Electrophoresis
Development & Consulting
Dr. Hanspeter Schickle
Wolfgang Gstrein

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Classical SDS and 2-Dimensional Electrophoresis

Due to a multi-phase buffer-syste we have separation down to 1500 Dalton in a normal 15% gel even without a gradient.
The problem is that SDS is not binding to all the peptides: below 8kD all proteomics 2D-gels appear “empty”. The peptides without an anodal tenside migrate slower and will probably be found among the bigger proteins

Bacillus subtilis in 1-dimensional SDS-electrophoresis: SDSGel 15% 25S. Hot Coomassie stain

K.Buettner, Greifswald (Germany)

E.coli in classical 2D electrophoresis:
First dimension: IPG-strip pH 4-7, 11 cm; second dim.: horizontal SDS 12.5%T

Bacillus subtilis run on IPG pH 4-7, then on a horizontal gel 15%T: The smallest peptide visible is ~10 kD
below this value the 2D-pattern appear “empty”

K.Buettner, Greifswald (Germany)

EDC Electrophoresis Development & Consulting, Vor dem Kreuzberg 17, 72070 Tübingen (Germany)