For ICC, myotubes were fixed in 4% (w/v) paraformaldehyde (Biosesang) and permeabilized with TRIS‐buffered saline containing 0.1% (v/v) Tween 20 (Sigma‐Aldrich). For immunohistochemistry (IHC), after necropsy, skeletal muscle tissues were frozen using isopentane (Thermo Fisher Scientific) cooled by liquid nitrogen. Frozen sections with a thickness of 10 μm were prepared and mounted onto slides. Immunostaining was performed using primary antibodies specific to myosin heavy chain proteins. Subsequently, secondary antibodies (Table S1 ) were applied and counterstained with DAPI (Sigma‐Aldrich). Images were captured and analysed using Cytation 5 (BioTek), and the fluorescence intensity of each MYH was normalized to the DAPI signal.
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Tween 20 is a non-ionic detergent commonly used in biochemical applications. It is a polyoxyethylene sorbitan monolaurate, a surfactant that can be used to solubilize and stabilize proteins and other biomolecules. Tween 20 is widely used in various laboratory techniques, such as Western blotting, ELISA, and immunoprecipitation, to prevent non-specific binding and improve the efficiency of these assays.
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8 916 protocols using tween 20
1
Immunostaining of Myosin Heavy Chains
2
Chondrocyte Differentiation Protocol
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Ascorbate 2-phosphate, β-glycerophosphate, paraformaldehyde (PFA), trypsin–EDTA, 2-amino-2-methyl-1-propanol (AMP), o-cresolphthalein complexon, 8-Hydroxyquinoline, Bovine serum albumin (BSA), Safranin O, Tween20, Kolliphor®P188 were obtained from Sigma (Taufkirchen, BY, Germany). L-Prolin, sodium-pyruvate, acetic acid, hydrochloric acid (HCl) and crystal violet were received from Roth (Karlsruhe, BW, Germany). Protease inhibitor cocktail, DAPI and insulin were bought from Roche (Mannheim, BW, Germany). Resazurin was purchased from Santa Cruz Biotechnology (Heidelberg, BW, Germany). Fetal bovine serum (FBS) was from Capricorn Scientific (Ebsdorfergrund, HE, Germany). ITS-G premix, high / low glucose medium (4.5 g/L) and Dulbecco’s Modified Eagle’s medium (DMEM/F-12) were obtained from Life Technologies (Darmstadt, HE, Germany). ∆9-tetrahydrocannabinol (Dronabinol) was bought from LGC (Wesel, NW, Germany). Collagenase (type I) was purchased from Worthington Biochemical Corp. (Lakewood, NJ, USA). Transforming growth factor-β3 (TGF-β3) was obtained from PeproTech (Hamburg, HH, Germany). 2-propanol and Oil Red O was bought from Merck (Darmstadt, HE, Germany).
3
Immunostaining of Myosin Heavy Chains
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For ICC, myotubes were fixed in 4% (w/v) paraformaldehyde (Biosesang) and permeabilized with TRIS‐buffered saline containing 0.1% (v/v) Tween 20 (Sigma‐Aldrich). For immunohistochemistry (IHC), after necropsy, skeletal muscle tissues were frozen using isopentane (Thermo Fisher Scientific) cooled by liquid nitrogen. Frozen sections with a thickness of 10 μm were prepared and mounted onto slides. Immunostaining was performed using primary antibodies specific to myosin heavy chain proteins. Subsequently, secondary antibodies (Table S1 ) were applied and counterstained with DAPI (Sigma‐Aldrich). Images were captured and analysed using Cytation 5 (BioTek), and the fluorescence intensity of each MYH was normalized to the DAPI signal.
4
Kinetics and Modulators of FHR Dimerization
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To study the kinetics of dimer formation, equimolar amounts of native FHR-1 and -2 in EDTA plasma deficient in either FHR-1 or -2 were incubated for a range of time points (zero minutes to overnight) at 37 °C. After incubation, samples were immediately placed on melting ice to halt further dimerization. Next, levels of formed FHR-1/2 heterodimers were determined as described above, with the difference that the sample incubation was carried out on melting ice.
To investigate the impact of pH on homo- and heterodimers, NHS was incubated at pH 6.5 to 9.0. Citric acid monohydrate (Merck Millipore) and 1,3-Bis[tris(hydroxymethyl)methylamino]propane (CBTP, Sigma Aldrich), both 40 mM prepared in an isotonic solution (Versylene® Fresenius, NaCl 0.9%, Fresenius Kabi, Serves, France) containing 0.02% (v/v) Tween®-20 and 0.3% (w/v) BSA (Sigma Aldrich), were used to prepare the pH range. FHR dimer ELISA’s were performed as described above with the only difference the incubation of serum at various pH conditions.
