Biotinylated Protein Isolation

In biology, efficient molecular labeling is usually performed by covalently binding to proteins of interest for further processing and analysis, such as detection, purification or separation. Biotinylation is the process of attaching biotin to proteins and other biomacromolecules, which can be used for protein detection, purification or separation. The binding ability between biotin and avidin or streptavidin is strong, highly specific, and suitable for most proteins. Whether it is protein research or application, it is usually necessary to express proteins efficiently, followed by purification and separation. Alfa Chemistry can develop a variety of methods for labeling biotinylated proteins, provide a variety of efficient biotinylated protein labeling strategies, and support efficient separation from complex environments to meet customers' wide range of uses.

The Services

Alfa Chemistry can provide services related to biotinylated protein labeling and separation including but not limited to:

• Efficient protein isolation strategies
• Professional data analysis
• Biotinylated protein sample preparation and purification
• Characterization of biotin and protein interactions
• Processing of biotinylated samples

The process of protein isolation and purification

Proteins are involved in important physiological activities and usually exist in the form of complex mixtures. Efficient purification and separation of proteins is a difficult task. The purification and separation of proteins need to consider whether the biological activity and integrity of the protein are affected. Improving the purity or activity of the sample is the overall goal of protein purification. The process of protein purification can be roughly divided into:

• Material pretreatment and cell disruption: When separating or purifying proteins, it is necessary to release proteins from tissues or cells. Mechanical disruption methods, osmotic disruption methods, ultrasonic methods and enzyme methods can be used.
• Extraction of protein: Choose appropriate buffer reagent to extract protein, and pay attention to the experimental environment to avoid inactivation and denaturation of protein
• Obtaining crude samples: Separating the target protein from other impurity proteins.
• Preparation of high-purity samples: The above samples are not pure enough, and further purification and separation are needed. The commonly used methods are gel filtration chromatography, ion exchange cellulose chromatography and affinity chromatography.

Figure 2. Protein isolation and purification process

Why is biotin the best choice for labeling proteins?

The interaction between biotin and protein is very strong, and biotin is smaller than other labeling reagents, which can avoid interference to a large extent. Multiple biotin molecules can be combined with the same protein, so as to realize the efficient detection of biotinylated protein, so as to achieve the purpose of its purification and separation. Due to the structure of biotin, it is easy to combine with the reactive part and will not affect the function of biotinylated protein.

Alfa Chemistry provides efficient protein biotinylation fixation services, provides a wide range of biotinylation strategies, and insists on meeting customer needs. If you are interested in our services, please contact us immediately.

References:

1. James. D. H.; et al. Easily reversible desthiobiotin binding to streptavidin, avidin, and other biotin-binding proteins: uses for protein labeling, detection, and isolation. Analytical Biochemistry. 2002, 308(2): 345-357.

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