Fast and Sensitive Colloidal Coomassie G-250 Staining for Proteins in Polyacrylamide Gels

Global role of the membrane protease LonB in Archaea: Potential protease targets revealed by quantitative proteome analysis of a lonB mutant in Haloferax volcanii

“…The gels were run at room temperature until samples passed the stacking gel and all proteins were concentrated into one protein band in the separation gel. Proteins were visualized with a coomassie brilliant blue (CBB-G250) stain as described by Dyballa and Metzger (2009) [27].…”

Monomeric agonist peptide/MHCII complexes activate T‐cells in an autonomous fashion

“…Protein samples were mixed 3:1 with a 4× loading buffer (250 mM Tris–HCl, 8% SDS, 40% glycerol, and 0.04% bromophenol blue, pH 6.8) optionally supplemented with 20 mM dithiothreitol (Merck) to arrive at non‐reducing and reducing conditions, respectively, and then subjected to 10–12% SDS–PAGE in running buffer (25 mM Tris–HCl, 192 mM glycine, and 0.1% SDS, pH 8.2). Silver staining and colloidal Coomassie G‐250 staining were carried out for visualization of the protein bands as described (Chevallet et al , 2006; Dyballa & Metzger, 2009).…”

Specific preadaptations of Rhodococcus equi cooperate with its Virulence‐associated protein A during macrophage infection

“…Lysosomes were prepared from J774E macrophages using a magnetic method as described (Becken et al, 2010), lysed by three fast freeze (−80°C) and thaw (37°C) cycles, and incubated with the indicated quantities of bovine serum albumin fraction V (BSA; Carl Roth No. 0163.4) in 75 mM citrate buffer (pH 4.5) for 30 min at 37°C and the digestion products were analyzed in SDS‐10% polyacrylamide gels with colloidal Coomassie staining (Dyballa & Metzger, 2009). (Lys) describes a ‘postnuclear supernatant’, i.e.…”