Chemical Biotinylation

Biotin-avidin interactions are often used to detect and/or purify proteins because the two molecules are highly specific for each other. Biotinylation is the process of attaching biotin to proteins and other macromolecules. Biotinylation reagents can be used to target specific functional groups or residues, including primary amines, thiols, carboxyls, and carbohydrates. Biotin is an ideal choice for labeling proteins and biomacromolecules, mainly due to its advantages of small molecular weight, strong anti-interference ability and high specific binding. The biotinylation reaction is fast, efficient and less susceptible to interference from environmental factors such as temperature, pH and proteases. Alfa Chemistry has established a professional biotinylation platform, focusing on providing suitable solutions and strategies for a variety of biological samples, constantly optimizing the service system, and insisting on meeting customer needs with high-quality services.

Alfa Chemistry focuses on efficient biotinylation services, provides a wide range of biotinylation strategies and solutions, and constantly improves the service system. We provide professional chemical biotinylation services, including but not limited to:

• Amine biotinylation

Amine groups can covalently form amide bonds with functional groups of carboxylic acids, which are the most common biomarker targets and are commonly used for biotinylation. Amino biotinylation reagents are divided into common N-hydroxysulfosuccinimide (NHS) and sulfonated N-hydroxysulfosuccinimide (Sulfo-NHS).

• Thiol biotinylation

Thiol groups exist on the surface in the form of disulfide bonds (sometimes in a free state), and after reduction, they selectively react with maleimide in the form of thiol alcohols to form stable thioether bonds. The addition reaction has a fast reaction speed and high selectivity under neutral pH conditions, and is a commonly used biomarker reaction.

• Carbonyl biotinylation

Carbonyl groups do not exist in natural materials in nature, but proteins can generate carbonyl groups through oxidation, which can be used for biotinylation labeling.

• Carboxylic acid biotinylation

Carboxylic acids are common functional groups present in proteins, peptides, polymers or other biomolecules. Amino-modified biotin can be used to label carboxylic acids for efficient biotinylation. Besides carboxylic acids, other functional groups can also react with amino groups to obtain effective biomarkers.

• Chemical biotinylation with biotin isothiocyanate

Thiocyanate (-NdCdS) is a bioconjugated functional group that reacts with the amine group of lysine residues and the N-terminus of proteins to form a stable thiourea moiety.

Biotinylation service features

• Protein labeling: we specialize in biotinylation services, which can be used for efficient biodetection and biomarking
• Hydrophobic: for intracellular or extracellular biotinylation

About avidin-biotin interaction services

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. Alfa Chemistry provides customers with high-quality biotinylation services to meet their needs.

Figure 2. Comprehensive biotinylation services to meet customer needs

The features of biotinylation platform

Alfa Chemistry has perfected the advanced service system and established an advanced biotinylation platform, which has the following high quality and characteristics:

• Biotinylation services play an important role in immunoassays
• Simple and efficient biotinylation and intracellular labeling of antibodies or proteins

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. Kenneth. K.W.L.; et al. Rhenium(I) polypyridine biotin isothiocyanate complexes as the first luminescent biotinylation reagents: synthesis, photophysical properties, biological labeling, cytotoxicity, and imaging studies. Inorg. Chem. 2008, 47( 2): 602-611.

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