In Vivo Biotinylation Service

The biotin-avidin/streptavidin system is a new type of biotinylated amplification system developed in the 1970s, which can be successfully applied to biomarkers and has become a research tool in the field of qualitative and quantitative detection of trace antigens and antibodies. The combination of biotin and streptavidin is the strongest known covalent biological interaction and has a wide range of applications in the field of biology. In addition to efficient biocoupling with avidin, biotin can also combine with streptavidin and neutravidin, which can amplify the signal of biotinylation reaction and greatly improve the detection sensitivity of proteins. Labeling purified proteins with biotin is an efficient method for protein capture, immobilization, and functionalization. Alfa Chemistry is committed to building a stable in vivo biotinylation system, can provide efficient in vivo biotinylation solutions and strategies, and develop and expand molecules suitable for biotinylation reactions to meet customer needs.

The Services

As a biotechnology service company, Alfa Chemistry has established a complete technical platform to provide professional in vitro biotinylation services. We have professional scientific research personnel to provide customized biotinylation strategies to meet the needs of customers. The in vivo biotinylation services we can provide include but are not limited to:

• In vivo biotinylation assay

Biotinylation takes advantage of the strong binding force and high specificity of biotin to the nucleophilin/streptavidin system, and has great application potential in purification or detection. Proteins can be biotinylated by biotin ligases in vivo or in vitro for protein immobilization, detection, purification and visualization.

• In vivo biotinylation of antigens

An antigen is a substance that elicits an immune response and binds to specific antibodies in the environment for potential biological therapy. Antibody responses can lead to enhanced autoimmune diseases, malignancies, or infections, so providing high-quality antigens is of great importance for the development of specific protein-targeting antibodies.

• In vivo biotinylation to study protein interactions

Interactions between proteins are part of cellular networks, similar basic structures in cells. Cellular proteins can interact and couple with large cellular proteins in ways that affect cellular pathways.

• In vivo site-specific biotinylation

Site-specific biotinylation of proteins in vivo can be achieved through cellular coexpression of a protein of interest fused to a biotin acceptor peptide (BAP) and a biotin ligase.

• In vivo biotinylation system

The biotin-avidin/streptavidin system can be successfully applied to biomarkers and has become a new technology in the field of qualitative and quantitative detection of trace antigens and antibodies.

• In vivo biotinylated expression system

Biotin can bind avidin or streptavidin with very high affinity, forming a biotin-avidin/streptavidin system. The high affinity between biotin and avidin or streptavidin has been widely used in biochemistry and molecular biology, often for efficient protein detection or capture.

• 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, strong anti-interference ability, and not easily affected by temperature, pH and proteolysis. Biotinylated proteins can be purified in one step with high-affinity avidin or streptavidin.

Advantages and disadvantages of biotinylation in vivo

In vivo biotinylation and target protein fusion, as E. coli biotinidase synthetase (BirA), can catalyze the efficient biotinylation of fusion protein. Selecting the appropriate biotinylated protein system for expression and analysis is of great significance to enhance the degree of biotinylation. Compared with traditional immunoaffinity methods, in vivo biotinylation has many advantages in the purification of protein complexes:

• The biotin-streptavidin system has high binding capacity and can be washed under stringent conditions, thereby reducing background binding.
• There are few naturally biotinylated proteins, which can reduce the chance of cross-reaction.
• In vivo biotinylation avoids the need to generate protein-specific antibodies.

Potential limitations are as follows:

• Biotinylation in vivo requires more time and effort to perfect the system
• Ectopic expression of proteins significantly above endogenous levels may lead to spurious protein complexes and increase nonspecific DNA binding

Figure 2. High-quality and efficient in vivo biotinylation system to meet professional biotinylation service requirements

Why choose us?

Alfa Chemistry focuses on the analysis and experiments of biotinylated samples, and provides efficient biotinylation solutions for global customers to meet biotinylation-related needs. The services we provide have the following advantages:

• We have self-developed expansion routes
• Broad range of biotinylation solutions and strategies
• Efficient in vivo biotinylation system
• Professional data analysis
• Services that support globalization
• Optimize service process

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

References:

1. 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.
2. Li, Y.F.; et al. Novel system for in vivo biotinylation and its application to crab antimicrobial protein scygonadin. Biotechnol Lett. 2012, 34(9): 1629-1635.
3. Paul. A.S.; et al. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Research. 1998, 26(6): 1414-1420.

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

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