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Antigen Processing and Presentation Protocols (Methods in by Solheim J.C.

By Solheim J.C.

Well-recognized and leading edge experimentalists aspect their state-of-the-art equipment for learning the antigen processing and presentation. Drawing on services from biochemistry, mobilephone biology, and immunology, they describe step by step equipment designed to question how MHC-binding peptides are generated, to check how peptides are brought to MHC molecules, to research MHC peptide-binding styles, and to assay the T-cell reaction to the MHC/peptide complicated. Emphasis is given these technical steps severe for experimental good fortune which are frequently passed over from equipment released within the fundamental literature. Eminently available and state of the art, Antigen Processing and Presentation Protocols presents either new and skilled investigators with hugely functional instruments that would expand the questions that may be requested, and successfully be spoke back, relating antigen processing/presentation.

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

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3. Methionine (Met) starving medium: Met-free, serum-free medium (RPMI or Dulbecco’s modified Eagle’s medium [DMEM]), containing 20mM HEPES. 4. PBS containing 10 mM L-Met (PBS–Met). 5. 5% fetal calf serum (FCS) and L-Met (I/Met). 6. rVV expressing the chimeric protein UbRNP. 7. 5% (v/v) 2-mercaptoethanol. 8. Protease inhibitor cocktail. Boehringer Mannheim’s (Indianapolis, IN) Complete inhibitors work well for this purpose. The cocktail is usually prepared as a 25X stock solution in water. 9. PhosphorImager (Molecular Dynamics, Sunnyvale, CA, or Fuji, Medical Systems, Stamford, CT), with software for quantitation of protein bands.

Biopolymers 43, 269–280. 8. , Powers, J. , and Orlowski, M. (1992) Inhibition of the chymotrypsin-like activity of the pituitary multicatalytic proteinase complex. Biochemistry 31, 9421–9428. 9. , and Huber, R. (1995) Crystal structure of the 20S proteasome from the Archaeon T. 4 Å resolution. Science 268, 533–539. 10. , Standaert, R. , Lane, W. , Corey, E. , and Schreiber, S. L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin.

Introduction Since the discovery of cross priming by Bevan (1) nearly thirty years ago, a large amount of work has focused on defining the mechanisms that account for this in vivo phenomenon. Following the discovery that the majority of major histocompatibility complex (MHC-I)-bound peptides are derived from endogenous (intracellular) sources (2,3), a paradigm was established that exogenous (extracellular) antigens (Ags) are presented on MHC-I molecules and endogenous Ags are presented on MHC-II.

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