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After coomassie staining, lanes were cut into bands and subjected to in-gel trypsinization.
Following separation of co-immunoprecipitated proteins by SDS-PAGE, the gel was cut into bands of 3 mm and the proteins digested in-gel with trypsin.
In brief, about 1.5 mg of total protein was separated by 12% SDS-PAGE gel and was cut into bands and then diced into 1 cm cubes.
Similar(57)
Each gel lane was cut into 12 bands followed by reduction, alkylation, in-gel digestion with trypsin and peptides were extracted, as described in [81].
For this, each gel lane was cut into ten bands.
The entire lane was cut into small bands, before being sent for protein identification.
Each lane was cut into 22 bands, and the gel slices were digested with trypsin.
Each lane of the protein gel was cut into ten bands and then washed with water.
Individual gel lanes were cut into three bands and were in-gel digested as described elsewhere (Wilm et al, 1996).
Each lane was cut into 22 bands and subjected to an in-gel tryptic digestion protocol as previously described [ 41].
Each gel lane was cut into 10 bands (4 mm × 6 mm) and further chopped into ~1 mm pieces and transferred to 1.5 ml Eppendorf tubes.
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