gel electrophoresis

In the early 1960s, he developed new applications for gel electrophoresis.

Among the research conducted at the laboratory was the development of gel electrophoresis.

Proteins can be studied by gel electrophoresis in two ways.

The proteins of the sample are separated using gel electrophoresis.

Those sets of fragments are then separated by gel electrophoresis.

In gel electrophoresis, molecules with big charges are going to move faster.

Gel electrophoresis can also be used for separation of nanoparticles.

Gel electrophoresis separates protein molecules according to both size and charge.

Purify products 120-160 base pairs in length by gel electrophoresis.

It has been tested and recommended for polyacrylamide gel electrophoresis.

"What I did was start a gel electrophoresis."

Gel electrophoresis then "yields the number of times each repeat unit appears in the fragment."

More recent techniques such as temperature gradient gel electrophoresis, allow for a faster result.

Silver staining is also used in temperature gradient gel electrophoresis.

However, gel electrophoresis is mainly a research tool, also when the subject is blood proteins.

Run both samples side by side on a polyacrylamide gel electrophoresis.

Gel electrophoresis is one of the principal tools of molecular biology.

The first method fractionates whole proteins and is called two-dimensional gel electrophoresis.

It migrates in beta-alanine-acetate-urea gel electrophoresis as a single compound.

These include methods based on gel electrophoresis, chromatography and mass spectrometry.

It is often used in gel electrophoresis.

This is a high-resolution alternative to slab gel electrophoresis.

In contrast to native gel electrophoresis, quaternary structure cannot be investigated using this method.

The resulting linear fragments form 'bands' after gel electrophoresis.

This page is a subsection of Gel electrophoresis.