The phrase "after the first dimension" is correct and usable in written English.
It can be used in contexts discussing dimensions in mathematics, physics, or any field that involves spatial or conceptual dimensions.
Example: "The analysis will focus on the properties of the object after the first dimension is established."
Alternatives: "following the initial dimension" or "subsequent to the first dimension".
After the first dimension, strips were equilibrated in a solution of 6 M urea, 1% DTT and 2% SDS for 15 min and then applied to gels.
After the first dimension of isoelectric focusing, the protein was separated in the second dimension on a 4 to 12% NuPAGE polyacrylamide gel (Invitrogen).
Since it is likely that no single dimension of LC suffices to resolve complex protein mixtures, we sought to employ a second dimension of LC after the first dimension separation by HIC.
After the first dimension, non-reducing electrophoresis, the entire lane containing the separated proteins was excised and soaked for 20 min in SDS sample buffer containing 100 mM dithiothreitol to reduce any disulfide bonds present between proteins or within proteins.
After the first dimension steps, the equilibrated strips were loaded onto 15% SDS-PAGE gels (20 × 20 cm) and run at 250 V for 4.5 h at room temperature.
After the first dimension run, the strips were equilibrated by incubation in 6 M urea, 0.375 M Tris HCl, pH 8.8, 2% SDS, 20% glycerol, 2.5% (w/v) DTT 10 ml per strip for 20 minutes at room temperature, followed by an incubation for 30 minutes in the same buffer but in which DTT was replaced by 2.5% (w/v) iodoacetamide.
After the separation, the first dimension strips were equilibrated twice with equilibration buffer (6 M urea, 50 mM Tris HCl pH 8.8, 20% glycerol, and 2% SDS) in the presence of 1% DTT in the first equilibration and 4% iodoacetamide in the second one.
RLGS fragments are separated along the first dimension after the application of the second enzyme.
After completion of development in the first dimension, the plates were immersed in methanol for 15 min, and then allowed to dry thoroughly (45 min).
For two-dimensional gel electrophoresis, eighty micrograms of protein purified from mitochondrial fractions isolated from cultured GCs after treatment were focused in the first dimension on IPG pH gradient 4 7 strips for 60 kV-h using a Bio-Rad Protean IEF Cell and second dimension followed by the Western blotting procedure and PHB antibody to detect protein spots corresponding to PHB.
After 17 h of passive rehydration, the first dimension was run on a Multiphor-II flatbed system (GE Healthcare) at 20°C with the following program: 15 min at 300 V, 15 min at 500 V, and 9 h at 3500 V.
