Difference between revisions of "Part:BBa K4623001"
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<partinfo>BBa_K4623001 short</partinfo> | <partinfo>BBa_K4623001 short</partinfo> | ||
| − | Streptavidin is a tetramer protein, and one molecule of streptavidin can bind to tetramolecular biotin with high specificity. The dissociation constant of streptavidin-biotin complex is on the order of 10mol/L, which is a very perfect biotin-binding protein, and its application range is wider than that of avidin, which is also commonly used in biology. Monomeric streptavidin called mSA has been developed by scientists through amino acid mutations and has the highest affinity for biotin among current monovalent streptavidins, with an affinity of 2.8nM. | + | Streptavidin is a tetramer protein, and one molecule of streptavidin can bind to tetramolecular biotin with high specificity. The dissociation constant of streptavidin-biotin complex is on the order of 10mol/L, which is a very perfect biotin-binding protein, and its application range is wider than that of avidin, which is also commonly used in biology. Monomeric streptavidin called mSA has been developed by scientists through amino acid mutations and has the highest affinity for biotin among current monovalent streptavidins, with an affinity of 2.8nM<sup>[1]</sup>. |
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K4623001 SequenceAndFeatures</partinfo> | <partinfo>BBa_K4623001 SequenceAndFeatures</partinfo> | ||
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| + | [1]Lim KH, Huang H, Pralle A, Park S. Stable, high-affinity streptavidin monomer for protein labeling and monovalent biotin detection. Biotechnol Bioeng. 2013 Jan;110(1):57-67. doi: 10.1002/bit.24605. Epub 2012 Aug 8. PMID: 22806584. | ||
Revision as of 12:42, 11 October 2023
Monomeric streptavidin(mSA)
Streptavidin is a tetramer protein, and one molecule of streptavidin can bind to tetramolecular biotin with high specificity. The dissociation constant of streptavidin-biotin complex is on the order of 10mol/L, which is a very perfect biotin-binding protein, and its application range is wider than that of avidin, which is also commonly used in biology. Monomeric streptavidin called mSA has been developed by scientists through amino acid mutations and has the highest affinity for biotin among current monovalent streptavidins, with an affinity of 2.8nM[1].
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 82
Illegal AgeI site found at 142 - 1000COMPATIBLE WITH RFC[1000]
References:
[1]Lim KH, Huang H, Pralle A, Park S. Stable, high-affinity streptavidin monomer for protein labeling and monovalent biotin detection. Biotechnol Bioeng. 2013 Jan;110(1):57-67. doi: 10.1002/bit.24605. Epub 2012 Aug 8. PMID: 22806584.