Human MHC is known as Human Leukocyte Antigen (HLA). Human MHC can be divided into MHC I, MHC II and MHC III. MHC I is composed of an alpha chain that spans the cell membrane and an extracellular β2- microglobulin (B2M) attached to this chain. The entire molecule consists of four regions, three of which are in the α chain (α1, α2, α3) and the β2-microglobulin forms the fourth region. The α1 and α2 located outside the cell form a groove in which the polypeptide can bind. Most T lymphocytes express a single, highly specific antigen receptor, TCR, on their surface, which, in the presence of an antigen-presenting cell (APC), can bind directly to the MHC I- peptide complex and initiate a CD8-specific immune response. The TCR has a relatively low affinity for monomeric MHC I- polypeptide complexes and a rapid mismatch rate, while its affinity for MHC I- polypeptide tetramers is greatly enhanced.

Schematic Representation for Human MHC I and MHC II Molecular Structure

1. Three mature expression systems can be freely selected. (E. coli, mammalian cells, and insect baculovirus)

2. Robust MHC-peptide complex preparation process. (Optimized folding ratio and binding ratio, more stable process)

3. SA active protein developed by AtaGenix. (Forms tetramers of biotinylated MHC- peptide monomers)

1. Efficient sorting of specific T-cells

2. Research on virus evasion immune mechanism

3. TCR affinity study

4. Short peptide affinity screening for antigenic epitopes

5. MHC immune function study

6. TCR-like antibody screening