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Purification of Amyloidogenic Transthyretin Protein Using Nuvia™ Q Anion Exchange Resin 

Abstract

Purification of recombinant amyloidogenic proteins can sometimes prove challenging due in part to their aggregation-prone character. Here, we demonstrate how we were able to use Bio-Rad's Nuvia Q Resin to successfully purify one such protein, transthyretin (TTR). 

TTR is involved in both senile and familial forms of amyloidosis. Over 100 amyloidogenic mutations have been reported and they represent the most common cause of hereditary amyloidosis. Purification of recombinant TTR can be problematic due to its aggregation properties, which prevent the use of acidic buffers or denaturant agents. Purification of recombinant TTR is typically performed by salting out TTR using an ammonium sulfate precipitation procedure. This procedure requires an extra purification step to isolate TTR from contaminating DNA and coprecipitating proteins. Since TTR has an isoelectric point of 5.7, we used high-capacity Nuvia Q Anion Exchange Resin to effectively purify it under neutral buffer conditions. 

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