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Nativepage bis tris gel

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NativePAGE Bis-Tris gels are electrophoresis gels designed for the separation and analysis of native, non-denatured protein complexes. They provide a gentle, non-denaturing environment to preserve the native structure and interactions of protein samples.

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Lab products found in correlation

Nativepage sample buffer, by Thermo Fisher Scientific (11 mentions) Nativepage running buffer, by Thermo Fisher Scientific (10 mentions) Nativemark unstained protein standard, by Thermo Fisher Scientific (5 mentions) Nativepage cathode buffer additive, by Thermo Fisher Scientific (3 mentions) Nativepage sample prep kit, by Thermo Fisher Scientific (3 mentions) Digitonin, by Thermo Fisher Scientific (3 mentions) Pvdf membrane, by Bio-Rad (3 mentions) Digitonin, by Merck Group (2 mentions) Nativepage transfer buffer, by Thermo Fisher Scientific (2 mentions) Coomassie g 250, by Thermo Fisher Scientific (2 mentions) Iblot system, by Thermo Fisher Scientific (2 mentions) Coomassie brilliant blue g 250, by Thermo Fisher Scientific (2 mentions) Trans blot sd, by Bio-Rad (2 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Sds running buffer, by Bio-Rad (1 mentions) Tris glycine gel, by Bio-Rad (1 mentions) Coomassie brilliant blue r 250, by Bio-Rad (1 mentions) Silver staining kit, by Bio-Rad (1 mentions) G 250 sample additive, by Thermo Fisher Scientific (1 mentions) Odyssey blocking buffer pbs, by LI COR (1 mentions)

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Bis-Tris gels (1248 citations) NativePAGE gels (23 citations) NativePAGE Novex 3–12% Bis-Tris Protein Gels (18 citations) NativePAGE 3-12% Bis-Tris Protein Gels (12 citations) NativePAGE 3 to 12% bis-Tris gels (2 citations) NativePAGE Novex Bis-Tris 3–12% gradient gels (2 citations) NativePAGE 4 to 16% Bis-Tris Mini Protein Gels (2 citations) NativePAGE Novex 3% to 12% Bis–Tris gels (2 citations) 4–16% NativePAGE Novex Bis-Tris Mini Gels (2 citations) NativePage Bis-Tris Protein Gels (2 citations)

54 protocols using nativepage bis tris gel

1

Native Gel Electrophoresis of Hsp60 and GroEL Proteins

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Native gel electrophoresis was performed using NativePAGE Bis-Tris Gels according to the manufacturer's instructions (Invitrogen, Carlsbad, CA, USA). Hsp60 and GroEL protein samples were diluted in NativePAGE Sample Buffer (1x) containing 1% digitonin and 0.5% n-dodecyl-β-D-maltoside (DDM) detergent solutions at pH 7.2. Samples and molecular weight marker (NativeMark Unstained Protein Standard-Invitrogen) were loaded on precasted 4–16% Novex NativePAGE Bis-Tris Gels that resolve proteins in the molecular weight range of 15–1,000 kDa. lectrophoresis was performed at 150 V constant voltage for 120 min, using XCell SureLock Mini-Cell (Invitrogen). Gels were stained by Coomassie G-250 staining. Gels were destained in 8% acetic acid until the desired background was obtained and scanned, using Gel Doc XR (Bio-Rad) molecular imager. Protein molecular weights were determined by the Quantity One software (Bio-Rad).
Vilasi S., Carrotta R., Mangione M.R., Campanella C., Librizzi F., Randazzo L., Martorana V., Marino Gammazza A., Ortore M.G., Vilasi A., Pocsfalvi G., Burgio G., Corona D., Palumbo Piccionello A., Zummo G., Bulone D., Conway de Macario E., Macario A.J., San Biagio P.L, & Cappello F. (2014). Human Hsp60 with Its Mitochondrial Import Signal Occurs in Solution as Heptamers and Tetradecamers Remarkably Stable over a Wide Range of Concentrations. PLoS ONE, 9(5), e97657.
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2

