Display Settings:

Format

Send to:

Choose Destination
    Curr Opin Biotechnol. 2006 Aug;17(4):353-8. Epub 2006 Jun 15.

    Enhancement of soluble protein expression through the use of fusion tags.

    Source

    Protein Expression Laboratory, Research Technology Program, SAIC-Frederick, Inc, NCI-Frederick, Frederick, MD 21702, USA.

    Abstract

    The soluble expression of heterologous proteins in Escherichia coli remains a serious bottleneck in protein production. Although alteration of expression conditions can sometimes solve the problem, the best available tools to date have been fusion tags that enhance the solubility of expressed proteins. However, a systematic analysis of the utility of these solubility fusions has been difficult, and it appears that many proteins react differently to the presence of different solubility tags. The advent of high-throughput structural genomics programs and advances in cloning and expression technology afford us a new way to compare the effectiveness of solubility tags. This data should allow us to better predict the effectiveness of tags currently in use, and might also provide the information needed to identify new fusion tags.

    PMID:
    16781139
    [PubMed - indexed for MEDLINE]

      Supplemental Content

      Icon for Elsevier Science

      Save items

      loading

      Recent activity

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      Write to the Help Desk