Format

Send to

Choose Destination
Sci Rep. 2015 Aug 14;5:12896. doi: 10.1038/srep12896.

Cell-free expression of functional receptor tyrosine kinases.

Author information

1
University of California Davis School of Medicine, Radiation Oncology, Sacramento, California, USA.
2
University of California Davis School of Medicine, Internal Medicine, Division of Hematology Oncology, Sacramento, California, USA.
3
University of California Davis School of Medicine, Biochemistry and Molecular Medicine, Sacramento, California, USA.
4
1] Lawrence Berkeley National Laboratory, Berkeley, California, USA [2] University of California Santa Cruz, Chemistry and Biochemistry, Santa Cruz, California, USA.
5
1] Lawrence Berkeley National Laboratory, Berkeley, California, USA [2] Scripps Research Institute, La Jolla, California, USA.
6
1] University of California Davis School of Medicine, Biochemistry and Molecular Medicine, Sacramento, California, USA [2] University of California Davis Comprehensive Cancer Center, Sacramento, CA California, USA.
7
1] University of California Davis School of Medicine, Internal Medicine, Division of Hematology Oncology, Sacramento, California, USA [2] University of California Davis Comprehensive Cancer Center, Sacramento, CA California, USA.
8
1] University of California Davis School of Medicine, Radiation Oncology, Sacramento, California, USA [2] University of California Davis Comprehensive Cancer Center, Sacramento, CA California, USA [3] Lawrence Livermore National Laboratory, Livermore, California, USA.

Abstract

Receptor tyrosine kinases (RTKs) play critical roles in physiological and pathological processes, and are important anticancer drug targets. In vitro mechanistic and drug discovery studies of full-length RTKs require protein that is both fully functional and free from contaminating proteins. Here we describe a rapid cell-free and detergent-free co-translation method for producing full-length and functional ERBB2 and EGFR receptor tyrosine kinases supported by water-soluble apolipoprotein A-I based nanolipoprotein particles.

PMID:
26274523
PMCID:
PMC4929682
DOI:
10.1038/srep12896
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center