Protein activity and functional studies rely largely on the availability of purified target proteins. Majority of protein studies are carried out on tagged recombinant proteins expressed in various host organisms. Over 50% of these tagged recombinant proteins are expressed as fusions with poly-histidine purification tags. The small size and the mild conditions utilized during His-tagged protein purification as well as the associated low costs makes this type of fusion the most popular (and in many cases, the first tag of choice). BioVision’s Ni-IDA Spin Columns are ideal for small-scale purification of these poly-histidine-tagged proteins rapidly. Each of these columns is filled with 100 µL of high performance Hi-Bind™ Ni QR Agarose Beads (Cat. #6562), enabling efficient capture and purification of up to 2.8 mg of poly-histidine tagged proteins per column. The small volume of beads inside the columns is optimal for loading various amounts of sample. At normal expression levels, it permits efficient displacement of non-tagged protein impurities by the more strongly binding poly-histidine tagged targets and improves the purity of the final product. The yield and purity of purification are protein specific and depends on various factors like the expression level, structure, solubility etc. The beads packed in each column deliver as much as 25% higher capacity than Ni-NTA adsorbents while dramatically decreasing purification times due to the ability to perform centrifugation.