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Tris glycine buffer

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Tris/Glycine buffer is a commonly used buffer solution in biochemistry and molecular biology. It is a mixture of Tris and glycine, which helps maintain a specific pH range for various laboratory applications, such as electrophoresis and Western blotting.

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Lab products found in correlation

Tris glycine sds buffer, by Bio-Rad (13 mentions) Native sample buffer, by Bio-Rad (6 mentions) Mini protean tgx precast gel, by Bio-Rad (6 mentions) Chemidoc imaging system, by Bio-Rad (6 mentions) Laemmli sample buffer, by Bio-Rad (5 mentions) Sds page gel, by Bio-Rad (5 mentions) Mini protean tgx gel, by Bio-Rad (5 mentions) Pierce bca protein assay kit, by Thermo Fisher Scientific (5 mentions) 2 mercaptoethanol, by Merck Group (4 mentions) Wet electroblotting system, by Bio-Rad (4 mentions) Tbs t, by Bio-Rad (4 mentions) Anti rabbit igg conjugated with horseradish peroxidase, by Cell Signaling Technology (4 mentions) Gapdh, by Merck Group (3 mentions) Immuno blot pvdf membrane, by Bio-Rad (3 mentions) Blotting grade blocker, by Bio-Rad (3 mentions) Pierce ecl western blotting substrate, by Thermo Fisher Scientific (3 mentions) Tbs t, by Cell Signaling Technology (3 mentions) Laemmli buffer, by Bio-Rad (3 mentions) Pvdf membrane, by Bio-Rad (3 mentions) β mercaptoethanol, by Merck Group (3 mentions)

Close spelling variants of this product

Tris/Glycine/SDS buffer (103 citations) Tris/Glycine/SDS running buffer (75 citations) Glycine (46 citations) Tris-glycine running buffer (11 citations) Tris buffer (5 citations) Tris/Glycine/SDS electrophoresis buffer (5 citations) Tris/glycine transfer buffer (5 citations) Tris-Glycine SDS Sample Buffer (4 citations) Tris/glycine buffer system (3 citations) Tris-glycine gels with Tris/glycine/SDS buffer (3 citations)

63 protocols using tris glycine buffer

1

Native PAGE Analysis of Proteins

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After CHAPS solubilization of HEK293 cells, PNS were incubated for 15 min at RT in native sample buffer (Bio-Rad) and subjected to 7.5% native nonreducing acrylamide gel in Tris/glycine buffer (Bio-Rad). Proteins were then transferred onto PVDF membrane in Tris/glycine buffer (Bio-Rad). Immunoblot analysis was performed as described above.
Rudinskiy M., Bergmann T.J, & Molinari M. (2022). Quantitative and time-resolved monitoring of organelle and protein delivery to the lysosome with a tandem fluorescent Halo-GFP reporter. Molecular Biology of the Cell, 33(6), ar57.
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2

Native Protein Immunoblot Analysis

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After CHAPS lysis, PNSs were incubated for 15 min at RT in Native Sample Buffer (Bio‐Rad) and run on 7.5% native acrylamide gel in Tris/Glycine Buffer (Bio‐Rad). Proteins were then transferred onto PVDF membrane in Tris/Glycine Buffer (Bio‐Rad). Immunoblot analysis was performed as described above.
Fregno I., Fasana E., Soldà T., Galli C, & Molinari M. (2021). N‐glycan processing selects ERAD‐resistant misfolded proteins for ER‐to‐lysosome‐associated degradation. The EMBO Journal, 40(15), e107240.
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3

