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Reax 2

Manufactured by Heidolph
Sourced in Germany

The Reax 2 is a laboratory shaker designed for gentle mixing and agitation of samples. It features a compact and sturdy construction, allowing for reliable and consistent performance in laboratory settings.

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14 protocols using reax 2

1

Feather Extraction for Analyte Analysis

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Weigh 1 g of feathers (approximately three large wing feathers) into a 50 mL polypropylene (PP) centrifuge tube (Greiner Bio-One, Alphen aan de Rijn, The Netherlands). Add internal standard solution and 2 mL of 0.125% TFA in MeOH to all samples. Shake thoroughly by hand and add 16 mL of McIlvain-EDTA buffer. Shake for 60 min using a rotary tumbler (Heidolph REAX-2, Schwabach, Germany) and centrifuge for 5 min at 3500 g. From here, extracts are submitted to sample clean-up.
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2

Extraction and Analysis of E-Liquids

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A 1-mL volume of the e-liquids bought during the monitoring of the online market was extracted by adding 1 mL of methanol and 1 mL n-hexane using an overhead shaker for 5 min at lowest rotation speed (Reax 2; Heidolph, Schwabach, Germany). Subsequently, samples were centrifuged at 2860 × g for 5 min (Heraeus Megafuge 1.0; Thermo Scientific, Schwerte, Germany). Ten microliters of the supernatant were evaporated to dryness at 40 °C under a gentle stream of nitrogen. Prior to analysis by the GC–MS system (injection volume 1 µL), the samples were reconstituted in 100 µL of dry ethyl acetate.
For NMR analysis, 1 mL of an e-liquid was extracted five times using n-hexane/ethyl acetate (99:1, v/v). The combined supernatants were evaporated to dryness and resulted in 4 mg of a raw extract containing 5F-Cumyl-PINACA, which was used for structure elucidation by NMR spectroscopy.
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3

Extraction of Milk Contaminants

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The sample preparation is summarized in Fig. 2. Apparatus: Overhead shaker: Reax 2, Heidolph Instruments (Schwabach, Germany); Centrifuge: Heraeus Megafuge 16, Thermo Fisher Scientific (Waltham, USA); Syringe Filter: Perfect-Flow, Wicom (Heppenheim, Germany); Turbovap: TurboVap LV, Zymark (MA, USA).

Extraction of HGA, MCPrG and their metabolites from raw milk

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4

Extraction of Birch Pollen Proteins

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Birch pollen (Betula Pendula) was purchased from Allergon (Allergon AB, Ängelholm, Sweden). Proteins were extracted from birch pollen with Tris-Borate buffer (8mM Tris with 10mM (NH4)2B10O16; pH8.5; in 1/10 w/v ratio) for 6h at 4°C at 500 rpm (Reax 2, Heidolph Instruments Schwabach, Germany), followed by centrifugation at 16 000 g, and filtration using a 0.22μm nitro cellulose membrane (Sartorius AG, Goettingen, Germany). The protein concentration was determined by the Bradford assay using bovine serum albumin as standard. The extract was stored at -80°C.
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5

Activated Sludge Floc Disintegration

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Astacus reagent ultrapure water system (P/N 110-000, membraPure, Henningsdorf, Germany)

8-Channel pipette, variable volumes (20 - 200µL) (P/N 613-5252, VWR, Darmstadt, Germany), for reagent and sample dosage into the plate wells

End-over-end shaker (REAX2, Heidolph, Berlin, Germany) for coarse dispersion of the sludge samples

Ultra-sonication bath (BANDELIN Electronic, Germany), frequency 35 kHz, operated at 70% of the maximum energy output, for the fine dispersion and disintegration of activated sludge flocs.

Synergy HT plate reader (Bio-Tek Instruments, Bad Reichenhall, Germany), controlled by the Gen5 software (Bio-Tek Instruments), for microplate reading of the 4-MUF fluorescence at excitation wavelength of 360 nm and emission wavelength of 460 nm. Gain settings (70 – 60) depended on sludge dilution, substrate concentration and recording period. Main fixed operation parameters were: top optics position with a top probe vertical offset of 1.00 mm, normal read speed, and thermostatic control of the plates at 30°C.

