein was determined in the tumor homogenates and cell lysates in the Bradford assay. Tumor and tumor cell lysates (50 µg protein) were subjected to electrophoresis in 7.5% polyacrylamide gel (PAGE) (Bio-Rad, Hercules, CA, USA) in SDS running buffer (Bio-Rad, USA). After electrophoresis, the proteins were transferred to nitrocellulose membranes and blotted with the primary antibody to rabbit mAb CD13/APN (D6V1W) (Cell Signaling, Danvers, MA, USA). Then, they were washed and stained with a secondary anti-rabbit antibody (Amersham, Little Chalfont, UK). The bands were developed in an ECL detection system (Bio-Rad, USA) and imaged using a ChemiDoc system (Bio-Rad, USA).

Tereshkina Y.A., Kostryukova L.V., Tikhonova E.G., Khudoklinova Y.Y., Orlova N.A., Gisina A.M., Morozevich G.E., Melnikov P.A, & Pokrovsky V.S. (2022). Chlorin e6 Phospholipid Delivery System Featuring APN/CD13 Targeting Peptides: Cell Death Pathways, Cell Localization, In Vivo Biodistribution. Pharmaceutics, 14(10), 2224.

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