MRC Technology has negotiated a licence for a protein synthesis technology, Genetically encoded Orthogonal Protection and Activated Ligation (GOPAL), with Bio-Techne, (Techne Corp.). The GOPAL technology was originated at the MRC Laboratory of Molecular Biology.
The licence will enable Bio-Techne to develop reagent products using GOPAL. GOPAL enables the formation of site-specific isopeptide bonds between proteins. Initially GOPAL will be applied to develop ubiquitin dimers, with the potential to also develop trimers and tetramers. The technology offers an advantage over in vitro synthesis as it allows for the production of a homogenous, high quality product, via the cellular expression of ubiquitin with a protected lysine incorporated at a site-specific, user-defined site. Following purification, the specific isopeptide bond enables creation of a ubiquitin dimer.
The technology has already been validated for ubiquitin, however it may also be applied to other proteins. Boston Biochem (a Bio-Techne company) will be applying the technology to its products to determine its full potential, including investigating its use in introducing post-translational modifications into proteins for structural and functional studies.
Dr Ranmali Nawaratne, Senior Business Manager, MRC Technology, said: “We are delighted to have worked with the MRC and Bio-Techne on this license agreement. We have every confidence that the reagents produced will be of great value to researchers.”
Dr Frank Mortari, VP Corporate Development, Bio-Techne, commented: “We are very pleased to have successfully negotiated with MRC Technology the terms on a license for this valuable technology. We look forward to applying GOPAL and realising its full potential in the creation of protein reagents.”
The technology was developed at the at the MRC Laboratory of Molecular Biology by Jason Chin (Programme Leader and Head of the LMB’s Centre for Chemical & Synthetic Biology) and Satpal Virdee (now a Programme Leader at the MRC Protein Phosphorylation and Ubiquitylation Unit at Dundee University). The work is described in Virdee et al Nat Chem Biol. 2010 Oct;6(10):750-7.