Anti-Human HLA-DP (Clone B7/21) - Purified No Carrier Protein (H250-GRP)

This anti-HLA-DP antibody is a recombinant chimeric version of the original clone B7/21 antibody. The variable domain sequences are identical to the original clone B7/21; however, the constant region sequences have been switched from mouse IgG3 which is prone to precipitation to human IgG1 to allow for easier downstream uses. This Recombinant HLA-DP antibody, clone B7/21, recognizes the major histocompatibility complex (MHC) class II molecule Human Leukocyte Antigen - DP isotype (HLA-DP). MHC class II is constitutively expressed on human professional antigen-presenting cells (APCs), including macrophages/monocytes, dendritic cells (DCs), and B cells, and is induced on T cells upon activation1. HLA-DP consists of two transmembrane proteins, a 35 kDa α (heavy) chain and 29 kDa β (light) chain2 encoded by the HLA-DPA1 and HLA-DPB1 genes, respectively, located in the HLA complex of chromosome 6. The N-terminal α1 and β1 domains form the antigen-binding groove, which binds 13-25 aa peptides derived from exogenous antigens3. On APCs, MHC class II plays a critical role in the adaptive immune response by presenting phagocytosed antigens to helper CD4 T cells. The T cell receptor (TCR)/CD3 complex of CD4 T cells interacts with peptide-MHC class II, which induces CD4 T cell activation leading to the coordination and regulation of other effector cells. CD4 molecules also bind to MHC class II, which helps augment TCR signaling4. It has also been demonstrated that MHC class II express on activated T cells are capable of antigen presentation5 and can transduce signals into T cells, enhancing T cell proliferation and activity6. High HLA-DP expression is associated with an increased risk of graft-versus-host disease7. Specific alleles of HLA-DP are associated with autoimmune diseases, including rheumatoid arthritis8.