Universal Protein
Tyrosine Phosphatase Substrate
Tech ID: 03-92-22
Researchers in Dr. Edmond H. Fischer's lab at the University of Washington have
identified a peptide that is an excellent substrate for protein tyrosine
phosphatase (PTPs) enzymatic assays. The peptide enables researchers to measure
PTP activity in immunoprecipitates and eliminates the need for a time-consuming
purification procedure. When introduced into a cell, it provides an alternate
and preferred binding site for receptor activity. Dr. Edmond H. Fischer was
awarded the 1992 Nobel Prize in physiology or medicine for his pioneering
research in reversible protein phosphorylation which led to their discovery and
purification of this peptide.
Background:
Dr. Fischer was the first to purify a PTP, and he has continued to research the
functional properties of this inhibitor of protein tyrosine kinase activity. As
part of ongoing research, the peptide was derived for use as a substrate in the
characterization of PTPs. However, further research indicates that the peptide
may also play a role in inhibiting cell transformation and signal
transduction.
Market:
The family of PTPs is an area of extreme interest to researchers because of the
potential for the development of therapeutics for a wide variety of disorders
that are affected or sustained by signal transduction. Research with PTPs has
been growing and that trend is expected to accelerate as more is learned about
PTP receptor activity, signal transduction, and the cascade effect. In addition
to its utility as a substrate for PTP assays, preliminary research indicates
that the peptide may also exhibit anti-oncogene properties. While more
investigation and development is required in this area it appears as though a
modified version of the peptide is an effective inhibitor representing an
excellent opportunity for development.
Applications:
Traditional means of purifying AAT from plasma for therapeutic use is tedious,
labor-intensive and very expensive. Since the half-life of plasma AAT is short,
regular administration is necessary and treatment can become restricted by cost
and volume. The availability of a recombinant product would offer patients a
more cost-effective therapy.
Status:
A U.S. patent has issued. The Washington Research Foundation is seeking
qualified commercial partners interested in developing therapeutics. License or
option arrangements are available.
For additional information, please contact:
Beth G. Etscheid, Ph.D.
Director of Licensing
Washington Research Foundation
2815 Eastlake Avenue E, Suite 300
Seattle, WA 98102
Tel: 206.336.5600
Fax: 206.336.5615
betschei@wrfseattle.org
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