Clone REA406 recognizes the human HLA-DM antigen, a non-classical MHC class II molecule (MHC II) chaperone that works in lysosomes and endosomes. MHC II molecules are transmembrane glycoproteins which function by binding processed antigenic peptides and presenting them to CD4+ T lymphocytes to initiate or maintain a specific immune response. Constitutive MHC II expression is restricted to professional antigen presenting cells including dendritic cells (DCs), B cells, and macrophages and to the epithelial cells of the thymus. Functional class II expression is highly dependent on the expression of two main chaperones, the invariant chain (Ii) and DM. Newly synthesized class II α- and β-chains form a nonameric complex with three Ii molecules in the endoplasmic reticulum where Ii blocks the peptide-binding groove and guides class II dimers to the endocytic pathway where Ii is proteolytically cleaved leaving the CLIP fragment bound to class II. HLA-DM, an endocytic chaperone, protects empty class II dimers until they bind a peptide capable to confer enough stability to the complex.
Additional information: Clone REA406 displays negligible binding to Fc receptors.
HLA-DMA, HLA-DMB, DMA, HLADM, RING6, D6S221E, RING7
Technical specifications
