Detecting and targeting specific MHC-peptide complexes is of material interest for understanding many disease conditions better and for developing novel therapeutic interventions. It has been very challenging to develop antibodies that bind selectively to an MHC-peptide combination over a more general MHC allotype.
Ankyrons provide a clear and powerful solution to this problem. Selected directly in vitro from our Teralibrary we can already offer a growing range of more than 16 of the most popular MHC-peptide combinations in cancer and infectious diseases in the listing below. Using guided selection we are able to select sequence specific Ankyrons quickly. ProImmune is also the world leader by publications from a commercial source in MHC-peptide multimer technology. So building MHC-peptide antigens for new Ankron discovery is already our core business.
Contact us with your Custom Ankyron™ requirements or Request a Quote for us to make a quantum leap in your MHC-peptide targeting project.
Data for MHC-peptide specific Ankyron staining
Figure. Staining of cell line constitutively expressing an infectious disease-specific MHC-peptide complex combination with Ankyrons selected to specifically bind the same (MHC-peptide specificity and study background are still subject to publication). Unstained data show background fluorescence. The cell line was stained with MHC-peptide specific Ankyrons as well as Ankyrons specific to an irrelevant peptide in the context of the same MHC allele. Staining was carried out in each case with and without additional stimulation with IFNγ. Stimulation with IFNγ strongly upregulates MHC-peptide presentation. In stimulated cells the staining of the cell line with the specific Ankyron separates clearly from that of the non specific Ankyron staining. Data provided by Prof. Antonio Bertoletti’s group at Duke NUS, Singapore.
Flow cytometric analysis of liver cancer cell lines HepG2 and HepG2.2.15 cells (obtained from the transduction of HBV genome into HepG2). HepG2.2.15 cells were stimulated with IFNgamma to induce higher expression of MHC class I molecules, then labeled with 5 µg/50 µl Ankryron ANK03496_1_APS40107 and 2.5 µl/50 µl anti-V5 PE antibody, (green). Negative controls: HepG2 with IFNgamma (blue), HepG2 without IFNgamma (pale blue), HepG2.2.15 without IFNgamma(pale green), unstained HepG2.2.15 with IFNgamma (dark grey), unstained HepG2.2.15 without IFNgamma (pale grey). Data kindly provided by Antonio Bertoletti, Duke-NUS Medical School.
Flow cytometric analysis of liver cancer cell lines HepG2 and HepG2.2.15 cells (obtained from the transduction of HBV genome into HepG2). HepG2.2.15 cells were stimulated with IFN gamma to induce higher expression of MHC class I molecules, then labeled with 5 µg/50 µl Ankryron ANK03341_1_A040418 and 2.5 µl/50 µl anti-V5 PE antibody, (green). Negative controls: HepG2 with IFNgamma (blue), HepG2 without IFNgamma (pale blue), HepG2.2.15 without IFNgamma (pale green), unstained HepG2.2.15 with IFNgamma (dark grey), unstained HepG2.2.15 without IFNgamma (pale grey). Data kindly provided by Antonio Bertoletti, Duke-NUS Medical School.
Flow cytometric analysis of liver cancer cell lines HepG2 and HepG2.2.15 cells (obtained from the transduction of HBV genome into HepG2). HepG2.2.15 cells were stimulated with IFNgamma to induce higher expression of MHC class I molecules, then labeled with 5 µg/50 µl Ankryron ANK03341_2_AO40422 and 2.5 µl/50 µl anti-V5 PE antibody, (green). Negative controls: HepG2 with IFNgamma (blue), HepG2 without IFNgamma (pale blue), HepG2.2.15 without IFNgamma (pale green), unstained HepG2.2.15 with IFNgamma (dark grey), unstained HepG2.2.15 without IFNgamma (pale grey). Data kindly provided by Antonio Bertoletti, Duke-NUS Medical School.
