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Literature summary for 3.4.22.70 extracted from
- Site-specific protein modification on living cells catalyzed by Sortase (2008), Chembiochem, 9, 802-807.
Application
| Application | Comment | Organism |
|---|---|---|
| molecular biology | a general strategy for the site-specific modification of cell surface proteins with synthetic molecules by using sortase, a transpeptidase from Staphylococcus aureus. The short peptide tag LPETGG is genetically introduced to the C terminus of the target protein, expressed on the cell surface. Subsequent addition of sortase and an N-terminal triglycine-containing probe results in the site-specific labeling of the tagged protein. C-terminal-specific labeling of osteoclast differentiation factor with a biotin- or fluorophore-containing short peptide on the living cell surface. The labeling reaction occurrs efficiently in serum-containing medium, as well as serum-free medium or PBS. The labeled products are detected after incubation for 5 min. In addition, site-specific proteinprotein conjugation is successfully demonstrated on a living cell surface by the Sortase-catalyzed reaction. This strategy provides a powerful tool for cell biology and cell surface engineering | Staphylococcus aureus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Staphylococcus aureus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Staphylococcus aureus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| His6-SrtA | Staphylococcus aureus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| sortase A | - |
Staphylococcus aureus |
| SrtA | - |
Staphylococcus aureus |
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