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Antisera to Detect Phosphorylated Phosphoinositide-Dependent Kinase 1 (PDK-1)

Posted Nov 30 2006 4:00pm

Description of Invention:
PDK-1 phosphorylates and activates a number of cellular kinases, and plays a major role in insulin and growth factor signaling. PDK-1 also represents a promising drug target for a number of cancers. Autophosphorylation at Ser244 (mouse) or Ser241 (human) is critical for PDK-1 activity.

Available for licensing are polyclonal rabbit antisera that specifically detect mouse PDK-1 protein phosphorylated at Ser244. These antisera are also expected to be specific for the human PDK-1 protein phosphorylated at Ser241.

  • Tool for screening PDK-1 autophosphorylation inhibitors for cancer and other indications
  • Tool for studying insulin and growth factor signaling

Michael J Quon (NCCAM)

Patent Status:
HHS, Reference No. E-330-2003/0

Relevant Publication:
  1. MJ Wick, FJ Ramos, H Chen, MJ Quon, LQ Dong, F Liu. Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop. J Biol Chem. 2003 Oct 31;278(44):42913-42919. [ PubMed abs ]

Licensing Status:
This technology is available as a research tool under a Biological Materials License.

Collaborative Research Opportunity:
The NIH, NCCAM, Diabetes Unit is seeking statements of capability or interest from parties interested in collaborative research to further develop, evaluate, or commercialize phospho-specific PDK-1 antibody and insulin signaling. Please contact Michael J. Quon, Chief, Diabetes Unit, NCCAM, NIH at for more information.

Cancer - Research Materials
Internal Medicine
Internal Medicine - Research Materials

For Additional Information Please Contact:
Tara Kirby Ph.D.
NIH Office of Technology Transfer
6011 Executive Blvd. Suite 325,
Rockville, MD 20852
United States
Phone: 301-435-4426
Fax: 301-402-0220

Ref No: 1474

Updated: 12/2006

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