Molecular Probes for Identification or Isolation of Membrane Proteins

Background:
The Nanobiology Program of the National Cancer Institute is seeking statements of capability or interest from parties interested in collaborative research to obtain pre-clinical data to be used to further develop, evaluate, or commercialize molecular probes designed around an iodonaphthyl succinate antigen.

Technology:
This technology describes a new class of molecular probes designed around an iodonaphthyl succinate antigen. The probes can be used to label and tag proteins using a variety of conventional protein modification chemistries. The technology is offered as a combination of probe + monoclonal antibodies against the probe (three clones). Several possible probes as well as monoclonal antibodies that react with these probes are described in this invention.

The probe can be used for labeling and tagging cell surface and integral membrane proteins as well as soluble proteins. The monoclonal antibodies were tested and found to be effective for immunoprecipitation, western blot, and flow cytometry. Once tagged, the modified proteins can be detected or isolated using an antibody reactive with the probe. These probes and their corresponding antibodies have significant advantages over the biotin-avidin system, including the ability to reverse binding for protein isolation and the lack of high, non-specific binding to cell surfaces. Additionally, an isotopic¹²⁵l label may be incorporated in the probe for tracking tagged proteins in vivo

Further R&D Needed:
Organic Synthesis of derivatives that are selective towards the lipophilic domain biological membranes.

R&D Status:
In vitro data is available

IP Status:
U.S. Provisional Application No. 60/906,166 filed 09 Mar 2007

Value Proposition:

• reversibility of binding for protein isolation
• lack of high, non-specific binding to cell surfaces
• ability to incorporate isotopicisotopic¹²⁵l label in the probe for tracking tagged proteins in vivo

Contact Information:
John D. Hewes, Ph.D., NCI Technology Transfer Center
Phone: 301-435-3121
E-mail: Hewesj@mail.nih.gov

Reference:  #511 JH

Posted 12/17/2007