Download e-book for iPad: Antigen Processing and Presentation Protocols (Methods in by Solheim J.C.

By Solheim J.C.

ISBN-10: 0896037452

ISBN-13: 9780896037458

ISBN-10: 1592590624

ISBN-13: 9781592590629

Well-recognized and cutting edge experimentalists aspect their state-of-the-art tools for learning the antigen processing and presentation. Drawing on services from biochemistry, cellphone biology, and immunology, they describe step by step tools designed to query how MHC-binding peptides are generated, to check how peptides are dropped at MHC molecules, to research MHC peptide-binding styles, and to assay the T-cell reaction to the MHC/peptide advanced. Emphasis is given these technical steps severe for experimental luck which are usually passed over from tools released within the fundamental literature. Eminently obtainable and state of the art, Antigen Processing and Presentation Protocols presents either new and skilled investigators with hugely sensible instruments that would expand the questions that may be requested, and successfully be responded, pertaining to antigen processing/presentation.

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Additional resources for Antigen Processing and Presentation Protocols (Methods in Molecular Biology Vol 156)

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Peptides and MHC-I in Ag Presentation 39 4. 1% Triton X-100 solution in BSS–BSA. 5. Microcentrifuge. 6. Spectrofluorometer. 5. 1. Time-course of Presentation 1. 1. 2. Use of Inhibitors 1. Stock solutions of inhibitors as outlined in Table 2. 3. 1. Ruling Out Peptide Contamination Any study of the presentation of exogenous Ags on MHC-I must rule out peptide contamination in the Ag preparation. Despite attempts to remove peptide from Ag preparations by gel filtration, centrifugation, or other methods, it is possible that peptide contamination that is undetectable biochemically may still be present.

Cell Biol. 109, 675–683. 10. , Nguyen, T. , and Wang, C. C. (1996) Purification and characterization of proteasomes from Trypanosoma brucei. Mol. Biochem. Parasitol. 78, 33–46. 11. , and Morisawa, M. (1993) Purification of proteasomes from salmonid fish sperm and their localization along sperm flagella. J. Cell Sci. 104, 907–915. 12. , Naude, R. , and Oelofsen, W. (1997) Purification and characterization of proteasome from ostrich liver. Int. J. Biochem. Cell Biol. 29, 611–622. 13. Koohmaraie, M.

2. After 1 h at 37°C, mixing every 10–15 min, add medium to reach a final cell density of 106 cells/mL. Incubate at 37°C for another 30 min. 3. Wash the cells with warm PBS buffer, and resuspend them in Met-free medium, containing the desired concentration of the inhibitor (see Note 2), at a density of 5 x 106 cells/mL. Incubate 20 min at 37°C (see Note 3). 4. Wash the cells, and resuspend them again in Met-free medium, containing the appropriate amount of inhibitor (final cell density of 107 cells/mL).

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Antigen Processing and Presentation Protocols (Methods in Molecular Biology Vol 156) by Solheim J.C.

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