KanPro Corporation is a contract research organization (CRO) headquartered in the Bioscience & Technology Business Center at the University of Kansas. The company is based on successful operations of the KU Enzyme Lab, KU Biochemical Research Services Lab and the KU COBRE-PSF Protein Production Group (PPG). The company is specializing in recombinant protein expression and purification from bacterial, yeast, insect, mammalian cells to cell-free systems. KanPro Corporation seeks partnership with academic and industrial researchers to develop contract research projects, produce challenging proteins failed elsewhere, and provides high margin services to our clients. Protein production is supplemented by manufacturing and testing biochemical reagents, kits, and equipment. Professional advice and consultation services are also provided.
The founder and director, Dr. Philip Gao, has been working full time in research areas of molecular biology, protein production and biophysical characterization of proteins for the last 18 years. He received his Ph.D. in Biochemistry at the University of Kansas (1996) studying the structure and function of the chloroplast ATP synthase. As an NIH postdoctoral fellow he worked on the structure and function of the E. coli lactose permease with Dr. Ronald Kaback in the Department of Physiology, Immunology and Microbiology and the Howard Hughes Medical Institute at UCLA. From 2001 to 2007, Dr. Gao established and managed a new membrane protein production facility at the National High Magnetic Field Laboratory at Florida State University. Since July 2008, he has directed the COBRE-PSF Protein Production Group Core Laboratory at the University of Kansas. Both at FSU and at KU, Dr. Gao's laboratory provided proteins used for team-based NIH projects focused on the structure and function of proteins. Dr. Gao has an excellent background in molecular biology, protein purification, cell culture, and fermentation. He also has extensive experience in the preparation of challenging proteins for enzymatic and NMR studies, X-ray crystallography, and mass spectrometry. He has been working in collaborative research with groups from different disciplines and backgrounds and has a record of successful and productive collaborative research projects.
During Phase II of COBRE-PSF, the PPG Core Lab provided cloning, protein production and other services to a total of 60 individuals from 37 different research groups in 31 different departments and institutions. Hands-on training in a range of techniques was provided to a total of 86 individuals (including students, postdocs and faculty PIs). A total of 51 guest workers used facilities and/or equipment in the PPG to conduct their own experiments. The PPG also completed 42 separate projects requested by 12 COBRE-supported investigators, and 55 additional projects requested by non-COBRE investigators at 22 different research and/or academic institutions. The success rate of project is about 95%.
Some highights of the PPG's recent productivity include:
The cloning of 69 genes from Chlamydia trachomatis into three different E. coli expression vectors using genomic DNA. A total of 207 clones were produced within less than seven weeks (for P. Scott Hefty, KU).
The ARMET promoter gene from human genomic DNA was cloned into a mammalian luciferase reporting plasmid. Stable transfection and clonal selection in HeLa cells were performed for high throughput screening (for HTS lab, KU).
Several batches of human paladin were produced from insect cells for crystallization in the COBRE PSL Core Lab (for Moriah Beck, WSU)
Three uniformly 15N- and 13C -labeled proteins (Hur, Bclx and Msi) were produced for drug binding screening using the COBRE BNMR lab (for Liang Xu, KU).
A new form of nicotine oxidase was genetically engineered and evolved from the existing 6-hydroxynicotine oxidase for manufacture of a nicotine biosensor (for Mark Richter, KU).
Three postdoctoral researchers from the KU Department of Physics were trained to label and purify proteins for single-molecule fluorescence studies (for Matthew Antonik, KU).
In our first Fragment Based Drug Design campaign, we screened a library of ca. 250 compounds by Surface Plasmon Resonace to study their binding to HDAC protein (for Scott Lovell, PSL, KU).
Several hundred milligrams of Ricin Vaccine protein (RiVax™) were produced from 10 liters of E. coli fermentation culture (for Russ Middaugh, KU).
The heterotrimeric yeast chromatin remodeler complex “RSC” was expressed and purified from yeast for stopped-flow fluorescence-based assays (for Christopher Fischer, KU).
Commercially available adenosine deaminase (ADA) from calf intestine was used to prepare the active, endotoxin free, pegylated form of the enzyme (for Margaret Bynoe, Cornell University).
Expression vector construction, expression optimization, protein purification up to 2 liters.
Any vector, any insert. Price may vary depending on the project.
KanPro Research Inc. has not received any reviews.
KanPro Research Inc. has not received any endorsements.