Home / Services / Protein Engineering and Optimization / Protein Modification and Labeling Services / Protein Biotinylation Service

Protein Biotinylation Service

Online Inquiry

Protein biotinylation services offer precise and efficient solutions for attaching biotin molecules to proteins, enabling researchers to study protein interactions, purify proteins, and develop diagnostic assays with high sensitivity and specificity. Our protein biotinylation services provide comprehensive support from initial consultation to final validation, ensuring that your biotinylated proteins meet your specific research and biotechnological needs.

Protein Biotinylation (G Elia, et al.,2010)

Overview Service Process Examples and Solutions Frequently Asked Questions


Protein biotinylation involves the covalent attachment of biotin, a small vitamin molecule, to specific amino acids within a protein. This modification allows the protein to bind with high affinity to streptavidin or avidin, which are commonly used in various biochemical assays and purification techniques. Our services utilize advanced biotinylation techniques to achieve high specificity and efficiency, ensuring that your proteins retain their functionality and integrity after modification.

Methods for Protein Biotinylation

Method Description Applicable Scenarios
Chemical Biotinylation Involves the use of biotinylation reagents that react with specific amino acid residues (e.g., lysine, cysteine) on the target protein. Suitable for biotinylating purified proteins, proteins in cell lysates, or cell surface proteins in a straightforward and scalable manner.
Enzymatic Biotinylation Utilizes biotin ligase enzymes (e.g., BirA) that specifically attach biotin to a biotin acceptor peptide sequence fused to the protein of interest. Ideal for specific and targeted biotinylation of proteins, especially in live cells or organisms, allowing for precise experimental control.
In Vivo Biotinylation Involves expressing a fusion protein containing a biotin acceptor peptide in cells along with biotin ligase, resulting in biotinylation within the cell. Used for studying protein interactions, localization, and dynamics in living cells or organisms, enabling real-time analysis.
Photoactivatable Biotinylation Uses biotinylation reagents that become reactive upon exposure to light, allowing spatial and temporal control over the biotinylation process. Useful for studying dynamic processes and interactions in specific cellular regions or during specific time windows.
Site-Specific Biotinylation Achieved through the incorporation of a biotinylation tag at a specific site within the protein using genetic engineering or chemical methods. Suitable for ensuring biotin is attached at a specific site, minimizing potential interference with protein function and interactions.
Affinity-Based Biotinylation Employs affinity tags and biotin-binding proteins to capture and biotinylate target proteins selectively. Used in complex mixtures where selective biotinylation of target proteins is required, often in combination with other affinity-based techniques.

Each biotinylation method offers specific advantages depending on the experimental needs, such as the requirement for in vivo biotinylation, site-specific tagging, or control over the biotinylation process.

Service Process

The process of protein biotinylation involves several critical and interrelated steps:

  1. Project Consultation: Collaborating with researchers to define the specific biotinylation requirements, including the target protein, desired biotinylation sites, and intended application.
  2. Protein Expression and Purification: Producing and purifying the target protein in a suitable expression system to ensure high purity and yield.
  3. Biotinylation Reaction: Applying chemical or enzymatic biotinylation techniques to attach biotin to specific amino acids within the protein. This step ensures high specificity and efficiency.
  4. Purification of Biotinylated Proteins: Isolating the biotinylated protein using techniques such as affinity chromatography to ensure high purity and specificity.
  5. Characterization and Validation: Assessing the biotinylated protein's purity, biotinylation efficiency, stability, and functionality using methods such as SDS-PAGE, Western blotting, mass spectrometry, and activity assays.
  6. Optimization and Scale-Up: Refining the biotinylation process based on initial results and scaling up production to meet the required quantities for research or commercial use.

For more information about our Protein Biotinylation Services or to discuss your specific needs, please contact us. Our team of experts is available to provide guidance and support for your research and biotechnological projects, ensuring you achieve your scientific and industrial goals.

Examples and Solutions

The following table provides an overview of various case studies in protein biotinylation and the solutions we offer to support your research and biotechnological endeavors:

Case Study Description Solutions We Offer
Affinity Purification Biotinylating proteins to facilitate their purification using streptavidin affinity columns. Custom biotinylation, optimization of labeling conditions, and validation.
Interaction Studies Investigating protein-protein interactions using biotinylated proteins in pull-down assays. Biotin conjugation, protein purification, and interaction assays.
Diagnostic Assay Development Developing biotinylated proteins for use in ELISA and other diagnostic tests. Biotinylation, assay development, and validation.
Cell Surface Protein Labeling Labeling cell surface proteins with biotin for cell sorting and tracking. Cell surface biotinylation, validation, and cell sorting.
Functional Protein Studies Studying the function of biotinylated proteins in various biological contexts. Custom biotinylation strategies, functional assays, and analysis.
Enzyme Activity Assays Biotinylating enzymes to study their activity and interactions. Biotin conjugation, activity assays, and functional validation.

Frequently Asked Questions

Q: What is protein biotinylation?

A: Protein biotinylation involves the covalent attachment of biotin to specific amino acids within a protein. This modification enables the protein to bind with high affinity to streptavidin or avidin, facilitating various biochemical assays and purification techniques.

Q: How is protein biotinylation performed?

A: Protein biotinylation is performed through a series of steps including project consultation, protein expression and purification, biotinylation reaction, purification of biotinylated proteins, characterization and validation, and optimization and scale-up. Each step ensures the precise and efficient biotinylation of proteins.

Q: What are the applications of protein biotinylation?

A: Applications include protein purification, protein-protein interaction studies, diagnostic assays, cell surface labeling, and functional studies. Biotinylated proteins are essential tools for various research and biotechnological applications.

Q: What are the key steps in the protein biotinylation process?

A: Key steps include project consultation, protein expression and purification, biotinylation reaction, purification of biotinylated proteins, characterization and validation, and optimization and scale-up. These steps ensure the successful production of high-quality biotinylated proteins.

Q: Why is protein biotinylation important?

A: Protein biotinylation is important for advancing research, developing new diagnostic tools, and improving purification processes. It provides essential tools for studying and manipulating proteins with high precision in various biological and biotechnological contexts.

Please note that all services are for research use only. Not intended for any clinical use.

Get a free quote

If your question is not addressed through these resources, you can fill out the online form below and we will answer your question as soon as possible.


There is no product in your cart.