Native PAGE Analysis of MDA5 Oligomerization

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Native PAGE for analyzing endogenous IRF3 dimerization was performed as previously described59 (link). For measuring MDA5 oligomerization, HEK293T or HEK293 MDA5 KO cells were transfected with WT or mutant FLAG-MDA5–2CARD or FLAG-MDA5 as indicated. Twenty-four hours later, cells were lysed in 1× NativePAGE sample buffer (Invitrogen) containing 1% (v/v) NP-40 on ice for 30 min and then lysates were cleared by centrifugation at 16,000 ×g at 4°C for 10 min. Cleared lysates were resolved on a 3–12% Bis-Tris NativePAGE gel (Invitrogen) as per the manufacturer’s instructions and analyzed by immunoblotting with the indicated antibodies.
Liu G., Lee J.H., Parker Z.M., Acharya D., Chiang J.J., van Gent M., Riedl W., Davis-Gardner M.E., Wies E., Chiang C, & Gack M.U. (2020). ISG15-dependent Activation of the RNA Sensor MDA5 and its Antagonism by the SARS-CoV-2 papain-like protease. bioRxiv.
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3

Analyzing MDA5 Oligomerization by Native PAGE

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Native PAGE for analyzing endogenous IRF3 dimerization was performed as previously described52 (link). For measuring MDA5 oligomerization, HEK293T or HEK293 MDA5 KO cells were transfected with WT or mutant FLAG-MDA5–2CARD or FLAG-MDA5 as indicated. Twenty-four hours later, cells were lysed in 1× NativePAGE sample buffer (Invitrogen) containing 1% (v/v) NP-40 on ice for 30 min and then lysates were cleared by centrifugation at 16,000 ×g at 4°C for 10 min. Cleared lysates were resolved on a 3–12% Bis-Tris NativePAGE gel (Invitrogen) as per the manufacturer’s instructions and analyzed by immunoblotting with the indicated antibodies.
Liu G., Lee J.H., Parker Z.M., Acharya D., Chiang J.J., van Gent M., Riedl W., Davis-Gardner M.E., Wies E., Chiang C, & Gack M.U. (2021). ISG15-dependent activation of the sensor MDA5 is antagonized by the SARS-CoV-2 papain-like protease to evade host innate immunity. Nature microbiology, 6(4), 467-478.
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4

Native-PAGE Analysis of HIV Env Oligomeric Status

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A modified BN-PAGE protocol59 (link) was used to determine the oligomeric status of the immunoisolated Env protein recovered under native conditions (elution with 3xFLAG peptide) from infected CEM cells. Briefly, the eluate, various Env-VLPs and soluble JR-FL gp120 (Progenics) were incubated in an equal volume of solubilization buffer (0.12% Triton X-100, 1 mM EDTA/1.5 M aminocaproic acid) containing protease inhibitor cocktail (Sigma). An equal volume of 2× sample buffer containing 150 mM MOPS, 100 mM Tris-HCl (pH 7.7), 40% glycerol and 0.1% Coomassie blue was then added and samples were loaded onto a 4–12% Bis-Tris native-PAGE gel (Invitrogen). Samples were electrophoresed at 4 °C for 3 h at 100 V with 50 mM MOPS/50 mM Tris (pH 7.7) containing 0.002% Coomassie blue as cathode buffer and the same buffer without Coomassie blue as the anode buffer. The gel was then transferred onto PVDF membrane. Excess Coomassie blue dye was removed after blotting by washing with 30% methanol/10% acetic acid then 100% methanol. The blot was probed using 1 μg ml−1 each of human monoclonal antibodies: 2G12, b12 and 447-52D (anti-gp120 cocktail) and 20 μg ml−1 each of 4E10 and 2F5 (anti-gp41 cocktail). Goat anti-human alkaline phosphatase conjugates were used to detect the primary antibodies at 1:3,000 (Jackson).
Luo Y., Jacobs E.Y., Greco T.M., Mohammed K.D., Tong T., Keegan S., Binley J.M., Cristea I.M., Fenyö D., Rout M.P., Chait B.T, & Muesing M.A. (2016). HIV–host interactome revealed directly from infected cells. Nature microbiology, 1(7), 16068.
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5

Analyzing RBD Multimer Protein Complexes

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RBD multimer proteins and particles were analyzed by blue native polyacrylamide gel electrophoresis (BN-PAGE). The proteins were mixed with sample buffer and G250 loading dye and added to a 3 to 12% bis-Tris NativePAGE gel (Life Technologies). BN-PAGE gels were run for 2 h at 150 V using the NativePAGE running buffer (Life Technologies) according to the manufacturer’s instructions.
Guo Y., He W., Mou H., Zhang L., Chang J., Peng S., Ojha A., Tavora R., Parcells M.S., Luo G., Li W., Zhong G., Choe H., Farzan M, & Quinlan B.D. (2021). An Engineered Receptor-Binding Domain Improves the Immunogenicity of Multivalent SARS-CoV-2 Vaccines. mBio, 12(3), e00930-21.
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6

