Introduction
Protein purification
1. Good activity: 8 amino acids are electrically neutral short labels, which do not affect the protein structure and activity.
2. Specificity: Combines with Strep-Tactin specifically, with an affinity 100 times that of Streptavidin
3. High purity: Proteins with >95% purity can be purified using physiological buffers
4. Super time-saving: Re-use purification column, quickly complete protein purification in 10 minutes
5. Wide application: can be labeled at the N or C terminus, suitable for mammalian cells, baculovirus, E. coli, yeast and other expression systems
Features / strengths
Strep-tag II is composed of 8 amino acids (WSHPQFEK) and can be used as a protein tag. Because the molecule is small and electrically neutral, it will not affect the protein's configuration, secretion characteristics, and active functions. Strep-tag II and its variant protein Strep-Tactin can form highly specific binding with reversible reactions.
Strep-Tactin protein is a variant protein of Streptavidin. The binding force between Strep-tag II and Strep-Tactin is 100 times stronger than that between Strep-Tag-II and Streptavidin. The single-step rapid purification method can purify the highest purity active protein, with purity up to >99%. Purification can be carried out under general physiological buffers, and can also be applied to a variety of different conditions, such as: detergents, chelators, salt, redox, etc.
This technology can be used for purification of genetically recombinant protein production (Strep-tag), protein interaction analysis (One-STrEP), immune cell markers (streptamers), etc.
Specification in detail
Product Information
Please email us for detailed specifications.