The FHR-1 and -2 dimers were further investigated by adding sodium chloride at indicated final concentrations (0.0625–2 M) during the sample step. FHR dimer assays were conducted and developed as previously described. Possible direct effects of this pH range or the sodium chloride concentration on antibody-antigen binding capacity was excluded using recombinant monomeric FHR proteins (supplemental Fig. 2 a, b).
To investigate the impact of pH on homo- and heterodimers, NHS was incubated at pH 6.5 to 9.0. Citric acid monohydrate (Merck Millipore) and 1,3-Bis[tris(hydroxymethyl)methylamino]propane (CBTP, Sigma Aldrich), both 40 mM prepared in an isotonic solution (Versylene® Fresenius, NaCl 0.9%, Fresenius Kabi, Serves, France) containing 0.02% (v/v) Tween®-20 and 0.3% (w/v) BSA (Sigma Aldrich), were used to prepare the pH range. FHR dimer ELISA’s were performed as described above with the only difference the incubation of serum at various pH conditions.
The FHR-1 and -2 dimers were further investigated by adding sodium chloride at indicated final concentrations (0.0625–2 M) during the sample step. FHR dimer assays were conducted and developed as previously described. Possible direct effects of this pH range or the sodium chloride concentration on antibody-antigen binding capacity was excluded using recombinant monomeric FHR proteins (supplemental Fig. 2 a, b).
5
Cell Fractionation and Membrane Isolation
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Cell fractionation was performed following previous publications41 (link),42 (link). The cells were first resuspended into AS buffer (30 mM HEPES, 15 mM NaCl, 350 mM sucrose, 1 tablet/10 mL EDTA-free protease inhibitor (Roche), pH=7.4) containing 0.015% digitonin (Sigma-Aldrich) and 0.5% Tween-20 (Sigma-Aldrich). The cell suspension was gently triturated 5 times, incubated on ice for 35 min, and centrifuged at 500 × g for 3 min. The supernatant was recovered and transferred to a clean tube labeled as Fraction 1. Then cell pellets were washed with 1 mL of AS buffer and resuspended in AG buffer (30 mM HEPES, 15 mM NaCl, 20% glycerol, 1 tablet/10 mL EDTA-free protease inhibitor, pH=7.4) containing 1% dodecyl maltoside. The operation is the same as above. The supernatant was recovered as Fraction 2. All collected fractions were centrifuged at 16,000 × g for 10 min, and the supernatant was subsequently collected as the cytoplasmic and plasma membrane fractions, respectively. Samples were stored at −20 °C for further analysis.
6
Engineered Nesprin Tension Sensor
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The TEV module was cloned using standard cloning techniques into the nesprin TSmod 25 in pcDNA3.1 (https://www.addgene.org/browse/sequence/244038/ )74 (link). The mCerulean and mVenus sequences were removed and replaced with either the 5 pN or 10 pN sensor leading to an insertion between the N-terminal actin-binding CH domain (1–485) and the C-terminal KASH SUN-binding domain (6525–6874) (Fig. 2l )
U2OS cells were cultured on coverslips and transfected using Lipofectamine 3000 reagent (ThermoFisher) according to the manufacturer’s instructions. Immunoblot protocols were executed as previously described75 (link). Briefly, 10 μg of protein were resolved by 10% SDS–PAGE gels and transferred onto polyvinylidene fluoride membranes (Bio-Rad). Membranes were blocked in 4% (wt/vol) milk in PBS + 0.1% (vol/vol) Tween-20 (Sigma-Aldrich). Primary and horseradish peroxidase-conjugated secondary antibodies were diluted in blocking buffer. A ChemiDoc gel imaging system (Bio-Rad) was used to visualize chemiluminescence.
For immunofluorescence, cells were fixed with 4% PFA/PBS for 15 min, permeabilized with 0.3% Triton X-100/PBS for 3 min, and blocked with 4% BSA/PBS (Sigma-Aldrich) for 1 hour. Coverslips were incubated for one hour with primary antibodies: FLAG (Millipore Sigma F3165, 1:500), HA (Roche 11867423001, 1:500), or LaminA (Invitrogen MA1–06101, 1:500). Samples were washed 2x with PBS for 5 min, incubated with Alexa Fluor (Life Technologies) secondary antibodies for one hour, and then washed 3x with PBS and mounted with ProLong Gold Antifade reagent + DAPI (Thermo Fisher P36935). Images were acquired on an LSM 880 laser scanning confocal microscope (Zeiss) with Airyscan using a C Plan-Apochromat 63×/1.40 oil DIC M27 objective using ZEN 2.1 software (Zeiss).
