Biotin is a water-soluble small molecule of vitamin B family, which can bind to avidin or streptavidin with high affinity and high specificity. Biotinylation is the process of covalently attaching biotin to biomolecules, either chemically or enzymatically. The biotin-avidin/streptavidin system is one of the strongest known non-covalent interactions and is resistant to a variety of factors, making it widely used in bioscience and medicine. The linkage of biotin to proteins is a specific post-translational modification catalyzed by biotin ligases, the most common of which is the protein BirA from Escherichia coli. BirA is also known as biotin ligase, biotin operon repressor protein, biotin holoenzyme synthase, biotin-[acetyl-CoA carboxylase] synthase. The natural substrate of BirA is the biotin carboxy carrier protein (BCCP), which was fused to the protein of interest before a smaller tag was recognized.
Biotinylation is the process by which biotin is linked to a molecule of interest, and can be achieved in a biologically enzymatic manner. Enzymatic biotinylation is highly specific and allows for a predetermined orientation of avidin or streptavidin binding. Alfa Chemistry has long adhered to strict quality assurance and quality control practices to create reliable biotinylation services. We continue to improve industry standards and can provide customized biotinylation services according to customer needs, including but not limited to:
RNAs are involved in gene regulation processes in organisms (such as chromatin remodeling and transcriptional activation) and are also involved in many human diseases (cancer and neurodegenerative diseases). Efficient and accurate characterization of the roles of RNA and other biomolecules is critical for understanding RNA biology and developing new therapeutic strategies.
Biotin can be covalently attached to proteins, polypeptides or nucleic acids by chemical or enzymatic means. Currently, state-of-the-art techniques are used to capture protein networks and subcellular microenvironments in cells and organisms. Using biotin ligase, rapid protein biotinylation can be achieved.
Site-specific enzymatic biotinylation of recombinant proteins can be used to overcome the limitations of their use. Recombinant proteins can be labeled with biotin at predetermined sites, which can be done by biological enzymes. It has been reported that Escherichia coli biotin holoenzyme synthase (BirA) can be used to label recombinant proteins in Spodoptera frugiperda (Sf9) cells.
In biodiagnostics, streptavidin-coated tubes, microtiter wells, or spherical particles are used as multifunctional surfaces for capturing biotinylated antibodies in various forms of immune responses. Site-specific biotinylated Fab fragments were tested in streptavidin-coated microtiter wells and showed specific binding.
Figure 2. Continuously optimized biotinylation system in line with industry specifications to meet customer needs
Alfa Chemistry's research team can support specific binding according to the characteristics of samples, develop and expand biotinylation projects, and provide high-quality biotinylation services at competitive prices. If you are interested in our services, pleasecontact us immediately.
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※ It should be noted that our service is only used for research, not for clinical use.
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