Purification and Functionalization of Nickel Microparticles

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Acrylamide/bis-acrylamide (40% wt/wt) solution (A7802), N,N,N′,N′-tetramethylethylenediamine (TEMED, T9281), ammonium persulfate (APS, A3678), sodium deoxycholate (D6750), β-Mercaptoethanol (M3148), imidazole (792 527), and SDS (L3771), were obtained from Sigma-Aldrich. Triton X-100 was purchased from Fisher Scientific (BP-151). 10× Tris/glycine buffer was obtained from Bio-Rad (161-0734). Phosphate buffered saline (PBS), pH 7.4 was obtained from Gibco (10 010–023). Tris-HCl, pH 6.8 was purchased from Teknova (T1568). PureProteome nickel magnetic microparticles with 10 μm diameter were obtained from Millipore Sigma (LSKMAGH02). A 6-tube magnetic separation rack was obtained from New England BioLabs (S1506S). N-[3-[(3-Benzoylphenyl)-formamido] propyl] methacrylamide (BPMAC) was custom synthesized by PharmAgra Laboratories. SU-8 developer (Y020100) and photoresist SU-8 2025 (Y111069) were obtained from MicroChem. Deionized water (ddH2O, 18.2 mΩ) was obtained using ultrapure water system (Millipore). Unless stated otherwise, chemicals and reagents were obtained from Sigma-Aldrich.
Kim J.J., Chan P.P., Vlassakis J., Geldert A, & Herr A.E. (2018). Microparticle Delivery of Protein Markers for Single-Cell Western Blotting from Microwells. Small (Weinheim an der Bergstrasse, Germany), 14(48), e1802865.
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4

Myocardial Tissue Protein Analysis

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Myocardial tissue samples were obtained from the right ventricle free wall at T3 and flash frozen at −80 °C. Whole tissue was homogenized, after which protein extraction and quantification was performed using Tissue Extraction Reagent‐I and Protease and Phosphatase Inhibitor EDTA‐Free (ThermoFisher, MA). Next, 30 μg of each tissue protein extract was loaded on SDS‐PAGE with running buffer (10× Tris/Glycine/SDS, Bio‐Rad, ON), blotted on a polyvinylidene difluoride membrane with 10× Tris/Glycine buffer (Bio‐Rad, ON), and probed overnight at 4 °C for cleaved caspase−3 (#9661, 1:1000), Akt (#4691, 1:1000), phospho‐Akt (#4060, 1:2000), endothelial nitric oxide synthase (eNOS; #32027, 1:1000), phospho‐eNOS (#9570, 1:1000; all Cell Signaling, MA) and GAPDH (G8795, 1:15000, Sigma‐Aldrich, MO) as loading control. Protein bands were detected using corresponding horseradish peroxidase–conjugated goat anti‐mouse (#7076, 1:3000) or anti‐rabbit secondary antibodies (#7074, 1:1000; both Cell Signaling), imaged via chemiluminescence on an Odyssey Fc Imaging System and quantified using Imaging Studio ver. 5.0 (LI‐COR Biotechnology, NE).
Kadowaki S., Siraj M.A., Chen W., Wang J., Parker M., Nagy A., Steve Fan C., Runeckles K., Li J., Kobayashi J., Haller C., Husain M, & Honjo O. (2023). Cardioprotective Actions of a Glucagon‐like Peptide‐1 Receptor Agonist on Hearts Donated After Circulatory Death. Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 12(3), e027163.
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5

Milk-based Protein Characterization Protocol

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Whole raw milk and raw cream were provided by a local supplier (Quebec City, QC, Canada) and skim milk powder (SMP) was obtained from Agropur (Quebec City, QC, Canada). The thermophilic yogurt culture YC-X11 Yo-Flex® (Chr. Hansen A/S, Hørsholm, Denmark) was composed of Streptococcus thermophilus and Lactobacillus delbrueckii subsp. Bulgaricus. Analytical-grade sodium hydroxide for the preparation of 0.1 M of NaOH was obtained from Fisher Chemical (Ottawa, ON, Canada). Mini-PROTEAN TGX Stain-Free Gels (12%, 15-well comb, 15 µL), 2× Laemmli sample buffer, native sample buffer, Precision Plus ProteinTM All Blue Standards, 10× Tris/glycine/sodium dodecyl sulfate (SDS) buffer, and 10× Tris/glycine buffer were all obtained from BioRad (Hercules, CA, USA). 2-Mercaptoethanol was provided by Sigma-Aldrich (St. Louis, MO, USA). Methanol was obtained from Fisher Chemical (Ottawa, ON, Canada) and glacial acetic acid from Anachemia (Radnor, PA, USA). Fast Green FCF and Nile Red were obtained from Sigma-Aldrich (Oakville, ON, Canada).
Krebs L., Bérubé A., Iung J., Marciniak A., Turgeon S.L, & Brisson G. (2021). Impact of Ultra-High-Pressure Homogenization of Buttermilk for the Production of Yogurt. Foods, 10(8), 1757.
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6

