All the above peanut seeds were pressed with a cold pressing machine (CA59G, German Monforts Group, Moenchen‐gladbach, North Rhine‐Westphalia, Germany) at a temperature below 60°C. Each oil obtained was centrifuged at 25,230 × g for 15 min (Avanti J‐26 XP, Beckman Coulter Inc., Brea, CA, USA) to remove residue and then kept cold (4 ± 2°C) for future experimental treatments.
Avanti j 26 xp
Manufactured by Beckman Coulter
Sourced in United States, France
The Avanti J-26 XP is a high-performance centrifuge designed for a wide range of applications in clinical and research laboratories. It features a rugged, compact design and offers fast acceleration and deceleration times, ensuring efficient sample processing. The Avanti J-26 XP is capable of reaching speeds up to 26,000 RPM and generates a maximum relative centrifugal force (RCF) of 106,210 x g, making it suitable for a variety of sample types and separation needs.
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Lab products found in correlation
Sonic dismembrator model 500, by Thermo Fisher Scientific (5 mentions)
Optima l 80 xp, by Beckman Coulter (3 mentions)
Protease inhibitor cocktail, by Roche (2 mentions)
Optima xpn 80, by Beckman Coulter (2 mentions)
High speed centrifuge, by Beckman Coulter (1 mentions)
New brunswick innova 44, by Eppendorf (1 mentions)
Rotor 70.1ti, by Beckman Coulter (1 mentions)
L8 m ultrafuge, by Beckman Coulter (1 mentions)
Ni2 nta resin, by GE Healthcare (1 mentions)
Emulsiflex c5 cell homogenizer, by Avestin (1 mentions)
Superdex 200 column, by GE Healthcare (1 mentions)
Superdex 75, by GE Healthcare (1 mentions)
Uv 1800, by Shimadzu (1 mentions)
Optima xe 100, by Beckman Coulter (1 mentions)
Vivaflow 200, by Sartorius (1 mentions)
Amicon ultra centrifugal filter device, by Merck Group (1 mentions)
Profinity imac ni charged resin, by Bio-Rad (1 mentions)
Optima l 90k, by Beckman Coulter (1 mentions)
Sodium cholate, by Merck Group (1 mentions)
Reacti vial, by Thermo Fisher Scientific (1 mentions)
64 protocols using avanti j 26 xp
1
Cold Pressing and Centrifugation of Peanut Oils
2
Isolation and Storage of Extracellular Vesicles
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Briefly, the harvested medium was collected and subjected to ultracentrifugation [17 (link), 21 ]. Subsequently, the cells, cell debris, and apoptotic bodies were removed by centrifugation at 300×g for 10 min, 2000×g for 15 min, and 5000×g for 15 min, sequentially. The EVs were then pelleted by further centrifugation at 20,000×g (Beckman Coulter Avanti J-26XP, High-Speed Centrifuge and JA-25.50 Fixed-Angle Aluminum Rotor) for 90 min at 4 °C. The resulting precipitant was collected, suspended in 1 ml of PBS, and then centrifuged at 20,000×g for 90 min. The EVs were collected and stored at − 80 °C until further use. The storage period did not exceed 2 weeks.
3
Purification of Nuo Enzyme Variants
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BW25113Δndh nuo::ntpII FRT (Burschel et al., 2019 (link)) was transformed either with pBADnuohisnuoF containing the nuo-operon encoding the wild type enzyme decorated with a His-tag or with pBADnuoHisnuoF D213GH encoding the variant. Cells were grown in autoinduction medium while shaking (180 rpm, New Brunswick Innova 44, Eppendorf). At an OD600 of ~4.0 cells were harvested by centrifugation (3,913 · g, 15 min, 4°C; JLA 8.1000, Avanti J-26 XP, Beckman Coulter), shock frozen in liquid nitrogen and stored at −80°C.
