Description
Sortase A was able to specifically recognize the protein containing the conserved amino acid sequence LPXTG at the C-terminus and polyglycine at the N-terminus (X was any amino acid except cysteine and tryptophan). The cysteine at position 184 in Sortase A attacks the peptide bond between the threonine/glycine in the substrate recognition sequence LPXTG, which breaks the peptide bond and forms an acylase intermediate between the enzyme and the substrate. The polyglycine attacks the acylase intermediate and forms a new peptide bond between the substrate and the polyglycine to complete the transpeptide reaction. We have directional protein refolding technology (LeaBioFOLD) and self-developed technology platforms for proteins covering screening and purification, engineering design, fixed-point coupling design, and dosage form development. Protein refolding is a process of recovering protein aggregates in inclusion bodies in the form of misfolded and inactive proteins expressed by prokaryotes such as Escherichia coli back into proteins with correct conformation and bioactivity under appropriate conditions in vitro. It is a key technology for biopharmaceutical companies but a major bottleneck in protein production in prokaryotic expression systems. Leading Biology has been specializing in protein refolding for many years, has a core team with over ten years of experience in this technology and rich experience in its industrialization. Our team is summarizing the experience to form an independent technological system of ours