Difference between revisions of "Part:BBa K3117015"
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The SpyTag/SpyCatcher system is based on a modified domain from a streptococcus pyogenes surface protein (SpyCatcher), which recognizes a cognate 13-amino-acid peptide (SpyTag), which can bind spontaneously and form an isopeptide bond (Hatlem et al. 2019). | The SpyTag/SpyCatcher system is based on a modified domain from a streptococcus pyogenes surface protein (SpyCatcher), which recognizes a cognate 13-amino-acid peptide (SpyTag), which can bind spontaneously and form an isopeptide bond (Hatlem et al. 2019). | ||
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| − | + | 1. Hatlem, Daniel; Trunk, Thomas; Linke, Dirk; Leo, Jack C. (2019): Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins. In: International journal of molecular sciences 20 (9). DOI: 10.3390/ijms20092129. | |
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Latest revision as of 01:34, 22 October 2019
SpyTag codon optimized for CHO expression
The SpyTag is a short, unfolded peptide that can be genetically fused to exposed positions in target proteins. It is used in the construct to recognize the corresponding molecule, Catcher, and form a covalent isopeptide bond between the side chains of an reactive aspartate and lysine in SpyCatcher (Hatlem et al. 2019).
Usage and Biology
The SpyTag/SpyCatcher system is based on a modified domain from a streptococcus pyogenes surface protein (SpyCatcher), which recognizes a cognate 13-amino-acid peptide (SpyTag), which can bind spontaneously and form an isopeptide bond (Hatlem et al. 2019).
References
1. Hatlem, Daniel; Trunk, Thomas; Linke, Dirk; Leo, Jack C. (2019): Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins. In: International journal of molecular sciences 20 (9). DOI: 10.3390/ijms20092129.