Quartz microcuvettes

Manufactured by Starna Cells

Quartz microcuvettes are small, transparent containers made of high-quality quartz material. They are designed to hold small volumes of samples for spectroscopic analysis, such as UV-Vis absorption or fluorescence measurements.

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Lab products found in correlation

Rapamycin, by Merck Group (2 mentions) Agilent multizonepeltier temperature controller, by Agilent Technologies (2 mentions) Cary eclipse fluorometer, by Agilent Technologies (2 mentions) Cary model 100 spectrometer, by Agilent Technologies (2 mentions) Quartz cuvette, by Starna Cells (2 mentions) Cary 3500 uv vis spectrophotometer, by Agilent Technologies (1 mentions)

4 protocols using quartz microcuvettes

Rapamycin-Induced Protein Aggregation

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Protein aliquots were thawed
and solubilized at 50 °C and then diluted to 6 μM in buffer
to adjust to a final salt concentration of 150 mM in 20 mM, Tris-HCl,
pH 8.5. SYNZIP-tagged constructs were similarly adjusted to 10 μM
in 150 mM NaCl, 20 mM HEPES, pH 6.8. The protein mixture, 60 μL
in volume, was added to quartz microcuvettes (10 mm path length) (Starna
Cells, Inc. Atascadero, CA). Cuvettes were inserted into a Cary 3500
UV–vis spectrophotometer controlled by an Agilent multizone
Peltier temperature controller (Agilent Technologies; Santa Clara,
CA). To test kinetics of rapamycin-induced dimerization and phase
separation of FRB and FKBP-tagged RGG constructs, rapamycin (Sigma-Aldrich;
St. Louis, MO) was spiked into the protein mixtures to a final concentration
of 10 μM and absorbance at 600 nm was measured over time. For
mapping the temperature-dependent phase separation, protein mixtures
were applied to quartz cuvettes preincubated at 50 °C. Cuvettes
were then inserted into the preheated spectrophotometer, set to 50
°C, and samples were cooled to 5 °C at a rate of 1 °C/min
while measuring the absorbance at 600 nm.

Garabedian M.V., Su Z., Dabdoub J., Tong M., Deiters A., Hammer D.A, & Good M.C. (2022). Protein Condensate Formation via Controlled Multimerization of Intrinsically Disordered Sequences. Biochemistry, 61(22), 2470-2481.

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Protein Phase Separation Kinetics

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Protein aliquots were thawed and solubilized at 50°C and then diluted to 6 μM in buffer to adjust to a final salt concentration of 150 mM in 20 mM, Tris-HCl pH 8.5. SYNZIP tagged constructs were similarly adjusted to 10 μM in 150 mM NaCl, 20 mM HEPES pH 6.8. 60 μL of protein was added to quartz microcuvettes (10 mm path length) (Starna Cells, Inc. Atascadero, CA). Cuvettes were inserted into a Cary 3500 UV-Vis spectrophotometer controlled by an Agilent multizone peltier temperature controller (Agilent Technologies; Santa Clara, CA). For kinetics tests of rapamycin-induced dimerization of FRB and FKBP tagged RGG constructs, rapamycin (Sigma-Aldrich; St. Louis, MO) was spiked into the protein mixtures to a final concentration of 10 μM and absorbance at 600 nm was measured over time. For mapping temperature dependent phase separation, protein mixtures were applied to quartz cuvettes preincubated at 50°C. Cuvettes were then inserted into the pre-heated spectrophotometer, set to 50°C, and samples were cooled to 5°C at a rate of 1°C per min while measuring absorbance at 600 nm.

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Fluorescent Molecule Spectroscopy Protocol

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Fluorescent and fluorogenic molecules for spectroscopy were prepared as stock solutions in DMSO and diluted such that the DMSO concentration did not exceed 1% v/v. Spectroscopy was performed using 1-cm path length, 3.5-mL quartz cuvettes or 1-cm path length, 1.0-mL quartz microcuvettes from Starna Cells. All measurements were taken at ambient temperature (22 ± 2 °C). Absorption spectra were recorded on a Cary Model 100 spectrometer (Agilent). Fluorescence spectra were recorded on a Cary Eclipse fluorometer (Varian). Maximum absorption wavelength (λ_abs), extinction coefficient (ε), and maximum emission wavelength (λ_em) were taken in 10 mM HEPES, pH 7.3 buffer unless otherwise noted; reported values for ε are averages (n = 3). Normalized spectra are shown for clarity.

Grimm J.B., Muthusamy A.K., Liang Y., Brown T.A., Lemon W.C., Patel R., Lu R., Macklin J.J., Keller P.J., Ji N, & Lavis L.D. (2017). A general method to fine-tune fluorophores for live-cell and in vivo imaging. Nature methods, 14(10), 987-994.

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Fluorescent Molecules Spectroscopy Protocol

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Fluorescent and fluorogenic molecules for spectroscopy were prepared as stock solutions in DMSO and diluted such that the DMSO concentration did not exceed 1% v/v. Spectroscopy was performed using 1-cm path length, 3.5-mL quartz cuvettes or 1-cm path length, 1.0-mL quartz microcuvettes from Starna Cells. All measurements were taken at ambient temperature (22 ± 2 °C). Absorption spectra were recorded on a Cary Model 100 spectrometer (Agilent). Fluorescence spectra were recorded on a Cary Eclipse fluorometer (Varian). Maximum absorption wavelength (λ_abs), extinction coefficient (ε), and maximum emission wavelength (λ_em) were measured in 10 mM HEPES, pH 7.3 buffer; reported values for ε are averages (n = 3). Normalized spectra are shown for clarity. For prototype ion indicators 32 and 33 (Extended Data Fig. 5d–e) the compounds were dissolved in 10 mM HEPES, pH 7.3 buffer alone or with either 100 mM KCl or 10 μM ZnCl₂; the fluorescence emission spectra of these solutions were recorded using λ_ex = 575 nm and λ_em = 625–825 nm.

Grimm J.B., Tkachuk A.N., Xie L., Choi H., Mohar B., Falco N., Schaefer K., Patel R., Zheng Q., Liu Z., Lippincott-Schwartz J., Brown T.A, & Lavis L.D. (2020). A general method to optimize and functionalize red-shifted rhodamine dyes. Nature methods, 17(8), 815-821.

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