The optical characterization of Ag NPs was performed by UV-visible spectroscopy scanning in the 300–1100 nm wavelength range. The spectra obtained were measured using a Shimazdu UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan) with a 1 cm quartz cell at room temperature.
Uv 1700 pharmaspec spectrophotometer
Manufactured by Shimadzu
Sourced in Japan
The UV-1700 PharmaSpec spectrophotometer is a laboratory instrument designed for the measurement and analysis of ultraviolet and visible light absorption spectra. It is a versatile tool capable of performing quantitative and qualitative analysis of various samples.
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Lab products found in correlation
Lightcycler 480, by Roche (5 mentions)
Mirneasy mini kit, by Qiagen (5 mentions)
Qiazol reagent, by Qiagen (4 mentions)
Sybr green 1, by Promega (4 mentions)
Miscript 2 rt kit, by Qiagen (4 mentions)
Itaq polymerase, by Promega (3 mentions)
Evolution capt software, by Vilber (2 mentions)
Phosphatase inhibitor cocktail 2, by Merck Group (2 mentions)
Sunfire prep c18 obd 5 m 30 150 mm column, by Waters Corporation (2 mentions)
1260 series instrument, by Waters Corporation (2 mentions)
Power wave xs elisa reader, by Agilent Technologies (1 mentions)
Cx31 microscope, by Olympus (1 mentions)
Protein assay reagent, by Bio-Rad (1 mentions)
Sybr green 1 kit, by Promega (1 mentions)
Fusion solo system, by Vilber (1 mentions)
Cytochrome oxidase activity colorimetric assay kit, by Abcam (1 mentions)
Nitrocellulose membrane, by Cytiva (1 mentions)
Femto reagent, by Thermo Fisher Scientific (1 mentions)
Fusion solo, by Vilber (1 mentions)
Jem 1400, by JEOL (1 mentions)
40 protocols using uv 1700 pharmaspec spectrophotometer
1
Optical Characterization of Silver Nanoparticles
2
Spectroscopic Characterization of Thin Gels
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UV-VIS spectra of thin gels were recorded on a Shimadzu UV-1700 PharmaSpec spectrophotometer and processed using UV-Probr 2.31 software, Shimadzu Corporation. The spectrophotometer was also used for estimation of solute absorbances at particular wavelengths. Absorbances in the wells of microtiter plates were measured using a Power Wave XS ELISA reader (BIO-TEK Instruments, USA). An Olympus CX31 microscope equipped with an Infinity 3 Luminera digital CCD camera was used to take micrographs of wet cryogels made on the surface of glass slides. FTIR spectra were recorded on a Nicolet 6700 instrument with a Smart ITR accessory using 16 scans, a standard KBr beam splitter, the spectral range of 5000–400 cm−1, and resolution of 4 cm−1. All spectra were processed and analyzed using the OMNIC™ 8 Spectra Software. Cryogel sample preparation for FTIR-spectroscopy was the same as for electron microscopy, see Section 2.3.6 .
3
Quantifying Soluble Proteins in NWL and SWL
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The determination of the total soluble proteins content in NWL and SWL was carried out by Bradford’s method using the BioRad Protein Assay reagent [31 (link)]. Bovine serum albumin (BSA) was used as standard. To prepare the BSA standard solution, 2.8 mg of BSA were weighed and dissolved in 1 mL of deionized water. To obtain a concentration of 0.1 mg/mL, 20 μL of solution were diluted with 540 μL of water. The calibration curve was obtained using 6 dilutions of BSA. The equation relative to the calibration curve obtained from the absorbance read by the spectrophotometer and related to the BSA standard solution concentration is y = 0.0481x + 0.075 (R2 = 0.998). The absorbances (595 nm) were measured at 15 min and one hour after sample preparation. For the measurements, a SHIMADZU UV-1700 PharmaSpec spectrophotometer (Kyoto, Japan) was used. This analysis was performed on the sample supernatants after centrifugation at room temperature at 4000 rpm for 15 min in a Heraeus Megafuge 1.0R (Kendro Laboratory Products GmbH, Hamburg, Germany). The lyophilized supernatants were suspended in water, and the difference between the supernatant of the NWL and SWL was evaluated.
4
In Vitro Drug Release Kinetics
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To study drug release, VFS (pH 4.2 and temperature 37 ± 1 °C) was used as the release medium to simulate the physiological characteristics of the vaginal environment (acidic pH due to the presence of lactic acid and body temperature) [37 (link)].
10 mg of the sample was placed in a plastic tube with a dialysis membrane attached to the end. The tube was immersed in a glass containing 30 mL of VFS (37 ± 1 °C) under constant stirring. At intervals (0.5, 1, 2, 3, 5, 7, 10, and 24 h), 2 mL of the release medium was sampled for spectrophotometric determination of MET concentration at 320 nm with a calibration curve using a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan). The sampled volume was replaced with 2 mL of fresh VFS. Each sample was tested in triplicate (n = 3).
10 mg of the sample was placed in a plastic tube with a dialysis membrane attached to the end. The tube was immersed in a glass containing 30 mL of VFS (37 ± 1 °C) under constant stirring. At intervals (0.5, 1, 2, 3, 5, 7, 10, and 24 h), 2 mL of the release medium was sampled for spectrophotometric determination of MET concentration at 320 nm with a calibration curve using a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan). The sampled volume was replaced with 2 mL of fresh VFS. Each sample was tested in triplicate (n = 3).
