Quartz cuvette

Manufactured by PerkinElmer

Sourced in United Kingdom

The Quartz cuvette is a laboratory equipment used for spectroscopic analysis. It is made of quartz material and is designed to hold liquid samples for analysis in spectrophotometers or other optical instruments. The quartz cuvette provides a transparent window for the passage of light through the sample, enabling accurate measurements of the sample's absorption or transmission properties.

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Lab products found in correlation

Ls50b luminescence spectrometer, by PerkinElmer (1 mentions) Isotemp 3016, by Thermo Fisher Scientific (1 mentions) Ls55 fluorometer, by PerkinElmer (1 mentions) Lambda 35 uv vis spectrometer, by PerkinElmer (1 mentions) Quartz cuvette, by Starna Cells (1 mentions) Lambda 750, by PerkinElmer (1 mentions) Syringe filter, by Merck Group (1 mentions) Lambda 850 uv vis spectrophotometer, by PerkinElmer (1 mentions)

7 protocols using quartz cuvette

Circular Dichroism Spectroscopy of Protein Complexes

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CD spectra were
recorded using a JASCO J-810 circular dichroism spectropolarimeter
and a quartz cuvette with a path length of 1 mm (PerkinElmer). All
samples were prepared in PBS, 10 mM MgCl₂. The PIC concentrations
were adjusted to 0.2 mg mL ^–1. The optical chamber
of the CD spectrometer was deoxygenated with dry nitrogen for 30 min
before use and kept under nitrogen atmosphere during experiments.
For each spectrum, five scans were accumulated and automatically averaged.

Deshpande S.R., Hammink R., Nelissen F.H., Rowan A.E, & Heus H.A. (2017). Biomimetic Stress Sensitive Hydrogel Controlled by DNA Nanoswitches. Biomacromolecules, 18(10), 3310-3317.

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ANS Binding Assay for Amyloid-beta

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ANS was titrated against 5 μM peptide (WT Aβ42 or each of the mutants) and fluorescence emission spectra were measured using a PerkinElmer LS50B luminescence spectrometer and a QS quartz cuvette of 10-mm path length. The ANS was diluted from a 10 mM stock to a series of concentrations starting from 10 μM up to the point at which saturation of fluorescence was achieved (∼70 to 100 μM, varying according to the peptide titrated against). The excitation wavelength was 380 nm and the emission range was from 400 nm to 600 nm. The excitation slit width was 5 nm and the emission slit width was 10 nm.

Thacker D., Sanagavarapu K., Frohm B., Meisl G., Knowles T.P, & Linse S. (2020). The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils. Proceedings of the National Academy of Sciences of the United States of America, 117(41), 25272-25283.

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Intrinsic Tyrosine Fluorescence Quenching Assay for InsP Binding to Arr1

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To assess InsP binding to Arr1, an intrinsic tyrosine fluorescence quenching assay was performed (Arr1 has 14 Tyr residues/monomer), as done previously (Wilson and Copeland, 1997 (link)). 300 nM Arr1 in 500 µL of Heparin Equilibration Buffer was mixed in a quartz cuvette (PerkinElmer, Waltham, MA) with mini stir bar mixing on low and temperature maintained at 20 °C. A PerkinElmer LS55, coupled to an Isotemp 3016S (Fisher Scientific, Pittsburgh, PA) to regulate temperature, was used to measure fluorescence of samples after serial addition of InsP stocks diluted in the same buffer as the Arr1. Device settings for the scans were Ex/Em range of wavelengths of 275/290–350 nm. A slit width of 7 nm was used with a scan rate of 100 nm per min. Every scan was repeated 3 times, and the emission peak at 305 nm was used for the tyrosine emission wavelength. Percent quench values were adjusted for increasing dilution with additional ligand added 5 µL at a time. Curves were fit to the means of the replicates with one site binding accounting for ligand depletion.

Sander C.L., Luu J., Kim K., Furkert D., Jang K., Reichenwallner J., Kang M., Lee H.J., Eger B.T., Choe H.W., Fiedler D., Ernst O.P., Kim Y.J., Palczewski K, & Kiser P.D. (2021). Structural evidence for visual arrestin priming via complexation of phosphoinositols. Structure (London, England : 1993), 30(2), 263-277.e5.

