In Vivo Biotinylation of Peptide Complexes

Biotinylation, the process of covalently attaching biotin to proteins, nucleic acids, or other biomolecules. The biotinylation reaction is fast, efficient and has strong anti-interference ability, and is not easily affected by temperature, pH and proteolysis. Biotinylated proteins can be purified in one step with high-affinity avidin or streptavidin. Biotin ligase (Biotin Protein Ligase) is used to catalyze the biotinylation reaction and is also a biotin-induced inhibitor. A common biotin ligase is the BirA enzyme in Escherichia coli, which has a wide range of applications in biomedicine. The BirA enzyme can recognize a polypeptide sequence, and when the fusion protein and the BirA enzyme are co-expressed, the sequence of the fusion protein can be effectively biotinylated. Coexpression of the peptide complex and the BirA enzyme allows for efficient in vivo biotinylation, resulting in the generation of histocompatibility complex (MHC) tetramers. Researchers are committed to developing efficient biotinylation strategies through co-expression of BirA enzymes and other biological systems to maximize biotinylation efficiency. Alfa Chemistry focuses on providing customers with high-quality biotinylation services to meet their needs.

The Services

In Alfa Chemistry, researchers are committed to the development of biotinylation systems, working on efficient biotinylation solutions, and providing efficient in vivo peptide complex biotinylation services, including but not limited to:

• Biotinylated expression and purification of peptide complexes
• Determination of the degree and efficiency of biotinylation
• Tetramer staining
• Western blot analysis
• Quantitative analysis

Biotinylation step catalyzed by BirA enzyme

• Reaction of biotin and ATP, this process fixes the activated biotin on the active site of BirA enzyme
• Activated biotin is coupled to specific lysine residues by reaction

Peptide modification: biotinylation

There is a stable non-covalent interaction between avidin and biotin, and it has a high affinity with avidin, mycoprotein, and streptavidin. The interaction between biotin-avidin is one of the strongest interactions known, which can be used for protein purification, detection, immobilization, protein structure analysis and drug targeting. Biotin-labeled peptides are easily bound to avidin for detection and purification, such as western blotting, ELISA, immunoprecipitation, peptide affinity purification, immunomics and cell surface labeling. Biotinylated peptides are used as bait-binding components, and in vivo biotinylated proteins can be obtained and purified using streptavidin.

Our service advantages

• Efficient R&D route, focusing on the efficient biotinylation reaction of peptide complexes
• Broad range of biotinylation solutions and strategies
• Professional team, providing accurate data analysis
• Optimized service process
• Responsive biotinylation project
• Professional biotechnology team, pioneering biotinylation service
• Support global payments
• Insist on innovation and continuous development

Alfa Chemistry provides professional in vivo peptide complex biotinylation services, focusing on high-quality biotinylation solutions and strategies, and supporting responsive biotinylation projects. If you are interested in our services, please contact us immediately.

Reference:

1. Yang. J.B.; et al. In vivo biotinylation of the major histocompatibility complex (MHC) class II/peptide complex by coexpression of BirA enzyme for the generation of MHC class II/tetramers. Human Immunology. 2004,65(7): 692-699.

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