Creative Proteomics offers an integrated solution for the identification of low abundance proteins in complex biological sample through 2D electrophoresis.

In two-dimensional gel electrophoresis, proteins are first separated by their pI in isoelectric focusing and then further separated by molecular weight through SDS-PAGE, thus the sample proteins are distributed across the two-dimensional gel profile. This technique expands the number of proteins that could be identified, provides more efficient data and detailed information for proteomics analysis.

Two-dimensional gel electrophoresis, abbreviated as 2-DE, is a form of gel electrophoresis commonly used to analyze mixture of proteins by two properties in two dimensions respectively.

2-D electrophoresis begins with 1-D electrophoresis and then separates the molecules by a second property in a direction 90 degrees from the first. In 1-D electrophoresis, the proteins separated in one dimension will lie along a lane, and then the molecules are spread out across in the 2-D gel. Generally, it is unlikely that two molecules will be similar in both two distinct properties, so molecules are more effectively separated in 2-D electrophoresis than in 1-D electrophoresis.

Isoelectric focusing (IEF) and Sodium Dodecyl Sulfate Poly Acrylamide Gel Electrophoresis (SDS-PAGE) are preferred in 2-DE separation. In IEF/SDS-PAGE, the proteins applied in the first dimension will move along the gel andaccumulate at their isoelectric point; that is, the point at which the protein has a neutral charge.

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