Tx2 metal-binding tag for purification and identification of recombinant proteins

Case ID:

 Tx2 Metal-Binding Tag for Purification and Identification of Recombinant Proteins  

WSU Tech#: 11-1058

Technology Summary:

The technology is a new method of protein purification similar to the principles behind that of a histidine and Ni column system.  The new technology uses a different amino acid sequence for generating a metal-binding cluster:


T: “H – (E/A) – E – A – H”

Tx2: “H – (E/A) – E – A – H - H – (E/A) – E – A – H”

Tx3: “H – (E/A) – E – A – H - H – (E/A) – E – A – H - H – (E/A) – E – A – H”


and a different type of column (Zinc) to purify proteins with less background and greater specificity than histidine and Ni columns. 

There are a number plethora of patents that use and mention zinc columns as part of their purification method for Immobilized Metal Ion affinity Chromatography (IMAC).  Thus, this will be a very difficult area to try and patent any generalized method.  More specific method based patents for very specific proteins (Heme, Pectin, IFN’s, etc.) have been filed so this may be a viable path, again for specific proteins, but likely not broad classes of proteins in general.


Competitive Advantages


There are nearly 30 suppliers of tagged protein purification systems.


Benefit Analysis:


In 2010, an estimated 22.3 million protein-purification reactions were conducted, 54.3% by tagged methods and 45.7% by non-tagged methods. Revenue for the global protein purification reagents market includes all reagents, consumables, and kits sold for tagged and non-tagged chromatography-based purification of all protein types globally. 

In 2010, this market earned $341.7 million in revenue at 4.8% growth. Certain market segments (i.e., tagged purification) are growing well; others (i.e., non-tagged) are declining. The switch to more expensive tag-based products and the growing interest in proteins in both basic and pharmaceutical research will drive this mature market at a compound annual growth rate of 5% through 2014

Stage of Development: Available


Patent Status:


No patents filed.


Licensing Opportunity:

WSU is looking for a commercial partner interested in furthering the validation of this technology and bringing it to market. 

Contact for Further Information:  

 Frank Urban, MS, CBA, BA.   email: frank.urban@wayne.edu   Phone (mobile): (734) 355-0730


Competitive Advantages:

  • Protein purification in multiple expression systems
  • High affinity and high specificity binding to transition metal ions that leads to more effective protein purification


Related publications or citations of work:

Jin, J.-P., and Smillie, L.B. FEBS Lett. 341:135-40, 1994

Jin, J.-P., and Samanez R. J. Mol Evol. 52:103-16, 2001


Patent Information:
For Information, Contact:
Ken Massey
Wayne State University
Jian-Ping Jin