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Related Experiment Videos

Cre-loxP biochemistry.

Kaushik Ghosh1, Gregory D Van Duyne

  • 1Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

Methods (San Diego, Calif.)
|November 15, 2002
PubMed
Summary
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This review details a protocol for purifying Cre recombinase enzyme and its mutants for in vitro and in vivo DNA manipulation. Assays are provided to test recombination activity, aiding researchers using Cre-loxP systems.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Cre recombinase is essential for complex DNA manipulations in both in vitro and in vivo settings.
  • High-purity Cre preparations and mutants are crucial for control experiments and altered activity studies.
  • In vivo applications often necessitate in vitro characterization and transient expression via enzyme transfection.

Purpose of the Study:

  • To provide a detailed protocol for the purification of native Cre recombinase.
  • To describe straightforward assays for testing Cre recombination activity in vitro.
  • To present methods for trapping Cre-loxP recombination intermediates for biophysical analysis.

Main Methods:

  • Detailed protocol for native Cre recombinase purification.

Related Experiment Videos

  • Development of simple in vitro assays to evaluate recombination activity.
  • Experimental design strategies for capturing Cre-loxP recombination intermediates.

    • Main Results:

    • A reliable method for obtaining purified Cre recombinase enzyme.
    • Established assays for functional characterization of Cre recombinase activity.
    • Framework for biophysical studies of site-specific recombination intermediates.

    Conclusions:

    • The described purification and assay methods are valuable for researchers needing purified Cre recombinase.
    • The protocol is broadly applicable to other site-specific recombination systems.
    • This work facilitates advanced studies of Cre-mediated DNA recombination.