0.1 cm quartz cuvette

Manufactured by Hellma

Sourced in United States, Germany

The 0.1 cm quartz cuvettes are optical cells designed for spectroscopic analysis. They feature a path length of 0.1 cm and are made of high-quality quartz material. These cuvettes are commonly used in various analytical techniques that require a short path length, such as UV-Vis spectroscopy.

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Lab products found in correlation

Chirascan cd spectrometer, by Applied Photophysics (1 mentions) J 815 spectrometer, by Jasco (1 mentions) Spectra manager 2, by Jasco (1 mentions)

4 protocols using 0.1 cm quartz cuvette

Tau Protein Structural Analysis by CD Spectroscopy

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CD spectra were acquired on a Jasco
J-810 CD spectropolarimeter using 0.1 cm quartz cuvettes (Hellma)
operated at 20 °C. To minimize buffer absorption, Tau samples
with 1 to 2.5 μM concentration were dialysed overnight against
10 mM sodium phosphate buffer, pH 7.8, in Slide-A-Lyzer MINI dialysis
devices (100 μL). CD spectra were recorded from 190 to 260 nm
at a scan speed of 20 nm/min and an increment of 1 nm. Four scans
were recorded for each sample. The buffer was used as a blank for
background subtraction.

Bryan L., Awasthi S., Li Y., Nirmalraj P.N., Balog S., Yang J, & Mayer M. (2022). Site-Specific C-Terminal Fluorescent Labeling of Tau Protein. ACS Omega, 7(50), 47009-47014.

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Circular Dichroism Protein Analysis

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Proteins were diluted to 0.1 mg/mL in degassed CD buffer (10 mM HEPES, pH 7.4 at 25 °C). CD measurements from a buffer only sample were subtracted from the protein CD measurements. CD experiments were carried out on a Chirascan CD spectrometer (Applied Photophysics) at 25 °C using 0.1 cm quartz cuvettes (Hellma Analytics).

Ferguson F.M., Dias D.M., Rodrigues J.P., Wienk H., Boelens R., Bonvin A.M., Abell C, & Ciulli A. (2014). Binding Hotspots of BAZ2B Bromodomain: Histone Interaction Revealed by Solution NMR Driven Docking. Biochemistry, 53(42), 6706-6716.

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Circular Dichroism Protein Analysis

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Circular dichroism (CD) measurements were performed at wavelengths from 200 to 250 nm at 20°C using 1 nm intervals with 10 accumulations per read. The proteins were diluted to a final concentration of 3 µM (BR3 Pol) and 1.3 µM (KOD Pol) in PBS buffer containing the corresponding salt concentrations and incubated at room temperature for 5 min before the measurements. A sample volume of 300 µl was used in a 0.1-cm quartz cuvette (Hellma, Huntington, NY, USA), and the measurement was performed on a Jasco J-815 Spectrometer (Jasco, Easton, MD, USA). The molar ellipticity was calculated by Spectra Manager II (Jasco).

Takahashi M., Takahashi E., Joudeh L.I., Marini M., Das G., Elshenawy M.M., Akal A., Sakashita K., Alam I., Tehseen M., Sobhy M.A., Stingl U., Merzaban J.S., Di Fabrizio E, & Hamdan S.M. (2018). Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea. The FASEB Journal, 32(6), 3346-3360.

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Functional Analysis of Glutaredoxin Enzyme

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The Cys13, Pro14, Tyr15, Cys16, Arg43, Thr55, Val56, and Pro57 residues in the active sites and binding sites were mutated to evaluate the effects of these residues on enzyme activity. To generate mutant forms of Ps-Grx3, the pET-28a(+) vector was used as a template for the site-directed mutagenesis of the Cys13, Pro14, Tyr15, Cys16, Arg43, Thr55, Val56, and Pro57 residues to alanine using the QuikChange Site-directed Mutagenesis Kit (Stratagene) following the manufacturer’s instructions. The primers designed for site-directed mutagenesis are shown in Table 1. The expression and purification of the mutant proteins were performed as described for wild-type Ps-Grx3.
For all Circular Dichroism (CD) measurements, five repeated scans were carried out to establish a baseline. Far-UV CD measurements were performed in a 0.1-cm quartz cuvette (Hellma, Germany) between 260 and 180 nm for 12 s every 1.0 nm using a bandwidth of 1.5 nm in a Jasco J-107 spectropolarimeter (Jasco, Japan). Ps-Grx3 and its mutant forms were separately diluted in a solution of 100 mM Tris–HCl (pH 8.0). Changes in secondary structure were presented as molar ellipticity [θ], according to the following equation: to the following equation:
in which θ is the ellipticity measured at a given wavelength λ (deg), n is the number of amino acids, l is the cell path length (cm), and c is the protein concentration (mol/L).

Wang Y., Hou Y, & Wang Q. (2021). Cloning, Expression, Characterization, and Antioxidant Protection of Glutaredoxin3 From Psychrophilic Bacterium Psychrobacter sp. ANT206. Frontiers in Microbiology, 12, 633362.

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