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Protein bands were stained with colloidal Coomassie Blue.
The separated gel bands were stained with GelCode Blue Stain Reagent and the entire lane (~30 slices) were excised from the gel.
ZG protein bands were stained with Coomassie Blue reagent, and the entire lane were excised in thirty gel slices for in-gel tryptic digestion (Fig. 1B).
In SDS PAGE, protein bands were stained with 0.1% (w/v) coomassie brilliant blue R-250 prepared in methanol:acetic acid:distilled water (v/v) (4:1:5) for 3 h at room temperature.
As shown in Fig. 1B, human ZG protein bands were stained with Coomassie Blue reagent and the entire lane were excised in thirty gel slices for in-gel tryptic digestion.
Protein bands were stained with Coomassie brilliant blue prior to silver staining.
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The bands are stained with ethidium bromide and photographed digitally.
The protein band was stained with Coomassie Brilliant Blue.
LKR/SDH enzyme partially purified from the tick midgut and ovary and recombinant His-LKR/SDH protein produced intensive black bands that were stained with the saccharopine and lysine substrate but no reaction in the absence substrates, indicating a specific activity for the LKR and SDH enzymes.
In order to reveal GC-rich bands, the chromosomes were stained with the fluorochrome chromomycin A3 (CMA), according to [ 24, 92] with slight modifications.
After electrophoresis, the protein bands on the gel were stained with coomassie brilliant blue R-250 and dehydrogenase-specific dyeing solution was implemented as described previously (Zhang et al. 2013a).
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