Sortase A 5M Recombinant Protein

Sortase A is a transpeptidase derived from Gram-positive bacteria. It specifically recognizes the LPXTG peptide motif in proteins and cleaves between Thr and Gly, followed by a transpeptidation reaction with molecules carrying an N-terminal oligoglycine motif. This enables a wide range of applications, including protein tag removal, site-specific labeling, antibody conjugation, and construction of multifunctional fusion proteins. Compared with traditional random chemical labeling methods, Sortase A-mediated site-specific ligation offers clearly defined reaction sites, controlled conjugation orientation, well-defined product structures, and high reproducibility. It is particularly suitable for antibody engineering, Fc fusion proteins, ADC construction, and protein engineering studies involving proteins that are sensitive to conformational or activity changes. More about the mechanism of Sortase A >>

Sortase A 5M is a high-activity engineered Sortase A variant obtained through directed evolution. It contains five key mutations: P94R, D160N, D165A, K190E, and K196T. While maintaining the recognition specificity for the LPXTG sequence, Sortase A 5M significantly improves transpeptidation efficiency and compatibility with complex substrates. DIMA BIOTECH now provides recombinant Sortase A 5M protein, which can be used for tag removal, site-specific biotinylation, fluorescent labeling, and site-specific antibody conjugation. For this recombinant Sortase A 5M protein, DIMA BIOTECH has completed multiple internal functional validations, including C-terminal site-specific biotinylation of BCMA-hFc followed by ELISA validation of its dose-dependent binding to BAFF-hFc, site-specific biotinylation of anti-B7-H3 antibody for Sandwich ELISA detection, and PE site-specific conjugation of anti-B7-H3 antibody with flow cytometry validation of its cell-binding activity. These results demonstrate that the protein serves as a stable and reliable enzymatic tool for protein engineering and antibody functionalization studies.