The Recombinant Protein Expression and Purification (RPrEP) Core was established in 2009 to provide a cost-effective resource to the MGH and DF/ HCC community for expression and purification of recombinant proteins necessary for pre-clinical studies as well as for basic mechanistic studies by immunologists and cancer biologists.
Recombinant Proteins can be manufactured by this Core for a variety of applications according to MGH-DF/ HCC investigator needs. In addition to large-scale production of recombinant proteins in yeast Pichia pastoris, a cost effective small-scale production service will be provided using E.coli or yeast Pichia pastoris expression system (e.g. for small animal studies, use as immunogens, ELISAs, or high throughput microarray platforms).
Technical Director: Dr. Zhirui Wang
Location of Core:
The facility is located at CNY 149-6117C 13th St. Charlestown, MA 02129.
Recombinant protein expression and purification in yeast Pichia pastoris
Large-scale purification of recombinant protein
Large-scale production of immunotoxins for cell depletion studies
Large-scale production of recombinant cytokines (e.g. IL-2, IL-3) not available or prohibitively expensive from commercial sources
Yeast display for protein-protein/antibody interaction study
BioFlo 510 Fermentor training and usage
*Access to the Core will be available to all members of the research community. Priority will be given to MGH and DF/HCC users.
Yeast display vector: pYD1, pYD5, and yeast display strain: yeast Saccharomyces cerevisiae EBY100 are available in this core (redistribution of pYD1, pYD5, and EBY100 permitted by inventors) for worldwide research community.
Potent IL-2 fusion toxins (murine, human and porcine) are available in this core for depleting IL-2 receptor positive cells including CD25+ Treg in vivo.
 Hermanrud, C.E., Lucas, C.L., Sykes, M., Huang, C.A., Wang, Z. (2011) Expression and purification of soluble murine CD40L monomers and polymers in yeast Pichia pastoris. Protein Expr Purif. 76:115–120.
 Wang, Z., Duran-Struuck, R., Crepeau, R., Matar, A., Hanekamp, I., Srinivasan, S., Neville, D.M., Sachs D.H., Huang CA. (2011) Development of a Diphtheria Toxin Based Antiporcine CD3 Recombinant Immunotoxin. Bioconjug Chem. 22:2014-2020.
 Hermanrud, C. E., Pathiraja, V., Matar, A., Duran-Struuck, R., Crepeau, R.L., Srinivasan, S., Sachs, D. H., Huang, C. A., Wang, Z. (2012) Expression and purification of non-N-glycosylated porcine interleukin 3 in yeast Pichia pastoris. Protein Expr Purif. 82:70-74.
 Peraino, J., Zhang, H., Hermanrud, C. E., Li, G., Sachs, D. H., M.D.; Christene A Huang, C. E., Wang, Z. (2012) Expression and purification of soluble porcine CTLA‑4 in yeast Pichia pastoris. Protein Expr Purif. 82:270-278.
 Peraino, J. S., Hermanrud, C. E., Springett, L., Zhang, H., Li, G., Srinivasan, S., Gusha, A., Sachs, D. H., Huang, C. A., Wang, Z. (2012) Expression and characterization of recombinant soluble porcine CD3 ectodomain molecules: Mapping the epitope of an anti-porcine CD3 monoclonal antibody 898H2-6-15. Cell Immunol. 276:162-167.
 Peraino, J. S., Schenk, M., Zhang, H., Li, G., Hermanrud, C. E., Neville Jr., D. M., Sachs, D. H., Huang, C. A., Duran-Struuck, R., Wang, Z. (2013) A Truncated Diphtheria Toxin Based Recombinant Porcine CTLA-4 Fusion Toxin. J Immunol Methods. 391:103-11.
 Peraino, J. S., Zhang, H., Li, G., Huang, C. A., Wang, Z. (2013) Molecular Basis of Cross-Species Reactivities of human versus Porcine CTLA-4. Hum Immunol.72:842-848.
 Peraino, J. S., Schenk, M., Li, G., Zhang, H., Farkash, E. A., Sachs, D. H., Huang, C. A., Duran-Struuck, R., Wang, Z. (2013) Development of a diphtheria toxin-based recombinant porcine IL-2 fusion toxin for depleting porcine CD25+ cells. J Immunol Methods. doi:pii: S0022-1759(13)00246-9. 10.1016/j.jim.2013.09.006.
To access the core, please contact Dr. Zhirui Wang at (617) 643-1957 or by email at
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