Issue 50, 2014

Site-specific protein labelling and immobilization mediated by microbial transglutaminase

Abstract

Microbial transglutaminase (mTG) shows broad substrate specificity that is amenable to in vitro bio-conjugation applications. Herein, test proteins were genetically fused with peptide tags, followed by mTG-mediated propargylation of their reactive Gln residues. The propargylated proteins were subjected to copper-assisted azide-alkyne cycloaddition to demonstrate either fluorescent labelling or immobilization.

Graphical abstract: Site-specific protein labelling and immobilization mediated by microbial transglutaminase

Supplementary files

Article information

Article type
Communication
Submitted
06 Feb 2014
Accepted
02 May 2014
First published
02 May 2014
This article is Open Access
Creative Commons BY license

Chem. Commun., 2014,50, 6604-6606

Author version available

Site-specific protein labelling and immobilization mediated by microbial transglutaminase

S. K. Oteng-Pabi, C. Pardin, M. Stoica and J. W. Keillor, Chem. Commun., 2014, 50, 6604 DOI: 10.1039/C4CC00994K

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements