Orthogonal protein purification facilitated by a small bispecific affinity tag.

ABSTRACT: Due to the high costs associated with purification of recombinant proteins the protocols need to be rationalized. For high-throughput efforts there is a demand for general methods that do not require target protein specific optimization . To achieve this, purification tags that genetically can be fused to the gene of interest are commonly used. The most widely used affinity handle is the hexa-histidine tag, which is suitable for purification under both native and denaturing conditions. The metabolic burden for producing the tag is low, but it does not provide as high specificity as competing affinity chromatography based strategies. Here, a bispecific purification tag with two different binding sites on a 46 amino acid, small protein domain has been developed. The albumin-binding domain is

SUBMITTER: Nilvebrant J 

PROVIDER: S-EPMC3462565 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature