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Literature summary for 3.1.21.4 extracted from

  • Xu, Z.; Rui, Y.N.; Balzeau, J.; Menezes, M.R.; Niu, A.; Hagan, J.P.; Kim, D.H.
    Highly efficient one-step scarless protein tagging by type IIS restriction endonuclease-mediated precision cloning (2017), Biochem. Biophys. Res. Commun., 490, 8-16.
    View publication on PubMed
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Application

Application Comment Organism
molecular biology protein tagging with a wide variety of epitopes and/or fusion partners is used routinely to dissect protein function molecularly. Frequently the required DNA subcloning is inefficient, especially in cases where multiple constructs are desired for a given protein with unique tags. The generated clones have unwanted junction sequences introduced. To add versatile tags into the extracellular domain of the transmembrane protein THSD1, a protein tagging technique is developed that utilizes non-classical type IIS restriction enzymes that recognize non-palindromic DNA sequences and cleave outside of their recognition sites. The method is highly efficient and can precisely fuse any tag into any position of a protein in a scarless manner. IT is cost-efficient and adaptable because it uses commercially available type IIS restriction enzymes and is compatible with the traditional cloning system used by many labs Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus Q69B20
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