U2OS cells were cultured on coverslips and transfected using Lipofectamine 3000 reagent (ThermoFisher) according to the manufacturer’s instructions. Immunoblot protocols were executed as previously described75 (link). Briefly, 10 μg of protein were resolved by 10% SDS–PAGE gels and transferred onto polyvinylidene fluoride membranes (Bio-Rad). Membranes were blocked in 4% (wt/vol) milk in PBS + 0.1% (vol/vol) Tween-20 (Sigma-Aldrich). Primary and horseradish peroxidase-conjugated secondary antibodies were diluted in blocking buffer. A ChemiDoc gel imaging system (Bio-Rad) was used to visualize chemiluminescence.
For immunofluorescence, cells were fixed with 4% PFA/PBS for 15 min, permeabilized with 0.3% Triton X-100/PBS for 3 min, and blocked with 4% BSA/PBS (Sigma-Aldrich) for 1 hour. Coverslips were incubated for one hour with primary antibodies: FLAG (Millipore Sigma F3165, 1:500), HA (Roche 11867423001, 1:500), or LaminA (Invitrogen MA1–06101, 1:500). Samples were washed 2x with PBS for 5 min, incubated with Alexa Fluor (Life Technologies) secondary antibodies for one hour, and then washed 3x with PBS and mounted with ProLong Gold Antifade reagent + DAPI (Thermo Fisher P36935). Images were acquired on an LSM 880 laser scanning confocal microscope (Zeiss) with Airyscan using a C Plan-Apochromat 63×/1.40 oil DIC M27 objective using ZEN 2.1 software (Zeiss).
7
Cannabinoid-Infused Hydrogel Formulation
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The dried Artemisia annua L. herbs were purchased from UAB “Žolynų Oazė” (Vilkaviškio raj, Lithuania). Cannabis seed oil was purchased from UAB “Strazdų žaliasis auksas” (Širvintų raj, Lithuania). The chemicals used for this research were acetic acid 99.8–110.5% purchased from Honeywell Fluka (Seelze, Germany); calcium chloride and medium-molecular-weight (MMW) chitosan (degree of deacetylation (DDA): approximately 75–85%; molecular weight: 190,000–310,000 Da) purchased from Sigma-Aldrich (Darmstadt, Germany); crystal-resistant distillate cannabidiol (CBD) purchased from Fitodenta (Kaunas, Lithuania); 96% ethanol (Vilnius, Lithuania), L-glutathione ≥ 98% (ROTH, Karlsruhe, Germany), phosphate-buffered saline (PBS) solution, and sodium alginate (molecular weight: 80,000–120,000 Da) purchased from TCI (Zwijndrecht, Belgium); Span 80 and Tween 20 purchased from Sigma-Aldrich (Steinheim am Albuch, Germany).
8
Biocidal Effects of Essential Oils on Phototrophic Biofilms
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The EOs were tested at 0.5% and 5% (v/v) concentrations as biocides against phototrophic microorganisms. This range was chosen as previous research has shown that EOs was effective at concentrations between 5 and 1% (v/v) (Bruno et al. 2019 (link); Gabriele et al. 2023 (link); Ranaldi et al. 2022 (link)). The range applied was chosen in order to assess the possibility of further reducing the minimum applicable concentration and to compare the results with previous studies. The solutions were prepared in distilled water (DM) and TWEEN20 (Sigma-Aldrich) (1% v/v).
BG11 biomass was centrifuged (10 min at 5000 g) and the supernatant discharged. One millilitre of the biomass (OD = 2.648 ± 0.056) was transferred to BG11 agar Petri dishes and incubated in growth chamber for 2 months (T = 22 ± 2 °C; irradiance = 10 μmol photons m2/s⁻1; photoperiod: 12 h light/dark), until the surface was fully covered with the phototrophic biofilm. According to Ranaldi et al. (2022 (link)), circular fragments (~ 1.5 cm in diameter) were cut from the biofilm and transferred to new agar plates. These plates were maintained under the same controlled conditions throughout the experiment. The EOs were applied by pipetting 200 μL of each one (~ 1 μL/cm2) onto the biofilm on the Petri dishes. Two different classes of commercially available biocides were used as positive controls: BIOBAN™ 104 Antimicrobial (CTRL + B) (Dow Chemical Company, MI, USA.), concentrated, stable blend of octylisothiazolinone and quaternary ammonium compound (QUAC-OIT), was tested as 3% (v/v) solution in DM, and ESSENZIO© (CTRL + E) (IBIX BIOCARE, Lugo, Ravenna, Italy), a blend of oregano and thyme EOs, tested as supplied (100% v/v). DM was used as negative control (CTRL −). Tests were performed in triplicate. The efficacy of each treatment was assessed by microscope observation and measuring photosynthetic activity using a portable pulse amplitude fluorometer (PAM).