Native Immunoblotting Protocol

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We performed immunoblotting under non-denaturing conditions according to a previously published method [60 (link)] and using the commercially available pre-cast Mini-PROTEAN TGX Gels 4–20% (Cat. # 4561093; Bio-Rad), Native Sample Buffer (Cat. # 1610738; Bio-Rad) and 10× Tris/Glycine Buffer (Cat. # 1610734; Bio-Rad) according to manufacturer’s instructions. Immunoblotting, primary and secondary antibodies incubation and development were done as described above for SDS-PAGE.
Ali T., Klein A.N., McDonald K., Johansson L., Mukherjee P.G., Hallbeck M., Doh-ura K., Schatzl H.M, & Gilch S. (2023). Cellulose ether treatment inhibits amyloid beta aggregation, neuroinflammation and cognitive deficits in transgenic mouse model of Alzheimer’s disease. Journal of Neuroinflammation, 20, 177.
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7

Protein Quantification by Western Blot

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Protein (8 ug) was loaded on 4–15% Criterion Tris/Glycine gels (Bio-Rad, #5671085) and run for 60 min at 150 constant volts in 1X Tris/Glycine buffer (Bio-Rad, #1610732). Protein was transferred from gels to nitrocellulose with Bio-Rad Turbo on default setting. All blots were air-dried, rehydrated with TBS and blocked for 1 h at RT in 5% BSA in TBST (0.1%). Blots were exposed to primary antibody in 5% BSA in TBST (0.1%) overnight at 4 C. Blots were washed 3× with TBST (0.1%), 5 min per wash, at RT. Secondary antibody was added at 1:18,000: anti-rabbit-HRP (CST 7074) and/or anti-mouse-HRP (CST 7076) in 5% BSA in TBST (0.1%). Blots were incubated at RT for 1 h. Blots were washed 3 times in TBST (0.1%) for 5 min each wash at RT. All incubations and washing were done while rocking. Signal was developed with 6 ml of Femto Max ECL substrate (ThermoFisher, #34094) for 4 min and blots read on ChemiDoc. Densitometry was performed with ImageLab.
Cantley J., Ye X., Rousseau E., Januario T., Hamman B.D., Rose C.M., Cheung T.K., Hinkle T., Soto L., Quinn C., Harbin A., Bortolon E., Chen X., Haskell R., Lin E., Yu S.F., Del Rosario G., Chan E., Dunlap D., Koeppen H., Martin S., Merchant M., Grimmer M., Broccatelli F., Wang J., Pizzano J., Dragovich P.S., Berlin M, & Yauch R.L. (2022). Selective PROTAC-mediated degradation of SMARCA2 is efficacious in SMARCA4 mutant cancers. Nature Communications, 13, 6814.
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8

