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For Research Use Only. Not For Clinical Use.
Plasma proteins
Membrane, Secreted (different isoforms)
Cell type enhanced (Adipocytes, NK-cells, Hepatic stellate cells)
Low immune cell specificity
Cell line enhanced (ASC diff, U-266/70)
Forms a heterotrimer with B2M and a self- or a pathogen-derived peptide (peptide-bound HLA-E-B2M) (PubMed:18339401, 30087334). Similarly to MHC class Ia assembly, HLA-E-B2M heterodimer interacts with components of the antigen processing machinery TAPBP and TAP1-TAP2 complex; this interaction is required for peptide loading and translocation to the cell surface (PubMed:9427624). Interacts with CALCR; this interaction is required for appropriate folding (PubMed:9427624). The optimum binding peptide is a nonamer (VL9) that is primarily derived from amino-acid residues 3-11 of the signal sequences of most HLA-A, -B, -C and -G molecules (PubMed:9754572, 18083576, 9660937, 18339401). The VL9 peptide anchors to five main sites in the peptide-binding groove of HLA-E (PubMed:18339401). Peptide-bound HLA-E-B2M complex interacts with KLRD1-KLRC1 receptor on NK cells (PubMed:9486650, 18083576). Binds with lower affinity to activating KLRD1-KLRC2 (PubMed:18083576, 23335510). The common subunit KLRC1 plays a prominent role in directly interacting with HLA-E (PubMed:18083576). Peptide-bound HLA-E-B2M interacts with the alpha-beta TCR on unconventional CD8+ T cells (PubMed:16474394). Peptide-free HLA-E interacts with HLA-F-B2M complex; this interaction may regulate the intracellular trafficking and the stability of peptide-free MHC class I open conformers (OCs).