4
Exfoliation and Purification of Flake-Like Phosphorene
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Example 1
FL-P dispersion preparation: BP crystals were purchased from Smart-Elements and stored in a dark Ar glovebox prior to use. Deionized water with 2% w surfactant was purged with ultrahigh purity grade Ar for at least 1 hr to remove dissolved oxygen. A customized tip ultrasonicator setup was prepared by perforating the plastic lid of a 50 mL conical tube with a 0.125 inch sonicator tip. The interface between the tip and the lid was sealed with PDMS several times to block potential diffusion pathways of ambient O2 and H2O. The deoxygenated water and BP were placed in this sealed conical tube with an initial concentration of 1 mg mL−1 under Ar atmosphere with less than 10% relative humidity. Additionally, Parafilm and Teflon tapes were used to further seal the vessel from ambient exposure. The sealed container was connected to the ultrasonicator (Fisher Scientific model 500 sonic dismembrator) in ambient conditions, and then BP crystals were exfoliated by ultrasonication. The resulting solution was centrifuged at 7,500 r.p.m. for 2 hrs at 15° C. to enrich FL-P nanosheets (Avanti J-26 XP, Beckman Coulter). Following centrifugation, the supernatant was collected and then ultracentrifuged at 14,000 r.p.m. for 2 hrs at 22° C. using a SW32Ti rotor (Optima L-80 XP, Beckman Coulter) before redispersing in deoxygenated water.
5
Solvent Exfoliation of 2D InSe Crystals
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Example 2
LPE of InSe. For solvent exfoliation experiments, ethanol and deionized water mixtures were sparged with ultrahigh purity grade Ar for at least 1 hr to remove dissolved oxygen. A customized tip sonicator setup was prepared to minimize ambient exposure, as reported previously. (See, Kang, J. et al. Stable aqueous dispersions of optically and electronically active phosphorene. Proc. Natl. Acad. Sci. U.S.A. 113, 11688-11693 (2016); and Kang, J. et al. Solvent exfoliation of electronic-grade, two-dimensional black phosphorus. ACS Nano 9, 3596-3604 (2015).) The resulting deoxygenated co-solvent mixture and InSe crystals were placed in the sealed tip sonicator vessel with an initial concentration of 1 mg ml−1 under an Ar atmosphere (<10% relative humidity). The container was then connected to a sonicator (Fisher Scientific Model 500 Sonic Dismembrator). The InSe crystals were exfoliated by ultrasonication at ˜30 W for 2 hrs in an ice bath under pulsed conditions (2 sec on and 1 sec off) to avoid solvent evaporation. As-prepared InSe dispersions were then centrifuged to remove unexfoliated InSe crystals (Avanti J-26 XP, Beckman Coulter).
6
Purification of Polyol Kinase Enzymes
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V. cholerae PFK and BsrV enzymes were overproduced in E. coli strain BL21 as 6×His-tagged constructs from a pET28b vector. Overnight cultures of overexpression strains were diluted into 250 mL LB broth and grown until OD600 = 0.5. Flasks were supplemented with 1 mM IPTG and shaking at 37º C for 2 h. Cells were pelleted, and resuspended in equilibration buffer (Tris 50 mM, pH 7.5, 50 mM NaCl, with protease inhibitor cocktail (Roche)) and disrupted by passaging once through a French press. Lysates were centrifuged for 1 h (25,000 rpm, Beckman Coulter Avanti J26-XP centrifuge, JL-25.50 rotor) at 4°C. Nickel-NTA resin (0.5 ml resuspended in equilibration buffer) was then added to the supernatant, followed by incubation at 4°C in a rotating wheel. The lysate was separated from the resin by centrifugation for 1 minute at 3,220 g and the resin washed (5×10 ml) with washing buffer (equilibration buffer adjusted to 1 M NaCl) and eluted with 2ml of washing buffer containing 500mM imidazole. Fractions were subjected to SDS-PAGE and Coomassie Brilliant Blue staining for purity assessment. Protein concentration was quantified with a Bradford assay.
7
Semiconducting CNT and MoS2 Dispersion Preparation
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The semiconducting CNT solution was prepared as previously reported via density gradient ultracentrifugation, with >99% semiconducting purity and refined average diameter of 1.6 nm26 (link)–31 (link). MoS2 dispersion preparation began with 60 mg of MoS2 powder (American Elements, Inc.) and 15 mL ethanol-water co-solvent (10 mL ethanol and 5 mL de-ionized water) being placed in a 50 mL plastic conical tube with a sealed setup32 (link) to avoid solvent evaporation and exfoliated by ultrasonication (Model 500 Sonic Dismembrator, Fisher Scientific) at ~30 W for 1 h in an iced bath. The resulting MoS2 dispersions were then centrifuged at 5000 rpm for 30 min to remove unexfoliated MoS2 powder (Avanti J-26 XP, Beckman Coulter, Inc.) and the supernatant was carefully decanted. CdSeS/ZnS alloyed quantum dots in aqueous solution (COOH functionalized, fluorescence wavelength maximum λem = 575 nm, 6 nm diameter, 1 mg/ml in H2O) were purchased from Sigma-Aldrich, Inc.
