The Strep-tag II is an eight-amino-acid peptide (WRHPQFGG), which, after fusion with the recombinant protein of interest, offers a practically useful solution to purify target protein. The Strep-tag II has negligible effect on the recombinant protein due to its chemically balanced amino acid composition. Generally, it does not interfere with folding or bioactivity and does not induce protein aggregation. Thus, there is no need for removing the tag.
PurKine™ Strep II-Tag Streptactin Resin 4FF effectively purifies high levels of Strep II-tagged proteins expressed in any express system such as, E. coli, insect, and mammalian cells at a variety of scales. The Resin consists of 90μm beads of cross-linked 4% agarose, to which Strep-Tactin has been coupled. Strep-Tactin is a streptavidin derivative which is one of the most stable proteins known. Tests confirm that performance equals or exceeds popular Strep-Tactin resins from other suppliers, and no decrease in performance occurs after at least five repeated uses. In addition, its high flow properties make it excellent for scaling-up.
PurKine™ Strep II-Tag Strep-Tactin Resin 4FF system is based on innovative high-capacity matrix for convenient single-step purifications of Strep II-Tag protein under physiological conditions, which means no influence of protein folding or function. The binding affinity of Strep II-Tag to Strep-Tactin is nearly 100 times higher than to streptavidin. Furthermore, the neutral pI of Strep-Tactin minimizes non-specific protein or nucleic acid binding. The product is safe and easy to use.