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FtsZ Polymerization Kinetics Analysis

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A reaction mix was prepared in a cold Eppendorf® tube where SaFtsZ (1 mg/mL) was mixed with the test compound at the desired concentration and a polymerization buffer diluted from a double strength buffer to give a final concentration of 25 mM PIPES pH 6.8, 50 mM KCl and 10 mM MgCl₂. The reaction mix was prepared such that the DMSO concentration remained constant at 2% (v/v). The mix was then added into a quartz cuvette (PerkinElmer®, United Kingdom), and placed in a PerkinElmer® LS 55 fluorometer under the fixed condition of excitation/emission at 350/350 nm, slit width <2 nm, a 1 s read interval. The temperature was calibrated to remain constant at 20 °C. The fluorescence was followed for 300 s to allow equilibration, then polymerization was initiated with the addition of 1 mM GTP. A separate negative control was prepared where 1 mM GDP was added instead of the GTP. The reaction was followed for 600 s.

Chai W.C., Whittall J.J., Song D., Polyak S.W., Ogunniyi A.D., Wang Y., Bi F., Ma S., Semple S.J, & Venter H. (2020). Antimicrobial Action and Reversal of Resistance in MRSA by Difluorobenzamide Derivatives Targeted at FtsZ. Antibiotics, 9(12), 873.

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Amyloid-Beta Binding Assay

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OPE₁²⁻ and MB absorbance and emission spectra were recorded at 1 μM in the presence of varying concentrations of Aβ40 (0, 1, 3 and 5 μM) in pH 7.4 10 mM PB after 30 minutes of incubation in the dark at room temperature. Absorbance spectra were obtained with a Lambda 35 UV/VIS spectrometer (PerkinElmer, Waltham, MA) in a quartz cuvette (PerkinElmer, Waltham, MA). Emission scans were obtained at excitation wavelengths of 390 nm and 660 nm for OPE₁²⁻ and MB, respectively, and were recorded using a PTI QuantaMaster 40 steady state spectrofluorometer (HORIBA Scientific, Edison, NJ) in a quartz cuvette (Starna cells Inc., Atascadero, CA).

Weibel E.R., Taylor C.R, & Hoppeler H. (1991). The concept of symmorphosis: a testable hypothesis of structure-function relationship.. Proceedings of the National Academy of Sciences of the United States of America, 88(22), 10357-10361.

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Spectroscopic Determination of MBP pKa

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Optical spectra were obtained using a Perkin-Elmer Lambda 750 spectrophotometer. Quartz cuvettes (Perkin-Elmer; 1 cm path length) were used; the spectrometer was blanked against Chelex-filtered 50 mM, phosphate buffer, pH 7.5. MBP pK_a values were determined by monitoring the optical spectrum of a 78 μM solution as a function of pH, and fitting the resultant pH-dependent absorbance values to a modified form of the Henderson-Hasselbach equation. Binding assays were conducted by the addition 0.1–3.0 molar equivalents of selected the MBP.

Craig W.R., Baker T.W., Marts A.R., DeGenova D.T., Martin D.P., Reed G.C., McCarrick R.M., Crowder M.W., Cohen S.M, & Tierney D.L. (2017). Substituent Effects on the Coordination Chemistry of Metal-Binding Pharmacophores. Inorganic chemistry, 56(19), 11721-11728.

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Batch Adsorption of Antibiotics on PIM-1

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Batch adsorption experiments for the four different antibiotics were conducted with an initial concentration of 200 µM. Five mL solution of the target antibiotics was mixed and stirred (using magnetic bar at a speed of 400 rpm) with PIM-1 (2 mg) at different adsorption times, pH, and temperatures. The solution’s pH was adjust using diluted sodium hydroxide or hydrochloric acid solutions. The samples were filtered with 0.22 µm syringe-filters from Millipore prior to UV-VIS measurements. Unknown concentrations were determined by a comparison against calibration curves. Calibration curves were established from four different concentrations (50, 100, 150, and 200 µM) with excellent linearity in all cases (R² > 0.999). UV-VIS spectra were recorded before and after adsorption using LAMBDA 850 UV/Vis spectrophotometer from PerkinElmer. Quartz cuvettes from PerkinElmer were used for the measurements. The reported adsorption data points in this study represent the average values of three individual experiments with standard deviations not exceeding 5%.

Alnajrani M.N, & Alsager O.A. (2020). Removal of Antibiotics from Water by Polymer of Intrinsic Microporosity: Isotherms, Kinetics, Thermodynamics, and Adsorption Mechanism. Scientific Reports, 10, 794.

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