Polysaccharides were dissolved in water to a final concentration of 25 mg/mL (up to 4 mL) for Heparin and dextranS and 5 mg/mL for λ-Carrageenan due to its low solubility. The reaction mixture was sonicated using a 3-mm diameter probe-type UP50H ultrasonicator (Hielscher, Teltow, Germany) (micro tip MS3), which provided an amplitude of 180 µm. The processor generated mechanical longitudinal vibrations with a frequency of 30 kHz that were produced by electrical excitation. With the reaction mixture at room temperature, the sonic pulses maintained a temperature of 60 °C in the reactor. Hydrogen peroxide 30% was added to obtain a final hydrogen peroxide/polysaccharide (w/w) ratio of 0.15. After 8 h of depolymerization, the reaction mixture was lyophilized prior to Glycol splitting.
Up50h ultrasonicator
Manufactured by Hielscher
Sourced in Germany
The UP50H ultrasonicator is a laboratory device designed for cell disruption, homogenization, and emulsification. It operates at a frequency of 30 kHz and provides a maximum power output of 50 watts.
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Lab products found in correlation
6 protocols using up50h ultrasonicator
1
Polysaccharide Depolymerization via Sonication
2
Ethanolic Extraction of R. salina Pigments
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Pigments were extracted from the lyophilized biomass (2 g) in absolute ethanol (500 ml). The mixture was sonicated at 50 W-30 kHz (UP50H ultrasonicator, Hielscher Ultrasonics GmbH, Germany) for 30 min, on ice and under constant stirring (Haguet et al., 2017) (link). The extractive solution was filtered (PVDF 0.22 μm membrane) and the solvent was evaporated under vacuum, resulting in the R. salina extract (Rs-EtOH, 0.53 g).
3
Extraction of Cellular Lysate for Biochemical Analysis
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To obtain the cellular lysate, at each tested time point, 3D models were collected from culture plates and centrifuged for 5 min at 1500 rpm. The cell pellets were then washed and resuspended in phosphate-buffered saline (PBS) solution. Further, the cellular models were sonicated for 30 s, three times on ice using a UP50H ultrasonicator (Hielscher Ultrasound Technology, Teltow, Germany) at 80% amplitude. The samples were then centrifuged for 10 min, 3000 rpm, 4 °C, and the supernatants were collected and used for further determinations. The protein concentration was measured using the Bradford method and bovine serum albumin (BSA) as standard protein.
4
Cell Lysis and Protein Quantification
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The breast adenocarcinoma and normal MRC-5 cells were collected from culture dishes after treatment and centrifuged for 5 min at 1500 rpm. Cell sediment was washed and then resuspended in PBS. Cells lysis was obtained by sonication on ice, three times for 30 s using a UP50H ultrasonicator (Hielscher Ultrasound Technology, Teltow, Germany) at 80% amplitude, 1 cycle. After the centrifugation (10 min, 3000 rpm, 4 °C), the supernatant was collected and used for further determinations. The protein concentration was measured by Bradford method using BSA as standard protein [27 (link)].
5
RAW 264.7 Cell Lysis and Protein Quantification
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RAW 264.7 cells were seeded in 75 cm2 culture flasks at a density of 2 × 106 cells/flask. After treatment with NPs, the cell suspensions were centrifuged for 5 min at 1500× g rpm, and the cellular pellets were washed and resuspended in PBS. Cell lysis was obtained through ultrasonication 3 times for 30 s each, on ice, using a UP50H ultrasonicator (80% amplitude, 1 cycle) from Hielscher Ultrasound Technology (Teltow, Germany). The total extract was centrifuged at 3000× g rpm for 10 min at 4 °C, and the supernatants were collected. The protein concentration in each sample was measured using the Bradford method and a calibration curve of bovine serum albumin (BSA) ranging from 0 to 1.5 mg/mL protein.
6
Protein Extraction from MDA-MB-231 Cells
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For the protein extraction protocol, MDA-MB-231 cells were seeded in 75 cm2 culture flasks at a density of 106 cells/flask and treated with two different doses of CDDP (0.316 and 0.632 μg/mL), SWCNT-COOH (0.5 and 1 μg/mL), and SWCNT-COOH-CDDP (0.5 + 0.316 and 1 + 0.632 μg/mL). After 24 and 48 h of treatment, the monolayer cultures were enzymatically detached from the culture flasks, the cell suspensions were centrifuged for 5 min, at 1500 rpm, and the cellular pellets were washed and resuspended in phosphate buffer saline (PBS).
Cell lysis was produced on ice, through ultrasonication (three times, 30 s), using a UP50H ultrasonicator (80% amplitude, 1 cycle, Hielscher Ultrasound Technology, Teltow, Germany). Then, the lysates were centrifugated (10 min, at 3000 rpm, 4 °C) and the resultant supernatants were collected and used for protein expression analysis. The protein concentration of the samples was estimated using Bradford reagent and a standard curve of 0–1.5 mg/mL bovine serum albumin (BSA).
Cell lysis was produced on ice, through ultrasonication (three times, 30 s), using a UP50H ultrasonicator (80% amplitude, 1 cycle, Hielscher Ultrasound Technology, Teltow, Germany). Then, the lysates were centrifugated (10 min, at 3000 rpm, 4 °C) and the resultant supernatants were collected and used for protein expression analysis. The protein concentration of the samples was estimated using Bradford reagent and a standard curve of 0–1.5 mg/mL bovine serum albumin (BSA).
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