OptiPrep® (iodixanol 60% (w/v)), CuSO4, lipoxidase V from Glycine max (EC 1.13.11.12), phospholipase A2 from porcine pancreas (EC 3.1.1.4), CaCl2, ascorbic acid, α-tocopherol (≥ 96%), and barbital buffer were from Sigma Aldrich (St. Louis, MO, USA). 5,5-Dimethyl-1-pyrroline N-oxide (DMPO) was from Dojindo (Kumamoto, Japan). Sephacryl S200 was from GE Healthcare Lifescience (Pittsburg, PA, USA). Agarose and BODIPY581/591 C11 were from Invitrogen (Grand Island, NY, USA). The BCA protein assay was from Pierce (Rockford, IL, USA). Chelex C-100 and Commassie Blue staining solution were from BioRad (Hercules, CA, USA). Phosphate and Tris buffers were prepared and Chelex-treated for removal of contaminant trace metal ions.
Barbital buffer
Manufactured by Merck Group
Sourced in United States, Sao Tome and Principe, Italy
Barbital buffer is a laboratory buffer solution used to maintain a specific pH level for various analytical and experimental procedures. It is commonly used in biochemical and immunological applications. The buffer solution contains sodium barbital and barbital as the primary components, which work to stabilize the pH within the desired range.
Automatically generated - may contain errors
Lab products found in correlation
Hydragel 15 30 lipoprotein e agarose gels, by Sebia (3 mentions)
Titan gel electrophoresis chamber, by Helena Laboratories (3 mentions)
Sudan black, by Merck Group (2 mentions)
Filipin, by Merck Group (2 mentions)
Agarose, by Thermo Fisher Scientific (1 mentions)
Sephacryl s 200, by GE Healthcare (1 mentions)
Bodipy 581 591 c11, by Thermo Fisher Scientific (1 mentions)
Optiprep, by Merck Group (1 mentions)
α tocopherol, by Merck Group (1 mentions)
5 5 dimethyl 1 pyrroline n oxide dmpo, by Dojindo Laboratories (1 mentions)
Phospholipase a2 from porcine pancreas, by Merck Group (1 mentions)
Ascorbic acid, by Merck Group (1 mentions)
Cacl2, by Merck Group (1 mentions)
Cuso4, by Merck Group (1 mentions)
Fluorescein, by Merck Group (1 mentions)
Sodium hydroxide (naoh), by Merck Group (1 mentions)
Boric acid, by Merck Group (1 mentions)
Egg yolk emulsion, by Merck Group (1 mentions)
Rpmi 1640 amino acids solution, by Merck Group (1 mentions)
Phosphate buffered saline (pbs), by Thermo Fisher Scientific (1 mentions)
6 protocols using barbital buffer
1
Oxidative Stress Assay Protocol
2
Serum-Fluorescein-Antibody Characterization
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Analytical grade N-cyclohexyl-2-aminoethanesulfonic acid (CHES), L-arginine, boric acid, sodium hydroxide, barbital buffer and fluorescein were obtained from Sigma Aldrich (St. Louis, Missouri). Mouse anti-fluorescein monoclonal antibody was obtained from Millipore Corporation (Temecula, CA) and lyophilized powder of human serum was purchased from Thermo Fisher (Fair Lawn, New Jersey). All the chemicals were used without further purification.
boric acid buffer (100 mM, pH 10), arginine buffer (100 mM, pH 11), CHES buffer (20 mM, pH 10) and barbital buffer (50 mM pH 8) were prepared in ultrapure water and their pH adjusted using 1 M sodium hydroxide solution. All the solutions were stored at 4 °C and allowed to equilibrate at room temperature before use. A stock solution of serum was prepared in ultrapure water at a concentration of 20 mg/mL and diluted to the appropriate final concentration. Sample mixtures were prepared by combining appropriate volumes of stock solutions of serum, fluorescein, and the anti-fluorescein antibody together and diluting to the desired concentrations using ultra-pure water.
boric acid buffer (100 mM, pH 10), arginine buffer (100 mM, pH 11), CHES buffer (20 mM, pH 10) and barbital buffer (50 mM pH 8) were prepared in ultrapure water and their pH adjusted using 1 M sodium hydroxide solution. All the solutions were stored at 4 °C and allowed to equilibrate at room temperature before use. A stock solution of serum was prepared in ultrapure water at a concentration of 20 mg/mL and diluted to the appropriate final concentration. Sample mixtures were prepared by combining appropriate volumes of stock solutions of serum, fluorescein, and the anti-fluorescein antibody together and diluting to the desired concentrations using ultra-pure water.
3
Artificial Mucus Composition for Antimicrobial Evaluation
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N-acetylcysteine (NAC), bromelain, ascorbic acid, Ribes nigrum, resveratrol, and pelargonium were kindly donated by Anvest Health s.r.l. (Castel San Giorgio, Salerno, Italy). Deoxyribonucleic acid (DNA), mucin from the porcine stomach, diethylenetriaminepentaacetic acid (DTPA), RPMI 1640 amino acids solution, egg yolk emulsion, sodium chloride, and potassium chloride, used for artificial mucus preparation, and barbital buffer were purchased from Sigma-Aldrich (Milan, Italy), while the hydroxyethylcellulose was obtained from A.C.E.F. SpA (Piacenza, Italy). Mueller–Hinton broth (MHB) and Mueller–Hinton agar (MHA) were acquired from Biolife (Milan, Italy); trypticase soy broth (TSB) was obtained from Difco Laboratories, and phosphate-buffered saline (PBS) from GIBCO, Thermo Fisher Scientific. All other solvents and chemicals were of analytical grade.
4
Serum Lipoprotein Electrophoresis and Cholesterol Staining
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Serum samples were loaded on Sebia Hydragel 15/30 lipoprotein (e) agarose gels (Sebia, Inc.) and run at 100 V for 1 hour in Barbital buffer (Millipore Sigma) in a Titan gel electrophoresis chamber (Helena Laboratories). Gels were fixed and stained with Sudan Black (Millipore Sigma) to detect neutral lipids or freshly prepared filipin (Millipore Sigma) to detect FC using previously described methods.[16 ]
5
Serum Lipoprotein Gel Electrophoresis
6
Lipoprotein Electrophoresis for Lp-X Quantification
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Ten microliters EDTA‐plasma or purified human lipoproteins (LDL, VLDL, and HDL) were loaded on Sebia Hydragel 15/30 lipoprotein(e) agarose gels (#4134; Sebia, Inc). Electrophoresis was performed for 1 hour at 100 V in barbital buffer (#B5934‐12VL; MilliporeSigma) in a Titan Gel electrophoresis chamber (Helena Laboratories). Gels were either fixed and stained with Sudan Black to detect neutral lipids or incubated with Filipin Stain to detect free cholesterol exactly as described in reference.5 Lp‐X, which migrates toward the cathode in the opposite direction as normal lipoproteins, was quantified by densitometry of the cathode‐migrating band in filipin‐stained gels, and background in an equal‐sized area of the gel 1 cm below the bottom of each band was subtracted using Alpha Imager software as described in Freeman et al, 2019.5
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