SARS-CoV-2 Spike Protein Analysis

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SARS-CoV-2 spikes and spike-presenting SApNPs were analyzed by blue native polyacrylamide gel electrophoresis (BN-PAGE) and stained with Coomassie blue. The proteins were mixed with sample buffer and G250 loading dye and added to a 4–12% Bis-Tris NativePAGE™ gel (Life Technologies). BN-PAGE gels were run for 2 to 2.5 hours at 150 V using the NativePAGE™ running buffer (Life Technologies) according to the manufacturer’s instructions.
He L., Lin X., Wang Y., Abraham C., Sou C., Ngo T., Zhang Y., Wilson I.A, & Zhu J. (2021). Single-component, self-assembling, protein nanoparticles presenting the receptor binding domain and stabilized spike as SARS-CoV-2 vaccine candidates. bioRxiv.
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7

Blue Native PAGE Analysis of SARS-CoV-2 Spikes

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SARS-CoV-2 spikes and spike-presenting SApNPs were analyzed by blue native PAGE and stained with Coomassie blue. The proteins were mixed with sample buffer and G250 loading dye and added to a 4 to 12% Bis-Tris NativePAGE gel (Life Technologies). BN-PAGE gels were run for 2 to 2.5 hours at 150 V using the NativePAGE running buffer (Life Technologies) according to the manufacturer’s instructions.
He L., Lin X., Wang Y., Abraham C., Sou C., Ngo T., Zhang Y., Wilson I.A, & Zhu J. (2021). Single-component, self-assembling, protein nanoparticles presenting the receptor binding domain and stabilized spike as SARS-CoV-2 vaccine candidates. Science Advances, 7(12), eabf1591.
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8

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 NativePAGETM 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 NativePAGETM 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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9

Native PAGE Analysis of Ebola Glycoprotein

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EBOV GPΔmuc and GPΔmuc-presenting NPs were analyzed by BN-PAGE and stained with Coomassie blue. The proteins were mixed with sample buffer and G250 loading dye and added to a 4–12% Bis-Tris NativePAGETM gel (Life Technologies). BN-PAGE gels were run for 2–2.5 h at 150 V using NativePAGETM running buffer (Life Technologies) according to the manufacturer’s instructions. BN-PAGE images were collected using Image Lab v6.0 software.
He L., Chaudhary A., Lin X., Sou C., Alkutkar T., Kumar S., Ngo T., Kosviner E., Ozorowski G., Stanfield R.L., Ward A.B., Wilson I.A, & Zhu J. (2021). Single-component multilayered self-assembling nanoparticles presenting rationally designed glycoprotein trimers as Ebola virus vaccines. Nature Communications, 12, 2633.
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10

Purified GPR Native PAGE Analysis

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Purified GPR samples were mixed with BN-PAGE loading buffer (50 mM Bis-Tris-HCl pH 7.2, 50 mM NaCl, 10% (v/v) glycerol) supplemented with 0.5% (w/v) Cymal-5 and 0.375% (w/v) Coomassie Brilliant Blue G-250. A total of 2.5 μg GPR were loaded per lane on a precast 4–16% Bis-Tris NativePAGE gel (ThermoFisher). The gel was run using an anode buffer (50 mM Bis-Tris, 50 mM Tricine pH 6.8) and a dark blue cathode buffer (50 mM Bis-Tris, 50 mM Tricine pH 6.8, 0.02% (w/v) Coomassie Brilliant Blue G-250) for the first 30 min at 150 V, and a light blue cathode buffer (50 mM Bis-Tris, 50 mM Tricine pH 6.8, 0.002% (w/v) Coomassie Brilliant Blue G-250) for the following 80 min at 250 V. The gel tank was immersed in ice water during the whole run.
Hirschi S., Kalbermatter D., Ucurum Z, & Fotiadis D. (2020). Cryo-electron microscopic and X-ray crystallographic analysis of the light-driven proton pump proteorhodopsin reveals a pentameric assembly. Journal of Structural Biology: X, 4, 100024.
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