040108: Method for the Separation of Peptide or Protein Materials
Case ID:
TEC2004-0108
Web Published:
7/21/2014
Description:
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
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.
Benefits
- 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.
Applications
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.
IP Protection
Status
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For Information, Contact:
Randy Ramharack
Technology Manager
Michigan State University - Test
517-355-2186
ramharac@msu.edu