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Glutathione S-transferase Clones for Members of the Ubiquitin-Dependent Protein Degradation Pathway

National Institutes of Health (NIH)
Development of cDNA for glutathione S-transferase (GST) clones for the following factors: Nedd4, XIAP, UBCH5B, and CBL-B.

Full description

Scientists at the National Institutes of Health have developed cDNA for glutathione S-transferase (GST) clones for the following factors: Nedd4, XIAP, UBCH5B, and CBL-B. These proteins are involved in the ubiquitin-dependent pathway of protein degradation in cells, the major cellular system for protein degradation. The ubiquitin-proteosome pathway regulates several cancer regulated proteins. Defects in this pathway can lead to cancer development. The GST clones can be used to produce corresponding GST fusion proteins in order to isolate each protein from the pathway for further analysis. These constructs can also be incorporated into assays/kits to detect proteins in the ubiquitin-dependent pathway.

 

Applications:

  • Research tools for detection and isolation of ubiquitin-dependent pathway members in order to understand the pathway defects that lead to cancer and develop preventions and treatments to overcome these defects
  • Research tools for generating fusion proteins of Nedd4, XIAP, UBCH5B, and CBL-B to further analyze their functions in vivo and in vitro
  • Controls for screening inhibitors of the ubiquitin-dependent pathway in order to better understand the different mechanisms of ubiquitin-dependent protein degradation

Patent information

HHS Reference No. E-245-2003/0 – Research Tool. Patent protection is not being pursued for this technology.

 

Inventors: 
Allan M. Weissman et al. (NCI)

 

 

Type of business relationship sought

Licensees Sought: 
Available for licensing under a Biological Materials License Agreement.

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National Institutes of Health (NIH)

The NIH supports and conducts basic, clinical, and translational medical research, and investigates the causes, treatments, and cures for both common and rare diseases.

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