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The HM14-1 monoclonal antibody specifically binds to the FAIM3 -encoded high affinity receptor for IgM (also known as, Fcµ Receptor, FcμR, Fc mu receptor, Immunoglobulin mu Fc receptor, FcmR, IgM Fc receptor). The FcμR is a type 1 transmembrane glycoprotei n that contains an extracellular Ig-like domain with sequence similarities to Fcα/μR and pIgR. It is likewise known as Fas apoptotic inhibitory molecule 3, TOSO or Regulator of Fas-induced apoptosis Toso based on its capacity to counter apoptosis mediated by Fas/CD95 (or TNF) in some experimental model systems. FcμRs are expressed by B cells, CD4 T cells, CD8 T cells, and NK cells and are highly expressed on Chronic Lymphocytic Leukemia cells. FcμRs may play roles in cellular activation, antigen presentation and IgM-dependent cell-mediated cytotoxicity. The relatively long cytoplasmic tail of FcμR contains several conserved tyrosine and serine residues. These get phosphorylated after FcμR ligation with Ig M immune complexes and may initiate signaling responses. Lymphocyte FcμRs can mediate the internalization of IgM-bound antigens including microbial and viral antigens. This in turn may cause cellular activation due to subsequent antigen processing and exposure of activating ligands to intracellular receptors including Toll-like receptors. The HM7-10 antibody, a related FcμR-specific antibody, reportedly recognizes an epitope near the IgM ligand binding site of the FcμR whereas the HM14-1 antibody does not.
