The fluorescence measurements were recorded using a fluorescence spectrophotometer (RF-6000, Shimadzu, Japan). The selective tryptophan excitation wavelength was set at 295 nm, and the emission was collected in the range of 200–400 nm using 5-nm/5-nm slits. The hydrophobic probe, 4,4′-Bis-1-anilino naphthalene 8-sulfonate (bis-ANS; Molecular Probes, Eugene, OR), was used to check the surface hydrophobicity of proteins. Bis-ANS emission spectra were detected using an excitation wavelength of 395 nm, and spectra were recorded from 200 to 560 nm using 5-nm/5-nm slits. Three scans were averaged, and buffer spectra were subtracted from protein spectra to calculate each spectrum.
4 4 bis 1 anilino naphthalene 8 sulfonate bis ans
Manufactured by Thermo Fisher Scientific
Sourced in United States
4,4′-Bis-1-anilino naphthalene 8-sulfonate (bis-ANS) is a fluorescent probe used in various research applications. It is a synthetic compound that exhibits a change in fluorescence intensity upon binding to hydrophobic regions of proteins or other biomolecules.
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Lab products found in correlation
2 protocols using 4 4 bis 1 anilino naphthalene 8 sulfonate bis ans
1
Protein Surface Hydrophobicity Analysis
2
Fluorescence Spectroscopy of Protein Hydrophobicity
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The uorescence measurements were recorded on a uorescence spectrophotometer (RF-6000, Shimadzu, Japan). The selective tryptophan excitation wavelength was set at 295 nm and the emission was collected in the range 200-400 nm using 5nm/5nm slits. The hydrophobic probe, 4,4′-Bis-1-anilino naphthalene 8-sulfonate (bis-ANS) (Molecular Probes, USA), was used to check the surface hydrophobicity of proteins. Bis-ANS emission spectra were detected using an excitation wavelength of 395 nm, and spectra were recorded from 200-560 nm using 5nm/5nm slits. Three scans were averaged and buffer spectra were subtracted from protein spectra to calculate each spectrum.
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