Cy7-Lys-LPETGG Sortase A Peptide is built around the LPETG/LPETGG recognition sequence used by Staphylococcus aureus Sortase A (SrtA). Sortase-mediated ligation, often called sortagging, is a widely used enzymatic method for site-specific peptide and protein modification. Sortase A Recognition of LPXTG Sortase A recognizes a C-terminal LPXTG motif, where X can vary. The enzyme cleaves the peptide bond between threonine and glycine and forms a transient thioacyl enzyme intermediate. An N-terminal oligoglycine nucleophile can then attack this intermediate to generate a new peptide bond. Because recognition is encoded by short peptide motifs, sortase chemistry can be used to attach synthetic peptides, fluorophores, polymers, lipids, proteins, surfaces, and other research components under relatively mild aqueous conditions. LPETG and LPETGG Research Peptides LPETG is one of the most frequently used experimental sortase recognition motifs. LPETGG derivatives retain the core LPETG sequence while adding an additional glycine that can be useful in synthetic design or handling. Special Feature of LT8725 Cy7 provides near-infrared fluorescence suitable for long-wavelength detection. Product sequence: Ac-K(Cy7)-LPETGG Sortase-recognition core: LPETGG Potential Research Applications - Sortase A substrate studies
- Site-specific protein labeling
- Peptide-protein ligation
- Protein immobilization
- Fluorophore installation
- Nanoparticle or surface conjugation
- Antibody and recombinant-protein modification
- Sortase reaction optimization
References Pishesha N, et al. Engineered Sortases in Peptide and Protein Chemistry. ChemBioChem. 2021.
Public source / publication Schmidt M, et al. Sortase-Mediated Ligation of Purely Artificial Building Blocks. Biomacromolecules. 2019.
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Peptide Carrier Protein Conjugation Research Use Only. Not for human, diagnostic, clinical, or therapeutic use. | 