Thiol Biotinylation

Biotinylation is the attachment of biotin to proteins or other biological macromolecules and can be used to target specific functional groups such as primary amines, sulfhydryls, carboxyl groups and carbohydrates. Biotin-avidin/streptavidin systems are often used for efficient detection or purification of proteins. Sulfhydryl groups, namely sulfhydryl groups (-SH), are also a commonly used class of biotin labeling sites. The thiol group exists on the surface in the form of a disulfide bond (sometimes in a free state), and after reduction, it selectively reacts with maleimide in the form of mercapto alcohol to form a stable thioether bond. The addition reaction has fast reaction and high selectivity under the condition of neutral pH, and is a commonly used biomarker reaction. Compared with amino labeling, the labeling site of thiol biotinylation is limited to cysteine, and the labeling has little effect on the biological activity of the protein.

Alfa Chemistry offers a wide range of biotinylation strategies and protocols to meet customer needs. We have experienced and dedicated scientific researchers to select suitable solutions and provide technical support for biotinylation projects. Over the years, we have gained industry acclaim for our efficient and reliable biotinylation services. Related services that we can improve include but are not limited to:

• Thiol biotinylation service
• Efficient biotinylation detection
• Labeling and purification services

Thiol biotinylation services

The thiol group (-SH) is a commonly used biotin labeling site. Sulfhydryl groups exist on the surface of biomolecules in the form of disulfide bonds. Sulfhydryl biotinylation is a typical redox post-translational modification of proteins, a non-enzymatic reversible process of disulfide bond formation, which can be used to label protein cysteine and other sulfhydryl-containing substrates. Alpha Chem focuses on efficient biotinylation services, we can provide professional thiol biotinylation solutions and strategies, and continue to innovate to meet customer needs.

Figure 2. We offer a wide range of biotinylation strategies and solutions to meet customer needs

Avidin-biotin interaction

The interaction between biotin and avidin is a useful tool for non-radioactive methods of purification, detection, immobilization, labeling, viral vector targeting, and drug targeting systems. The interaction between biotin-avidin/streptavidin is the strongest force known so far, and is not easily affected by pH, temperature, and organic solvent factors.

What can we offer?

• High-performance biotinylation reagents
• Fast labeling and purification services
• Optimized solutions and wide strategies

The features of biotinylation platform

• We support biotinylation service requirements for different types of functional groups
• Biotinylated peptides play an important role in immunoassays
• Thiol-targeted antibody biotin for better control of labeling reactions and purification processes
• Enables simple and efficient biotinylation and intracellular labeling of antibodies, proteins, and other primary amine-containing molecules

Alfa Chemistry has a professional biotinylation platform, strictly controls quality and continuously improves industry standards. If you want to know more about our services, please contact us immediately.

References:

1. Petri. S; et al. In vitro enzymatic biotinylation of recombinant Fab fragments through a peptide acceptor tail. Bioconjugate Chem. 1998, 9(6): 725-735.
2. Zhong. H.F.; et al. Advances in the application of affinity separation for analyzing protein ubiquitination. Chinese Journal of Chromatography. 2021, 39 (1): 26-33.

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