Anti-HLA-DR1 (empty) Purified

*Potolicchio I, Chitta S, Xu X, Fonseca D, Crisi G, Horejsi V, Strominger JL, Stern LJ, Raposo G, Santambrogio L: Conformational variation of surface class II MHC proteins during myeloid dendritic cell differentiation accompanies structural changes in lysosomal MIIC. J Immunol. 2005 Oct 15;175 (8) :4935-47. , URL: https://www.ncbi.nlm.nih.gov/pubmed/16210595?dopt=, *Carven GJ, Chitta S, Hilgert I, Rushe MM, Baggio RF, Palmer M, Arenas JE, Strominger JL, Horejsi V, Santambrogio L, Stern LJ: Monoclonal antibodies specific for the empty conformation of HLA-DR1 reveal aspects of the conformational change associated with peptide binding. J Biol Chem. 2004 Apr 16;279 (16) :16561-70., URL: https://www.ncbi.nlm.nih.gov/pubmed/14757758?ordin

The antibody MEM-267 specifically binds extracellularly to the empty but not peptide-loaded form of HLA-DR1. DR is the isotypes of human MHC Class II molecules expressed on antigen-presenting cells (APC; dendritic cells, B lymphocytes, monocytes, macrophages) .