Protein Biotinylation Purification

In the era of post-gene sequencing, efficient identification and purification of proteins is of great significance to the development of protein biology. Currently, high-throughput biotinylation is one of the most common methods for protein labeling. Biotin is a naturally occurring metabolic enzyme cofactor that exhibits activity only when covalently attached to the enzyme by the action of a specific protein-biotin ligase. The binding of biotin and avidin is the strongest non-covalent interaction known in nature, so more and more purification methods based on high affinity have been developed for protein purification. The high affinity of biotin to avidin or streptavidin is not easy to be destroyed in a strict environment, and it can efficiently bind to proteins, reduce background binding, and make other substances easier to elute. At the same time, in the process of protein purification, the use of biotin system will greatly reduce cross-reaction and greatly improve the efficiency of biotinylation. Alfa Chemistry researchers are familiar with the characteristics of the biotin-avidin/streptavidin system, and can perform customized protein biotinylation according to customer needs, so as to use high-efficiency affinity for protein labeling and purification.

The Services

Alfa Chemistry can provide customized protein purification services according to the needs of customers, using the efficient affinity of the biotin-avidin/streptavidin system to achieve efficient protein purification. The related services we can provide include but are not limited to:

• Biotin-avidin/streptavidin system affinity calculation
• Design of efficient protein purification solutions
• Protein biotinylation and purification
• Professional handling of samples

Biotinylation for protein purification

With the rapid development of biotechnology, proteomics requires a simpler and more efficient way to purify proteins. The biotin-avidin/streptavidin system has very high affinity and is therefore used for efficient purification of proteins and complexes. Biotinylation can occur by the cell's endogenous protein-biotin ligase or by co-expression of an exogenous biotin ligase. The use of biotin labeling systems shows great application potential in the field of protein purification. An increasing number of affinity purification methods are being developed for proteomics research. Specific proteins can be biotinylated by efficient design, using high-efficiency biotin-avidin technology, which can be used for the purification and characterization of proteins and complexes.

What can we provide?

Alfa Chemistry focuses on efficient biotinylation detection services, and can provide customized services according to customer needs to meet customer needs. We have professional researchers and an efficient quality control platform. In addition to professional data analysis, we can also process experimental samples, including analysis of extracts and conjugates, western blot analysis, and chromatin pull-down experiments，to meet customers' requirements for protein biotinylation labeling and purification

Supports efficient system expansion and updates

• Enables efficient protein biotinylation purification in less time
• We can save samples, reagent consumption
• Support more reasonable strategies to achieve step-by-step system upgrades

Process for biotinylated protein purification

It is essential for the purification of biotinylated proteins, and its purification process can be divided into sample capture, simple purification and fine purification. Host contamination, sample solubility, protein activity and integrity need to be considered.

The researchers of Alfa Chemistry can use highly efficient biotinylation systems for efficient protein purification. If you are interested in our services, please contact us immediately.

References:

1. Ernie. B.; et al. Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice. PNAS.100 (13) : 7480-7485.

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

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