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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag
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Orthogonal Protein Purification Facilitated by a Small Bispecific Affinity Tag

Published on: January 16, 2012

Choline-binding domain as a novel affinity tag for purification of fusion proteins produced in Pichia pastoris

J Caubín1, H Martín, A Roa

  • 1Departamento de Microbiología II, Facultad de Farmacia, Universidad Complutense, Plaza de Ramón y Cajal s/n. 28040, Madrid, Spain.

Biotechnology and Bioengineering
|May 23, 2001
PubMed

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Tagging and Fusion Proteins01:24

Tagging and Fusion Proteins

Proteins are involved in several cellular processes and biochemical reactions. Analyzing a specific protein of interest requires it to be isolated from the other proteins in the cell. This is achieved by overexpressing the specific gene in a suitable host to produce large quantities of the target protein. A tag or label is recombined with the gene to produce a fusion protein containing the target protein and the tag. The tags on these fusion proteins can then be used for easy detection and...