Western Blot Protein Analysis

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Protein lysates (40 μg per lane) were loaded on a 4–15% SDS-PAGE gel (Bio-Rad), separated in 1X Tris-Glycine Buffer (Bio-Rad), and transferred to PVDF membranes via a wet electro-blotting system (Bio-Rad), all according to the manufacturer’s directions74 (link). PVDF membranes were blocked for 1 hour in 5% non-fat milk in Tris-buffered saline containing 0.1% Tween-20 (TBS-T, Bio-Rad), then incubated overnight at 4°C with antibodies listed in STAR Methods in 5% BSA in TBS-T. Blots were then probed with anti-Rabbit IgG conjugated with horseradish peroxidase (1:5000, Cell Signaling Technology) in 5% BSA in TBS-T for 1 hour at room temperature. Signal was detected with the Pierce™ ECL Western Blotting Substrate (Millipore, MA, USA), and blot images were collected with a Bio-Rad ChemiDoc imaging system.
Wang E., Simard M., Bergeron Y., Beauchamp D, & Bergeron M.G. (2000). In Vivo Activity and Pharmacokinetics of Ziracin (SCH27899), a New Long-Acting Everninomicin Antibiotic, in a Murine Model of Penicillin-Susceptible or Penicillin-Resistant Pneumococcal Pneumonia. Antimicrobial Agents and Chemotherapy, 44(4), 1010-1018.
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9

Western Blot Analysis of Protein Samples

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Mini-PROTEAN TGX precast gels (Bio-Rad) were loaded with protein in Laemmli sample buffer (Bio-Rad) containing 5% (v/v) 2-mercaptoethanol (Sigma). The Precision Plus Protein Kaleidoscope standard (Bio-Rad) was used to determine protein size. Electrophoresis took place in 1X Tris/glycine/SDS buffer (Bio-Rad) at 100 volts at room temperature. The protein was transferred onto Immuno-Blot PVDF Membrane (Bio-Rad) in 1X Tris/glycine buffer (Bio-Rad) at 22 volts overnight at 4 °C. The membranes were blocked for 30 minutes with 5% (w/v) Blotting-Grade Blocker (Bio-Rad) in TBST at room temperature. Membranes were incubated with primary antibodies for one hour at room temperature or overnight at 4 °C. Membranes were incubated with secondary antibodies (goat anti-mouse IgG-HRP [sc-2005, Santa Cruz Biotechnology, Dallas, TX] or goat anti-rabbit IgG-HRP [sc-2004, Santa Cruz Biotechnology]) for one hour at room temperature. Protein bands were detected using the Pierce ECL Western Blotting Substrate (Thermo). Relative band intensities were determined using ImageJ software (NIH).
Cartularo L., Laulicht F., Sun H., Kluz T., Freedman J.H, & Costa M. (2015). Gene expression and pathway analysis of human hepatocellular carcinoma cells treated with cadmium. Toxicology and applied pharmacology, 288(3), 399-408.
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10

Western Blotting Protein Analysis Protocol

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Mini-PROTEAN TGX precast gels (Bio-Rad) were loaded with protein in Laemmli sample buffer (Bio-Rad) containing 5% (v/v) 2-mercaptoethanol (Sigma Aldrich). The Precision Plus Protein Kaleidoscope standard (Bio-Rad) was used to determine protein size. Electrophoresis took place in 1X tris/glycine/SDS buffer (Bio-Rad) at 100 volts at room temperature. The protein was transferred onto Immuno-Blot PVDF Membrane (Bio-Rad) in 1X tris/glycine buffer (Bio-Rad) at 22 volts overnight at 4°C. The membranes were blocked for 30–60 minutes with 5% (w/v) Blotting-Grade Blocker (Bio-Rad) in TBST at room temperature. Membranes were incubated with primary antibodies for one hour at room temperature or overnight at 4°C. Membranes were incubated with secondary antibodies (goat anti-mouse IgG-HRP [sc-2005, Santa Cruz Biotechnology, Dallas, TX] or goat anti- rabbit IgG-HRP [sc-2004, Santa Cruz Biotechnology]) for one hour at room temperature. Protein bands were detected using the Pierce ECL Western Blotting Substrate (Thermo Fisher Scientific). Relative band intensities were determined using ImageJ software (NIH).
Cartularo L., Kluz T., Cohen L., Shen S.S, & Costa M. (2016). Molecular Mechanisms of Malignant Transformation by Low Dose Cadmium in Normal Human Bronchial Epithelial Cells. PLoS ONE, 11(5), e0155002.
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