After amplification, a 5 μL aliquot of each sample was directly subjected to gel electrophoresis in 2% agarose gel in the presence of ethidium bromide.
In order to evaluate molecular weight of the polymer that was grafted on to the surface of the nanoparticles, it was degrafted suitably and subjected to gel permeation chromatography analysis.
Fractions 1 5 were combined and subjected to gel permeation via Sephadex LH-20 (CH2Cl2) to afford a white oil designated 79 mg of AMJ2, Rf = 0.54 TLC (Hex/EtOAc) 2 8).
The remaining half portions of the extracts were also subjected to gel filtration at the same scale as the Sephadex G-25 column, and all the active fractions obtained were combined (Fr-G-1 3, 21.76 g).
The samples were subjected to gel electrophoresis and western blotting as described above.
In order to further purify construct 4, the enzyme was concentrated and subjected to gel filtration chromatography.
The incubation medium containing sulfate-labeled degradation fragments was subjected to gel filtration on a Sepharose CL-6B column.
Only one peak was found when MIF-II activity was subjected to gel filtration on Sephacryl S-300.
BSA-digoxin immunized serum (200 µL), which was determined to contain bispecific antibodies, was subjected to gel filtration to exclude the involvement of antibody aggregates.
Glioma cells were sorted from the cell mixture based on GFP expression and subjected to gel electrophoresis and Western Blot analysis.
Whole cell extracts (50 µg to 100 µg) were subjected to gel electrophoresis (SDS-PAGE) and transferred to PVDF membranes (Millipore Corporation, Bedford, USA).
