High quality protein microarray using in situ protein purification.

ABSTRACT:

Background

In the postgenomic era, high throughput protein expression and protein microarray technologies have progressed markedly permitting screening of therapeutic reagents and discovery of novel protein functions. Hexa-histidine is one of the most commonly used fusion tags for protein expression due to its small size and convenient purification via immobilized metal ion affinity chromatography (IMAC). This purification process has been adapted to the protein microarray format, but the quality of in situ His-tagged protein purification on slides has not been systematically evaluated. We established methods to determine the level of purification of such proteins on metal chelate-modified slide surfaces. Optimized in situ purification of His-tagged recombinant proteins has the pot

SUBMITTER: Kwon K 

PROVIDER: S-EPMC2746808 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature