Eosin Y: A reversible stain for detecting electrophoretically resolved protein
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Organic photoredox catalysts for wastewater remediation: Beyond the established advanced oxidation processes
2022, Chemical Engineering Journal AdvancesCitation Excerpt :Thus, degradation of two pollutants could be achieved in one shot, one through oxidation and the other through reduction, minimizing the costs and the efforts of the process and being an example of circular economy. Eosin Y (EY), a low cost xanthene synthetic dye with a characteristic band at 530 nm, responsible for its red-pink color, constitutes an example of organic photocatalyst able to produce reduction of the recalcitrant contaminants from its triplet excited state[37,38]. Its UV–visible absorption spectrum together with its well-known photophysical properties are shown in Fig. 4.[39]
Role of polycation adsorption in poly-Si, SiO<inf>2</inf> and Si<inf>3</inf>N<inf>4</inf> removal during chemical mechanical polishing: Effect of polishing pad surface chemistry
2011, Colloids and Surfaces A: Physicochemical and Engineering AspectsInvestigation on the pH-dependent binding of Eosin Y and bovine serum albumin by spectral methods
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2007, Developmental and Comparative ImmunologyProcessing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
2003, Journal of Biological ChemistryCitation Excerpt :The molecular masses of the synthetic peptides were determined with MALDI mass spectra. The purity of the authentic and synthetic peptides was checked with 20% acetic acid-urea polyacrylamide gel electrophoresis followed by Coomassie staining for peptides as described by Selsted and Becker (23). A low molecular mass calibration kit for electrophoresis (Amersham Biosciences) was used, containing rabbit muscle phosphorylase b (94 kDa), bovine serum albumin (67 kDa), egg white ovalbumin (43 kDa), bovine erythrocyte carbonic anhydrase (30 kDa), soybean trypsin inhibitor (20.1 kDa), bovine milk α-lactalbumin (14.4 kDa), and aprotinin (6.5 kDa).
Structural determinants of procryptdin recognition and cleavage by matrix metalloproteinase-7
2003, Journal of Biological ChemistryCitation Excerpt :Resolved proteins were visualized by staining with Coomassie R-250 after fixation in formalin-containing acetic acid/methanol. Crp4 and pro-Crp4 were identified by co-migration with authentic mouse Crps and pro-Crps in AU-PAGE (>0.6 × R F of methyl green dye) as described (22) and confirmed by MALDI-TOF-MS and NH2- terminal sequencing. For reduction and alkylation, recombinant peptides dissolved at 500 μg/ml in 6m guanidine HCl, 100 mm Tris-HCl (pH 8.0) were reduced with dithiothreitol at 50 °C for 3–4 h using 5 mol of dithiothreitol per mol of polypeptide cysteine.