Binding Protein for Detecting Phosphatidic Acid

 

Introduction

 

Phosphatidic acid (PA) is an essential component of living cells. PA-signaling processes are extremely important biochemical pathways that are likely implicated in many diseases and in the pathology of serious health conditions. Its detection and measurement can be very important for basic science and biomedical research. Current methods for detecting PA are difficult, expensive, and widely considered adequate at best. This hampers important biomedical research related to basic cellular biochemistry and pathologies.

 

Description of Technology

 

MSU’s invention relates to the identification and cloning of a newly characterized PA-binding protein, TGD2, and the uses of this protein as the basis of new methods to detect and measure PA. These methodologies are based on the specific molecular interaction of the protein with PA. The TGD2 protein is unique in that it interacts only with PA and offers a level of specificity not achievable with other reagents.

 

Key Benefits

  • Direct and simple: New in-vitro assay procedures enabled by this discovery replace the complex, indirect biochemical methods required by traditional detection and measurement methods.
  • Affordable: Eliminates the need for complex and expensive equipment that is unavailable to most laboratories.
  • Unique intracellular localization and assay platform: Permits simple assay development for high-content screening and research applications involving PA biochemistry and signaling.

 

Applications

  • Life science reagents for studying PA biochemistry and cellular signal transduction pathways in biomedical research
  • High-content screening by individual drug discovery companies within the biotechnology and pharmaceutical industry with interest in PA-biochemistry
  • Possible target for herbicide development by Agro-biotech companies due to TGD2’s

 

Patent Status

 

Patent pending

 

Inventors

 

Christoph Benning, Binbin Lu

 

Tech ID

 

TEC2008-0076

 

Patent Information:

For Information, Contact:

Thomas Herlache
Assistant Director
Michigan State University
herlache@msu.edu