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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.
Public source / publication Related LifeTein Services
Custom Peptide Synthesis
Fluorescent Peptide Labeling
Peptide Click Chemistry and Conjugation
Peptide Carrier Protein Conjugation
Research Use Only. Not for human, diagnostic, clinical, or therapeutic use.
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