In Vitro Enzymatic Biotinylation of Proteins

Enzymatic protein biotinylation is involved in important life activities. Biotin exhibits biological activity only when covalently attached to metabolic enzymes. Usually, enzymatic protein biotinylation can only be attached to proteins by biotin ligase, which can be widely used in biochemistry, cell biology and bioassay technology. Biotin can be covalently attached to the active sites of certain enzymes that transfer carbon dioxide from bicarbonate to organic acids to form cellular metabolites. The linking of biotin to protein by biotin ligase has high specificity, which can realize protein biotinylation in vivo or in vitro. The biotinylation reaction is an important tool for studying protein interactions, gaining high specificity and stability from the biotin and streptavidin system. The biotin-avidin/streptavidin system is widely used in various biotechnological and in vitro diagnostics.

The Services

Alfa Chemistry has a professional biotinylation technical team that can provide efficient in vitro biotinylation strategies and support high-throughput biotinylation services. We are committed to expanding a wide range of biotinylation services, including but not limited to:

• Efficient in vitro biotinylation strategy
• Biotinylated western blot detection
• Expression, purification and identification of biotinylation
• Biotinylated hexd detection
• Genome vector construction
• Professional data analysis
• Biotinylation degree detection

In vitro enzymatic biotinylation

• Enzymatic biotinylation has highly specific binding and can efficiently biotinylate any protein in vitro
• Mild reaction conditions for enzymatic biotinylation
• Biotin suitable for enzymatic biotinylation with low mass and space

Enzymatic biotinylation reaction

Biotin protein ligase (BPL) is a specific lysine enzyme that links biotin to the biotinidase active site. In E. coli, the biotin carboxyl carrier protein (BCCP) subunit of lysine residue acetyl-CoA carboxylase is recognized and biotinylated by BirA (BPL of E. coli). The biotinylation reaction is the formation of an amide bond between the carboxyl group of biotin and the modified lysine. Every organism has a BPL-encoding gene for efficient biotinylation. The BPL of Escherichia coli controls the biotin synthesis mechanism and controls the interaction between the substrate ATP and biotin, which provides an important direction for future research on biotin. With the rapid development of protein in vitro biotinylation technology, it is more and more used in the field of life sciences, such as antibody preparation, western blot detection, drug development and biological detection.

What can we provide?

Alfa Chemistry is committed to high-quality biotinylation services. In addition to experienced staff, we are also equipped with an efficient quality control platform to meet customer needs with efficient services.

• Professional biotinylation strategies and solutions
• Efficient biotinylation service
• Professional data analysis
• Strict biotinylation quality control platform

Alfa Chemistry provides efficient in vitro protein biotinylation services to meet customers' needs. If you are interested in our services, please contact us immediately.

References:

1. Petri. S.; et al. In vitro enzymatic biotinylation of recombinant Fab fragments through a peptide acceptor tail. Bioconjugate Chem. 1998, 9(6): 725-735.
2. Marta. F.S.; et al. Protein−protein interaction detection in vitro and in cells by proximity biotinylation. J. Am. Chem. Soc. 2008, 130(29): 9251-9253.

※ It should be noted that our service is only used for research, not for clinical use.