Recombinant protein tagging is the genetic fusion of a peptide or protein sequence to a target protein, producing a polypeptide with an additional recognition or functional element. Tags can provide binding sites and can alter the solubility, yield, or folding of the fusion protein [1]. An affinity tag interacts with a corresponding ligand, allowing the tagged product to be selectively captured from a mixture [2]. Tag sequences can also encode epitopes, localization reporters, or elements that recruit cellular activities; their placement must preserve the reading frame of the target coding sequence [3]. In split-fluorescent-protein systems, a short fused fragment associates with a complementary fragment to assemble a fluorescent complex, linking detection to the presence of the tagged protein [4].
- fusion protein
- peptide tag
- linker
- recombinant expression
References
- David S. Waugh; Making the Most of Affinity Tags. Trends Biotechnol. 2005, 23, 316-320, 10.1016/j.tibtech.2005.03.012.
- Ana Sofia Pina; Christopher R. Lowe; Ana Cecília A. Roque; Challenges and Opportunities in the Purification of Recombinant Tagged Proteins. Biotechnol. Adv. 2014, 32, 366-381, 10.1016/j.biotechadv.2013.12.001.
- Giel Vandemoortele; Sven Eyckerman; Kris Gevaert; Pick a Tag and Explore the Functions of Your Pet Protein. Trends Biotechnol. 2019, 37, 1078-1090, 10.1016/j.tibtech.2019.03.016.
- Stéphanie Cabantous; Thomas C Terwilliger; Geoffrey S Waldo; Protein Tagging and Detection with Engineered Self-assembling Fragments of Green Fluorescent Protein. Nat. Biotechnol. 2005, 23, 102-107, 10.1038/nbt1044.