Each trainee spends 2-3 summer months or longer (up to six months) in an industrial research laboratory. This typically occurs in the summer following the two years of NIH support (e.g., after the third year of thesis work). Students and their mentors are provided with an industrial contact list in advance (typically at the time of acceptance into the Training Program) to initiate contact with an appropriate industrial laboratory. This group of companies, from the Training Program Industrial Partners Program, represents a broad range of industries and research/development areas in biomolecular science and engineering, from pharmaceutical companies to pharmaceutical and chemical outsourcing firms to small biotechnology start-ups including
- Albany Molecular Research (Albany, NY),
- Pfizer (Groton, CT),
- Merck & Co (Whitehouse Station, NJ),
- Agrivida Inc. (Medford, MA),
- Potentia Pharmaceuticals (Louisville, KY),
- UCB Celltech (Slough UK),
- Ecovative Design (Green Island, NY),
- J&J Centocor (Spring House, PA) and
- Medtronic (Minneapolis, MN).
In addition to these companies, students are free to choose from other companies. The Executive Committee will entertain additional companies identified by trainees and training faculty, and this will result in an expansion in the number of companies affiliated with the Training Program.
Katherine Mezic: Katherine’s internship with GE Global Research, Niskayuna, NY involved independently developing an expression system for a thermophilic sulfatase from Thermotoga maritima, using a unique promoter from a colicinogenic plasmid (June 5, 2017-August 25, 2017.
Topics/techniques used: molecular biology, cell growth, gel electrophoresis, and chromatography, including IMAC and SEC with the AKTA Avant preparative chromatography system.
Megan Mason: Mason’s internship with UCB Celltech, Slough, UK involved studying the effect of single amino acid substitutions in antibodies (June 1, 2008-November 30, 2008; Dr. Bernie Sweeney, Group Manager, Antibody Biology) . For example, changing a glycine to an alanine in the heavy chain variable region of one of our therapeutic candidates results in a four-fold increase in expression level in CHO cells, but has no effect on the antibody affinity for its target.
Utilizing site-directed mutagenesis, the aim was to create a panel of antibodies containing every amino acid at the position of interest, and measure various factors, such as mRNA levels and protein stability, with the intent of determining what influences or regulates the level of antibody expression. With this fundamental information, antibodies may be able to be engineered that can be produced in more concentrated quantities, thus reducing cost and timelines for production of potential therapeutics.
Topics/techniques used: molecular cloning, mammalian cell culture, cell line engineering, ELISA, site-directed mutagenesis, vector design, transient transfection, stable cell line generation, DNA/RNA purification.