2-DE
Creative Proteomics offers an integrated solution to the identification of low
abundance proteins in complex biological sample through 2D electrophoresis.
This technique sorts proteins according to two independent properties in two
discrete steps. Each spot on the resulting two-dimensional array corresponds
to a single protein species in the sample. Thus thousands of different proteins
can be separated, and the information is obtained including the protein pI, the
apparent molecular weight, and the amount of each protein.
What Is 2D Electrophoresis?
Two-dimensional gel electrophoresis, abbreviated as 2-DE, is a form of gel
electrophoresis commonly used to analyze mixtures of proteins by two
properties in two dimensions respectively. 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 can be identified, and provides
more efficient data and detailed information for proteomics analysis.
2D Electrophoresis
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.
2D Electrophoresis Service at Creative Proteomics
2-DE is a powerful and widely used method for the analysis of complex protein
mixtures extracted from cells, tissues, or other biological samples. At Creative
Proteomics, we can provide services 2D electrophoresis service according to
standard operating procedures (SOPs).
2 DE. Before separating the proteins by mass in the second dimension, they
are treated with sodium dodecyl sulfate (SDS) along with reducing reagents
which unfolds them into long, straight molecules bound with a number of SDS
molecules. Since the SDS molecules are negatively charged, all of the proteins