BG11 biomass was centrifuged (10 min at 5000 g) and the supernatant discharged. One millilitre of the biomass (OD = 2.648 ± 0.056) was transferred to BG11 agar Petri dishes and incubated in growth chamber for 2 months (T = 22 ± 2 °C; irradiance = 10 μmol photons m2/s⁻1; photoperiod: 12 h light/dark), until the surface was fully covered with the phototrophic biofilm. According to Ranaldi et al. (2022 (link)), circular fragments (~ 1.5 cm in diameter) were cut from the biofilm and transferred to new agar plates. These plates were maintained under the same controlled conditions throughout the experiment. The EOs were applied by pipetting 200 μL of each one (~ 1 μL/cm2) onto the biofilm on the Petri dishes. Two different classes of commercially available biocides were used as positive controls: BIOBAN™ 104 Antimicrobial (CTRL + B) (Dow Chemical Company, MI, USA.), concentrated, stable blend of octylisothiazolinone and quaternary ammonium compound (QUAC-OIT), was tested as 3% (v/v) solution in DM, and ESSENZIO© (CTRL + E) (IBIX BIOCARE, Lugo, Ravenna, Italy), a blend of oregano and thyme EOs, tested as supplied (100% v/v). DM was used as negative control (CTRL −). Tests were performed in triplicate. The efficacy of each treatment was assessed by microscope observation and measuring photosynthetic activity using a portable pulse amplitude fluorometer (PAM).
9
Nanocelluloses and Biopolymer-Based Films
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Nanocelluloses used in the study were gNCC (Navitas, Podcerkev, Slovenia) and pNCC (Celluforce, Montreal, QC, Canada). For natural polymers, sodium alginate Protanal® LF 10/60 (ALG) (FMC BioPolymer, Philadelphia, PA, USA), pectin (PEC) (Sigma–Aldrich, St. Louis, MO, USA), and chitosan from low-viscous shrimp shells (CHI) (both from Sigma–Aldrich, St. Louis, MO, USA) were used. IBU was sourced from Fagron (Rotterdam, The Netherlands) and glycerol from Pharmachem Sušnik (Ljubljana, Slovenia). Acetic acid (Merck, Darmstadt, Germany) was added to chitosan-based casting dispersions. Capryol® 90 from Gattefosse (Saint-Priest, France), as well as Kolliphor® EL from BASF (Ludwigshafen, Germany), served as SMEDDS components. Additionally, a solubility study of IBU was performed using the following excipients: oleic acid (Sigma–Aldrich, St. Louis, MO, USA), castor oil (Caesar & Loretz GmbH, Hilden, Germany), Capmul MCM C8 (ABITEC Corporation, Columbus, OH, USA) Tween 20 (Merck, Darmstadt, Germany), Tween 80 (Sigma–Aldrich, St. Louis, MO, USA), Labrasol (Gattefosse, Saint-Priest, France), and Labrafil M2125 CS (Gattefosse, Saint-Priest, France). For High-Performance Liquid Chromatography (HPLC) analysis, all reagents used acetonitrile (Fischer Scientific, Radnor, PA, USA), as well as the sodium hydroxide and sodium dihydrogen phosphate (Merck, Darmstadt, Germany), were analytical grade.
10
Cannabidiol-based Formulation Development
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Cannabidiol was purchased from Medcolcanna Organics Inc. (Calgary, AB, Canada), refined hemp oil from Molpharma (Ustroń, Poland), Glycerol from PPH Micropharm (Zabierzów, Poland), SLS, and α-Tocopherol from Sigma-Aldrich (St. Louis, MO, USA). The soybean phospholipids (Lipoid P 75) and the egg yolk phospholipids (Lipoid E 80) were very kindly gifted by Lipoid GmbH (Ludwigshafen, Germany). Kolliphor HS15 and ELP; Tween 20, and 80; sodium deoxycholate were purchased from Sigma-Aldrich (St. Louis, MO, USA). Water for injection was purchased from B. Braun Melsungen AG (Melsungen, Germany). All organic solvents used in the studies were of analytical or high-performance liquid chromatographic grade and were purchased from Avantor Performance Materials Poland (Gliwice, Poland).
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