Difference between revisions of "Part:BBa K3117037"

 
 
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<partinfo>BBa_K3117037 short</partinfo>
 
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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).
  
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===Usage and Biology===
 
===Usage and Biology===
  
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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).
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K3117037 SequenceAndFeatures</partinfo>
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===References===
  
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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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===Functional Parameters===
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<partinfo>BBa_K3117037 parameters</partinfo>
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Latest revision as of 01:33, 22 October 2019


SpyTag (E.coli 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.