Related Experiment Video
Updated: Jul 12, 2026

Engineering Cell-permeable Protein
Published on: December 28, 2009
Partial purification and characterization of a recombinase from human cells
Abstract:
We describe the partial purification and characterization of a human recombinase activity from RPMI 1788 B lymphoblasts. Stoichiometric amounts of recombinase carry out a strand transfer reaction between linear duplex DNA and homologous circular single-strand DNA. The product of strand transfer by the recombinase is a joint molecule composed of a single-strand circle joined to one end of the linear duplex molecule by a region of DNA heteroduplex at least 150 bp long. Formation of DNA heteroduplexes is accompanied by strand displacement. Strand invasion initiates at the ends of the linear duplex. Finally, strand displacement by human recombinase exhibits polarity and proceeds in a 3' to 5' direction. This is the first demonstration of a strand transfer activity from a high eukaryote. We discuss similarities between our recombinase and the RecA and rec1 recombination proteins from E. coli and Ustilago maydis, respectively.
More Related Videos
11:36Rapid and Efficient Generation of Recombinant Human Pluripotent Stem Cells by Recombinase-mediated Cassette Exchange in the AAVS1 Locus
Published on: November 20, 2016
06:41Transgene Expression in Cultured Cells Using Unpurified Recombinant Adeno-Associated Viral Vectors
Published on: October 20, 2023
Related Concept Videos
Recombinant DNA
Conservative Site-specific Recombination and Phase Variation
The recognition sites for Cre recombinase called LoxP...
DNA Isolation