Method for the Separation of Peptide or Protein Materials
The recent focus on proteomics research has resulted in an increased demand for sophisticated methods to identify and analyze post-translational processing of proteins for the purpose of analyzing cellular signaling networks and diagnosing diseases. The reversible process of phosphorylation/dephosphorylation is one modification that is critical for intra- and intercelluar signaling. To better study the properties of phosphorylated proteins and peptides, it is important to be able to separate them from their unphosphorylated counterparts. Current methods for accomplishing this separation have limitations.
Description of Technology
This technology describes a method for separating and enriching phosphorylated proteins and peptides from complex mixtures of cellular or tissue extracts. Separation is accomplished by a two-step process involving derivatization of carboxylate groups followed by binding to a diazo group-substituted organic moiety immobilized on solid-phase separation media. The purified phosphorylated proteins or peptides are then liberated from the resin.
- Reliable, reproducible process: This technology can provide reproducible separation of phosphorylated proteins.
- Improved yields and purity: This method avoids some of the non-specific binding observed in other methods, reducing contamination with non-phosphorylated proteins and peptides.
Isolation of phosphorylated proteins and peptides is important for studying biochemical processes that regulate cellular functions, which are critical for health and disease. Information acquired through use of this invention could enable development of new diagnostic tests and identification of novel targets for therapeutic intervention.
US 2006/0014234 A1 (filed Jun 7, 2005)
Jetze Tepe, Thomas Pinnavaia
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