LILRB1 Antibody - #DF9603

Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G and HLA-F alleles. Receptor for H301/UL18, a human cytomegalovirus class I MHC homolog. Ligand binding results in inhibitory signals and down-regulation of the immune response. Engagement of LILRB1 present on natural killer cells or T-cells by class I MHC molecules protects the target cells from lysis. Interaction with HLA-B or HLA-E leads to inhibition of FCER1A signaling and serotonin release. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions. Recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide. Upon interaction with peptide-bound HLA-G-B2M complex, triggers secretion of growth-promoting factors by decidual NK cells. Reprograms B cells toward an immune suppressive phenotype.

Phosphorylated on tyrosine residues. Dephosphorylated by PTPN6.

Cell membrane>Single-pass type I membrane protein.

Secreted.

Expressed in B cells, monocytes and various dendritic cell (DC) subsets including myeloid, plasmacytoid and tolerogenic DCs (at protein level). Expressed in decidual macrophages (at protein level). Expressed in decidual NK cells (at protein level).

Binds PTPN6 when phosphorylated. Binds FCER1A and FCGR1A. Interacts with human cytomegalovirus/HHV-5 protein UL18. Interacts with peptide-bound HLA-G-B2M complex. Interacts with peptide-bound HLA-F-B2M complex but not with peptide-free HLA-F open conformer. It does not probe the peptide sequence directly.

Contains 4 copies of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. The phosphorylated ITIM motif can bind the SH2 domain of several SH2-containing phosphatases.