Difference between revisions of "Part:BBa K4623001"
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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>.
 
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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===Usage and Biology===
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Compared to the native recombinant streptavidin tetramer (55 kD), the binding capacity to biotin is equivalent, even the binding effect with biotin-labeled ligands is superior. Overall, it is more effective in avoiding steric hindrance effects due to spatial positioning. Additionally, it can prevent the crosslinking effects caused by tetrameric streptavidin that may lead to aggregation or precipitation, resulting in better experimental reproducibility. The smaller size of mSA allows for easier spatial access to targets, leading to improved labeling efficiency.
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===Characterization===
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Revision as of 09:39, 1 October 2024


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].

Usage and Biology

Compared to the native recombinant streptavidin tetramer (55 kD), the binding capacity to biotin is equivalent, even the binding effect with biotin-labeled ligands is superior. Overall, it is more effective in avoiding steric hindrance effects due to spatial positioning. Additionally, it can prevent the crosslinking effects caused by tetrameric streptavidin that may lead to aggregation or precipitation, resulting in better experimental reproducibility. The smaller size of mSA allows for easier spatial access to targets, leading to improved labeling efficiency.

Characterization

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 82
    Illegal AgeI site found at 142
  • 1000
    COMPATIBLE 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.