Enzymatic Biotinylation of Spodoptera Frugiperda Cells

Biotin (vitamin H) can usually be immobilized on the surface of avidin or streptavidin for the binding of various ligands, so more and more reagents have been developed to facilitate biotinylation. All cells contain proteins, and biotin can be covalently linked for efficient biotinylation. E. coli contains biotin carboxyl carrier protein (BCCP). In an ATP-dependent reaction, biotin holoenzyme synthase (BirA) is coupled to the e-amino group of Lys122 in BCCP via an amide bond (4, 5). Site-specific enzymatic biotinylation of recombinant proteins can be employed to overcome the limitations of their use. The recombinant protein can be labeled with biotin at the predetermined site, which can be carried out by means of biological enzymes. At present, it has been reported that E. coli biotin holoenzyme synthase (BirA) can be used to label recombinant proteins in Spodoptera frugiperda (Sf9) cells. Alfa Chemistry serves universities and biological research institutions around the world and is committed to providing high-quality biotinylation services.

Biotin and protein binding can be used to immobilize on avidin or streptavidin surfaces for efficient ligand binding. Compared to chemically biotinylation, enzymatic biotinylation is highly specific and predetermined. Efficient protein biotinylation, does not affect biological activity, and can be labeled with biotin at predetermined sites. The researchers of Alfa Chemistry focus on providing professional services for enzymatic biotinylation of Spodoptera frugiperda cells including but not limited to:

• Enzymatic biotinylation of Spodoptera frugiperda cells
• High efficiency test of biotinylated Spodoptera frugiperda cells
• Affinity calculation

The advantages of enzymatic biotinylation

• In vivo, no subsequent processing required
• Efficient repeatability
• Avoid the interference of heterogeneity
• Eliminate repeatability or heterogeneity

Alfa Chemistry insists on innovation and meets the needs of customers with efficient biotinylation services. If you are interested in our services, please contact us immediately.

Reference:

1. Siobain. D; et al. Site-specific, enzymatic biotinylation of recombinant proteins in spodoptera frugiperda cells using biotin acceptor peptides. ANALYTICAL. BIOCHEMISTRY. 1998, 262: 122-128.

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