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6

Recrystallization of S-layer Proteins on Emulsomes

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1 mg lyophilized S-layer protein was dissolved in 1 mL 5 M GHCl 50 mM Tris/HCl buffer (pH 7.2). The solutions were dialysed against distilled water at least 24 h at 20 °C. For recrystallization of the S-layer protein on emulsomes, the S-layer protein solution was mixed with the emulsome suspension and diluted with Milli-Q water to achieve final protein and DPPC concentrations of 300 μg mL−1 and 150 μg mL−1, respectively. Recrystallization of the S-layer protein was carried out for 3 h at room temperature in a test tube rotator (REAX2, Heidolph, Germany) with a rotation speed of 32–36 rpm. Excess non-assembled S-layer protein was removed by centrifugation at 14,100 × g for less than 1 min. The pellet containing the S-layer coated emulsomes was resuspended in Milli-Q water and stored at 4 °C until further analysis.
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7

Quantifying Nitrate and Ammonium in Soil

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For the determination of the nitrate concentrations in the two soil habitats, one gram of soil was diluted with two milliliters of deionized water, mixed in an overhead shaker (Reax 2, Heidolph Instruments, Schwalbach, Germany) and centrifuged at 16.249 × g (Mikro 20, Hettich GmbH, Tuttlingen, Germany). The supernatant was filtered through a 0.2 µm regenerated cellulose membrane (Rotilabo, Carl Roth GmbH & Co. KG, Karlsruhe, Germany) and analyzed by ion chromatography [42 (link)]. For the analyses of the ammonium concentrations in the two soil habitats, two grams of soil were extracted with 8 mL 1 M KCl, and the concentration was determined by a colorimetric assay [43 (link)].
pH values of soil solutions (extraction with 0.01M CaCl2) were measured with a pH meter (Ino Lab pH 720, WTW 82362 Weilheim, Germany).
Statistical comparisons were done with ANOVA and Tukey HSD Test, using SPSS version 20. The model included the factors “treatment”, “soil habitat”, their interaction, and “block” as a random factor. The main effect of factors “mineral-N” and “Manure” was also tested.
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8

Polystyrene Foam Preparation via Powder Mixing

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The polystyrene PS168N pellets were grinded in a ZM200 freezer mill (Retsch, Haan, Germany) using a mesh size of 1000 μm at a rotation speed of 18.000 rpm. The powdered PS was mixed with 1.0 wt.% (batch foaming) or 5.0 wt.% (extrusion foaming) of the finely powdered corresponding kinked bisamide. A Reax 2 overhead shaker (Heidolph, Schwabach, Germany) was used for 24 h at 50 rpm to achieve a homogeneous powder–powder mixture of the PS and kinked bisamides.
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9

Peanut Roasting and Oil Extraction

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In a ULM 500 drying oven (Memmert, Schwabach, Germany) pre-tempered to (170 ± 2) °C, 50 g of raw, unroasted peanuts with shell were distributed on an aluminium foil and roasted for 20 min or 40 min, respectively. After cooling at room temperature, the peanuts were shelled, the seed coats were removed, and the peanuts were ground at 5000 rpm for a few seconds using the Grindomix 100 food processor (Retsch, Haan, Germany) and stored in the freezer at -21 °C [12] (link). The fat content was analysed using the Weibull-Stoldt method [18] . For the cold extraction of the peanut oil, about 3.0 g of peanuts were weighed into a 50 mL Greiner tube, mixed with 30 mL diethyl ether, and placed in the overhead shaker REAX 2 (Heidolph, Schwabach) for 1.5 h at room temperature. After subsequent filtration (Whatman 595.5), the solvent was completely rotated off under vacuum at 40 °C and 600 mbar. 2.0 g of native peanut oil were heated by the rancimat 892 professional (Methrom, Herisau, Switzerland) under an oxygen flow of 20 L/h at 170 °C for 20 min and 40 min [15] (link).
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10

Pharmaceutical Adsorption Experiments

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Batch adsorption experiments were performed by contacting the adsorbents (AAC or CAC) with solutions of pharmaceutical (CBZ, SMX or PAR) prepared either in ultrapure or in the collected wastewater. Pharmaceutical solutions of CBZ, SMX or PAR, with an initial concentration (C0) of 5 mg L -1 were shaken together with a known concentration (M) of the corresponding adsorbent in polypropylene tubes. The tubes were shaken in a head-over-head shaker (Heidolph, Reax 2) at 80 rpm, under controlled temperature (25.0 ± 0.1 ºC). After shaking, solutions were filtered through 0.2 µm PVDF filters (Whatman) and analysed for the residual concentration of pharmaceutical by micellar electrokinetic chromatography (MEKC) (as described in section 2.6).
Control experiments, i.e. the pharmaceutical solution in absence of adsorbent, were run in parallel. All experiments were run in triplicate.
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