In Vivo Site-Specific Biotinylation

Biotinylation of recombinant proteins in vivo and in vitro, mainly by a chemoselective reaction between cysteine-biotin and a thioester group at the C-terminus of the protein. The binding between biotin and streptavidin is the strongest covalent biological interaction known and has a wide range of applications in the field of biology. Labeling purified proteins with biotin is an effective method for protein capture, immobilization and functionalization. Site-specific biotinylation of proteins in vivo can be achieved by cellular co-expression of a protein of interest fused to a biotin acceptor peptide (BAP) and a biotin ligase. As a biopharmaceutical and biotechnology service company, Alfa Chemistry has established a comprehensive technology platform that can provide professional in vivo and in vitro biotinylation services. We have professional scientific researchers who can design personalized biotinylation strategies according to the characteristics of target samples, and can establish advanced site-specific biotinylation platforms to meet customer needs.

The Services

Alfa Chemistry can provide site-specific biotinylation services. With a unique biotinylation system, it can achieve site-specific biotinylation while eliminating interference. The related site-specific biotinylation services we can provide include but are not limited to:

• Antigen biotinylation in vivo
• Purification of biotinylated molecules
• quantitative analysis
• Determination of biotinylation efficiency
• In vivo site-specific biotinylation

About site-specific biotinylation

The avidin-biotin system is a fundamental technique in biomedicine for immunolocalization, imaging, nucleic acid blotting, and protein labeling. Protein or viral gene therapy vectors can be site-specifically biotinylated for conjugation with other biotins. The biotin-antibiotin interaction is characterized by high affinity and specificity, and has been widely used as a high-efficiency biomarker. The high specificity of site-specific biotinylation of recombinant proteins can be used to avoid many problems and overcome limitations. At present, more and more studies can be used for site-specific biotin labeling, such as site-specific biotin-labeled recombinant IgG affinity peptides, on the basis of ensuring sufficient binding activity, to achieve detection sensitivity, specificity and stability.

What can we provide?

• Adhere to the independent development route
• Focus on a broad range of biotinylation solutions and strategies to accommodate site-specific biotinylation of a variety of samples
• Support biotinylation detection project management, provide professional data analysis
• Optimized service process, saving time, labor and money
• Professional biotinylation platform, perfect service system, suitable for biotinylation of a wide range of samples

Why choose us?

At Alfa Chemistry, our scientific research team focuses on the analysis of biotinylated samples to provide high-quality biotinylation solutions and strategies. Our experts insist on optimizing the service system, improving the biotinylation service system, and have the ability to provide customers with comprehensive biotinylation services. In the future, we will insist on innovation, continuous development, and make unremitting efforts to meet the needs of customers.

Alfa Chemistry has established a comprehensive biotechnology service platform, focusing on efficient biotinylation strategies and providing professional in vivo and in vitro biotinylation services. If you are interested in our services, please contact us immediately.

References:

1. Andrea. P.; et al. In vivo site-specific biotinylation of proteins within the secretory pathway using a single vector system. BMC Biotechnol. 2008, 18(8): 41.
2. Souvik. C.; et al. Strategies for site-specific protein biotinylation using in vitro, in vivo and cell-free systems: toward functional protein arrays. Nature Protocols. 2006, 1: 2386-2398.

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

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