Research
Print page Print page
Switch language
The Capital Region of Denmark - a part of Copenhagen University Hospital
Published

Expression, purification and characterization of the cancer-germline antigen GAGE12I: A candidate for cancer immunotherapy

Research output: Contribution to journalJournal articleResearchpeer-review

  1. Purification and characterization of recombinant full-length and protease domain of murine MMP-9 expressed in Drosophila S2 cells

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Purification and characterization of osteopontin from human milk

    Research output: Contribution to journalJournal articleResearch

  1. Adoptive cancer immunotherapy using DNA-demethylated T helper cells as antigen-presenting cells

    Research output: Contribution to journalJournal articleResearchpeer-review

  2. Biweekly cetuximab and irinotecan as second-line therapy in patients with gastro-esophageal cancer previously treated with platinum

    Research output: Contribution to journalJournal articleResearchpeer-review

  3. Cancer-germline antigen vaccines and epigenetic enhancers: future strategies for cancer treatment

    Research output: Contribution to journalReviewResearchpeer-review

View graph of relations
GAGE cancer-germline antigens are frequently expressed in a broad range of different cancers, while their expression in normal tissues is limited to the germ cells of the immune privileged organs, testis and ovary. GAGE proteins are immunogenic in humans, which make them promising targets for immunotherapy and candidates for cancer vaccines. Recombinant proteins may be superior to peptides as immunogens, since they have the potential to prime both CD4(+) and CD8(+) T cells and are not dependent on patient HLA-type. We have developed a method for production of highly pure recombinant GAGE12I-His by intracellular expression in yeast (Pichia pastoris) and nickel affinity, ion exchange and gel filtration purification. The identity of the purified protein was confirmed by mass spectrometry. This strategy yielded a total of 48 mg of highly pure (>98%) GAGE12I from 8 L of culture (6 mg/l). Interestingly, gel filtration and formaldehyde cross-linking indicated that GAGE12I forms tetramers. The purified recombinant GAGE12I represents a candidate molecule for vaccination of cancer patients and will form the basis for further structural analysis of GAGE proteins. (C) 2010 Elsevier Inc. All rights reserved
Original languageEnglish
JournalProtein Expression and Purification
Volume73
Issue number2
Pages (from-to)217-222
Number of pages6
ISSN1046-5928
DOIs
Publication statusPublished - 2010

ID: 32288044