5
Quantifying miRNA and Gene Expression
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Total RNA was extracted 24 h after transfection using miRNeasy Mini Kit and Qiazol reagent (Qiagen) according to the manufacturer’s protocol. RNAs quality and quantity were verified by gel electrophoresis and a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Japan). The iTaq polymerase (Promega) and SYBR Green I kit were used to determine the expressions of miRNAs and other target genes by qRT-PCR in LightCycler 480 (Roche Applied Science, Penzberg, Germany) using 2−ΔΔCt method with normalization to U6. The sequences of all primers and reaction conditions used for RT-PCR and qRT-PCR are described in Table S2 .
6
Antioxidant Activity Evaluation of Essential Oils
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Several in vitro assays were employed for the assessment of the antioxidant activity of the examined EOs, namely: (i) interaction with the free stable radical DPPH (1,1-diphenyl-2-picrylhydrazyl), (ii) ABTS (2,2′-azino-bis (3-ethylbenzothiazoline-6-sulfonic acid)) radical cation decolorization assay, and (iii) FRAP (ferric-reducing antioxidant power). In all of the aforementioned assays, the EO samples were diluted in absolute EtOH at a concentration of 5 mg mL−1 (for the DPPH assay) or 1 mg mL−1 (for the FRAP and the ABTS assays). In all assays, a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan) was used for the absorbance measurement. All experiments were carried out in triplicate and the results were expressed as mean ± standard error.
7
Protein Extraction and Western Blotting
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The total protein was extracted from the transfected cells using a lysis buffer containing 2% Triton-X, 0.2 mM PMSF, and 1% phosphatase inhibitor cocktail II (Sigma-Aldrich, St. Louis, MO, USA). The protein concentrations were assessed via a Bradford assay using a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan) at 595 nM. The samples (20 µg/lane) were then loaded on SDS-PAGE, electrophoresed, incubated with specific primary antibodies (Table S3 ) overnight at 4 °C, and labeled with HRP-conjugated anti-rabbit or anti-mouse IgG antibodies for 1 h. The blots were developed using a Femto commercial kit (Thermo Fisher Scientific) with a Fusion Solo system (Vilber, Marne-la-Vallée, France). The intensities of the blots were analyzed with Evolution Capt software (Vilber).
8
Cytochrome Oxidase Activity Assay
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The activity of cytochrome oxidase in IMQ-treated and untreated cells was analyzed by Cytochrome Oxidase Activity Colorimetric Assay Kit (BioVision) that was performed according to manufacturer's instruction. In short, the cells were maintained in 6-well plates and treated with or without IMQ. After the indicated time points, total cell lysate were harvested. For each reaction, the 30 μg cell lysate was mixed with 120 μl of reduced cytohrome c. We measured the reduction in absorption at the wavelength of 550 nm using UV/Vis UV-1700 PharmaSpec spectrophotometer (Shimadzu, Benelux BV, Hertogenbosch, The Netherlands) over a period of 30 ~ 45 minutes. The reduced absorbance was normalized to the amount of protein and the difference in time. The reduced absorbance of untreated group was as 1 fold.
9
Quantitative RT-PCR Analysis of C2C12 Cells
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Qiazol reagent (Qiagen, Hilden, Germany) was used to isolate total RNAs from C2C12 cells. RNA quality and purity were confirmed using a miRNeasy Mini Kit (Qiagen), and RNA concentrations were determined using a UV-1700 PharmaSpec spectrophotometer (Shimadzu, Kyoto, Japan). cDNA was prepared with reverse transcription using a miScript II RT Kit (Qiagen) and subjected to qRT-PCR in a Light Cycler 480 (Roche Applied Science, Penzberg, Germany) using SYBR Green I (Promega, Madison, WI, USA). Reaction conditions and the sequences of primers used for qRT-PCR are listed in Table S2 . Relative gene expressions were calculated using the 2−ΔΔCt method, and U6 was used as the internal control.
10
Quantitative Western Blot Analysis of Proteins
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Total protein was extracted from C2C12 cells using a lysis buffer containing 0.2 mM PMSF, 2% Triton-X, and 1% phosphatase inhibitor cocktail II (Sigma-Aldrich, St. Louis, MO, USA). Protein concentrations were determined using the Bradford assay with a UV-1700 PharmaSpec spectrophotometer (Shimadzu). The protein samples (20 µg/well) were separated by electrophoresis and transferred onto nitrocellulose membranes (Amersham, Braunschweig, Germany). After blocking with 5% skim milk in TTBS solution (1% Tween 20 in TBS) for 1 h, the membranes were incubated with primary antibodies (Table S3 ) overnight at 4 °C, washed with TTBS (6 × 5 min), and developed with a secondary antibody (1:10,000 dilution). The blots were then visualized using Femto reagent (Thermo Fisher Scientific, Waltham, MA, USA) and the analytical scanning system Fusion Solo (Vilber, Marne-la-Vallée, France), and the densities of blots were analyzed with Evolution Capt software (Vilber).
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