8
Cultivation of Gluconobacter oxydans NL71
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Gluconobacter oxydans NL71 strain (derived from ATCC621) was stored on sorbitol-agar culture medium containing 50 g/L sorbitol, 15 g/L agar, and 5 g/L yeast extract at 4 °C. G. oxydans was germinated in a 250-mL Erlenmeyer flask with three baffles containing 50 mL nutrient medium (100 g/L sorbitol and 10 g/L yeast extract) and cultivated in a constant temperature shaker at 30 °C and 220 rpm for 24–36 h. Bacteria were harvested using refrigerated centrifugation (Avanti J-26 XP, Beckman Coulter) at 8000 rpm for 5–10 min as a reserve [6 (link)].
9
Isolation and Purification of E. coli Cytoplasmic Membranes
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Escherichia coli BW25113 cells were grown aerobically (180 rpm) at 37°C in baffled flasks using LB-medium. The cells were harvested by centrifugation (5700 × g, 10 min, 4°C, Rotor JLA 8.1000, Avanti J-26 XP, Beckman Coulter) in the late exponential phase yielding approximately 6.5 g cells/L. All further steps were carried out at 4°C. After centrifugation, 5 g of the cell pellet were resuspended in fourfold volume of buffer 1 (50 mM MES/NaOH, pH 6.0, 50 mM NaCl, 0.1 mM PMSF supplemented with desoxyribonuclease I) and disrupted by passing twice through a French Pressure Cell Press (110 MPa, SLM-Aminco). Cell debris and non-disrupted cells were removed by centrifugation (9500 × g, 20 min, 4°C, Rotor A8.24, RC-5 Superspeed Refrigerated Centrifuge, Sorvall Instruments). The cytoplasmic membranes were obtained from the supernatant by centrifugation at 252000 × g (60 min, 4°C, Rotor 70.1Ti, L8-M Ultrafuge, Beckman). The sediment was suspended in an equal volume (1:1, w/v) of buffer 1 and was used directly or frozen in liquid nitrogen and stored at -80°C.
10
Purification of His-tagged Proteins from E. coli
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Proteins bearing an N-terminal, TEV-cleavable His6-tag were produced in E. coli Rosetta 2 (DE3) or E. coli BL21 (DE3) RIL cells in auto-inducing ZY medium [58 (link)] for 24 h at 18 °C. The following steps were performed at 4 °C. Cells were resuspended in solubilization buffer (50 mM sodium phosphate, pH 8.0, 500 mM NaCl, 30 mM imidazole, 5 mM β-mercaptoethanol) and lyzed using an EmulsiFlex-C5 cell homogenizer (Avestin). The soluble fraction was separated from the insoluble fraction by centrifugation for 30 min at 55,900 x g in an Avanti J-26 XP centrifuge (Beckman Coulter). Target proteins were captured on Ni2+-NTA resin (GE Healthcare), washed with solubilization buffer and eluted with elution buffer (250 mM imidazole, pH 8.0, 300 mM NaCl, 5 mM β-mercaptoethanol). Tags were cleaved with 1:50 TEV during overnight dialysis against 10 mM sodium phosphate, pH 8.0, 300 mM NaCl, 30 mM imidazole, 5 mM β-mercaptoethanol, and cleaved samples were again passed over Ni2+-NTA resin. The flow-through was collected, concentrated, and subjected to size exclusion chromatography (SEC) in SEC buffer (10 mM Tris-HCl, pH 8.0, 300 mM NaCl, 0.1 mM EDTA, 1 mM DTT) using Superdex 75 and Superdex 200 columns (GE Healthcare). Peak fractions were analyzed by SDS-PAGE. Fractions containing the target protein were pooled, concentrated, and shock-frozen in liquid nitrogen.
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