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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 380, Issue 12 (Dec 1999)

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Comparison of the Tamoxifen Regulated Chimeric Cre Recombinases MerCreMer and CreMer

Chrysi Verrou / Yong Zhang / Christa Zürn / Wolfgang W.A. Schamel / Michael Reth
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.1999.184

Abstract

The site-directed recombinase Cre can be employed to delete or assemble genes in the genome of living cells. We have constructed expression vectors for chimeric Cre recombinases carrying a mutated hormone binding domain either at the C-terminus only (CreMer) or at both the N and C-termini (MerCreMer). The chimeric Cre proteins can be activated by culturing transfected cells with 4-hydroxytamoxifen. In transfected embryonic stem (ES) cells, we compared the extent of recombination of a floxed gene with the expression levels of the chimeric Cre proteins. Our data demonstrate that the bulky MerCreMer protein is not less active than the CreMer protein. Thus, the tighter control and low background activity of the MerCreMer enzyme is not due to a generally low recombinase efficiency.

About the article

Published Online: 2005-06-01

Published in Print: 1999-12-20


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.1999.184.

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