α-Crystallin (50 µM) was incubated with increasing concentrations of histones: 0.0714, 0.143, 0.357, 0.536, 0.714, 1.071, 1.43, 1.79, and 2.14 μM (1, 2, 5, 7.5, 10, 15, 20, 25, and 30 μg/ml, respectively). The histone–α-crystallin mixtures were then filtered through 0.22-μm filters and water-soluble proteins were separated in succession on G3000 PWXL and G5000 PWXL size-exclusion chromatography columns (Tosoh Bioscience LLC, Prussia, PA) in line with the Viscotek TDA 302 triple-detector array system (Viscotek/Malvern) equipped with a VE-1122 pump and a VE-7510 degasser for measuring UV absorption, refractive index, right-angle light scattering (RALS), and viscosity. Viscotek OmniSEC software was used to calculate the molecular weights of the crystallin proteins using bovine serum albumin and the 92-kDa Pullulan Malvern standards. The protein samples (100 μl) were injected into the columns with 0.5× Dulbecco's modified PBS as the mobile phase at a flow rate of 0.8 ml/min at 37 °C. The protein concentrations were calculated on the basis of the refractive index using a dn/dc of 0.185 for both the bovine serum albumin standard and the crystallin proteins.
Tda 302 triple detector array system
Manufactured by Malvern Panalytical
Sourced in Panama
The TDA 302 is a triple-detector array system designed for advanced light scattering analysis. The system incorporates three detectors that simultaneously measure the intensity of scattered light at different angles, providing comprehensive data on the size, molar mass, and shape of macromolecules and nanoparticles in solution.
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Lab products found in correlation
2 protocols using tda 302 triple detector array system
1
Histone-Induced α-Crystallin Interactions
2
Murine Lens Protein Analysis by SEC-MALS
Check if the same lab product or an alternative is used in the 5 most similar protocols
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The murine lenses were homogenized, and water-soluble proteins were extracted as described previously [10 (link)]. The molecular weights of the extracted proteins were determined from the light scatter data, and the concentrations were calculated based on the refractive index data. In the studies involving water-soluble proteins from WT and knock-in mouse lenses, 100 μl of water-soluble lens proteins were separated in succession on G3000 PWXL and G5000 PWXL size exclusion chromatography columns (Tosoh Bioscience LLC, Prussia, PA) in line with the Viscotek TDA 302 triple detector array system, which measured UV absorption, refractive index (RI), multi-angle light scattering, and viscosity (Viscotek/Malvern). The GPC system was equipped with a VE-1122 pump and a VE-7510 degasser. The Viscotek OmniSEC software was used to calculate the molecular weight of the crystallin proteins using bovine serum albumin (BSA) and the 92-kDa Pullulan Malvern standards. The protein samples (100 μl) were injected onto the columns, and Dulbecco’s Phosphate-Buffered Saline (PBS) Modified buffer (0.5x) without Ca2+ or Mg2+ was used as the mobile phase at a flow rate of 0.8 ml/min at 25°C. The protein concentration was calculated based on the refractive index using a dn/dc of 0.185 for both the BSA standard and the crystallin proteins.
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