What degree of purity can be expected?
Over 95 %. It must be mentioned that potential impurities may result from non-specific interactions of the recombinant protein itself with other proteins leading to lower purity grades. More purity related FAQs you find in chapter “Contaminations”. • How can the protein be eluted? Elution is performed by the addition of 2.5 mM desthiobiotin, a derivative of biotin. It is a stable, reversibly binding (columns can be regenerated) low molecular weight substance which does not interfere with the protein or general protein assays. • Is the protein’s bioactivity preserved? Yes. Bioactivity is preserved due to the mild washing and elution conditions by the use of physiological buffers. • When the protein elutes from the column, is it complexed with desthiobiotin? No. Desthiobiotin can be removed via gel filtration or dialysis • Is the Strep-tag® system stable in the presence of imidazole? Yes, the Strep-tag system tolerates up to 250 mM imidazole in the protein extract. Therefore, elution fra
