Biotin Labeled Proteins

BOC Sciences has been focusing on custom synthesis, and has accumulated many years of experience in molecular coupling and labeling. There are abundant researches on biotin labeling and biotin modification, such as protein biotinylation and antibody biotinylation.

Fig.1 Direct detection of biotinylated proteins by mass spectrometry. (Schiapparelli et al., 2014)

Biotinylation of Proteins

Biotinylation is the process of attaching biotin to proteins and other macromolecules. Detection and purification of proteins and antibodies are accomplished with this method. Aside from biotin's strong affinity for amphiphiles, it has two properties that make it ideal for labeling proteins and macromolecules. In the first place, biotin is smaller than globular proteins, minimizing interference with many proteins, and allowing multiple biotin molecules to bind to an individual protein, therefore maximizing anti-biotin detection. Second, biotin has valeric acid side chains that can be easily derivatized and attached to reactive portions of chemical structures without altering the antibiotin protein's binding function.

Services for Biotinylated Proteins

Using the characteristics of the biotin-affinity system, proteins can be biotinylated to bind specifically to affinity proteins for the purposes of antigen-antibody recognition detection, biomolecule capture, and protein interaction detection.

How to Biotinylate Protein

(1) Biotinylated proteins are obtained by chemical biotin labeling method after protein purification. Usually, the carboxyl group of biotin can be chemically modified to make a variety of active group derivatives, and then chemically reacted with proteins.

(2) Biotinylation of proteins is achieved by fusion expression of Avitag with proteins and biotinylation of the biotin tag in vitro. This specific targeted modification has little effect on the activity of the protein and the product is specialized, but this method must fuse the target protein with the biotin tag for fusion expression, and then purify to obtain a high-purity product.

Protein Biotinylation Considerations

• Solubility - The solubility of the biotinylated reagent greatly affects the ability to label the target protein or other macromolecules.
• Length of spacer arm - Binding of biotin to anti-biotin proteins is affected by the length of the spacer arm.
• Cleavability/Reversibility - Captured biotinylated proteins can be recovered or purified by cleavage of the biotin molecule from the target protein or reversal of the attenuated biotin-affinity interaction.
• Functional groups - Specific reactive portions bind to any amino acid or a functional group of specific amino acids, respectively, for non-selective or targeted biotinylation.

Why Choose BOC Sciences?

Product Delivery

Depending on the customer's needs and the performance characteristics of the product, we will provide records of the synthesis of biotin labeled proteins (original synthesis records, etc.) as well as data reports from HPLC, GC, MS and NMR.

Full Time Employment (FTE)

We provide our clients with a research team that works full-time on their projects, and sends experimental progress reports and analytical test data directly to clients, oriented to their needs.

Product and Innovation Capabilities

Our products and solutions are often high value-added and can make a significant contribution to environmental sustainability. BOC Sciences has a high diversity of products and our team has the research, development and innovation capabilities to accelerate innovation and product development.

Project Workflow

Frequently Asked Questions (FAQ)

How are proteins labeled with biotin?

Biotin labeling of proteins typically involves covalently attaching biotin to specific amino acid residues, such as lysines or cysteines, on the protein's surface. This is usually achieved through chemical conjugation using biotinylated reagents, which react with the protein under controlled conditions to form a stable bond. The degree of biotinylation can be controlled depending on the application.

What are the main applications of biotin-labeled proteins in molecular biology?

Biotin-labeled proteins are widely used in molecular biology for applications like protein-protein interaction studies, immunoprecipitation, and affinity purification. The strong and specific binding between biotin and streptavidin allows for easy isolation and detection of proteins from complex mixtures, enabling researchers to study protein behavior and interactions in detail.

How does biotin labeling enhance protein detection in assays?

Biotinylation improves protein detection in assays by using the high affinity between biotin and streptavidin or avidin. This allows for highly sensitive detection using biotin-specific probes, such as biotinylated antibodies or enzymes, which amplify the signal in applications like ELISA, Western blotting, or immunohistochemistry.