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Leukocyte immunoglobulin-like receptor B1 (LILRB1, also known as ILT2/CD85j) is a type I transmembrane inhibitory leukocyte receptor encoded by the LILRB1 gene. It contains four extracellular immunoglobulin-like domains and intracellular ITIM motifs that recruit SHP phosphatases, and is widely expressed on monocytes, macrophages, dendritic cells, NK cells, and subsets of lymphocytes. LILRB1 recognizes multiple classical and non-classical HLA class I molecules, particularly β2-microglobulin-associated HLA-I complexes, including HLA-G. LILRB2 also recognizes diverse HLA-I ligands, including HLA-G, but differs from LILRB1 in its ability to interact with certain β2-microglobulin-free HLA-I heavy chains. Through HLA-I-dependent inhibitory signaling, LILRB1 contributes to immune tolerance and regulation of NK-, T-, and myeloid-cell activity. Altered LILRB1 signaling has also been associated with immunosuppressive tumor microenvironments, making it an important research target for HLA-I recognition and inhibitory immune signaling studies.
LILRB1, as a broad-spectrum MHC-I inhibitory receptor anchored on the surface of myeloid cells and NK cell membranes, relies on the extracellular immunoglobulin domains arranged in series to specifically recognize HLA-I ligands bound by β2 microglobulin, and at the same time recruits tyrosine phosphatase through intracellular ITIM motifs to start the downstream cascade inhibition signal. It can combine the broad-spectrum ligand binding characteristics of classical HLA subtypes, form a clear functional differentiation with LILRB2 which only targets HLA-G, and construct a universal tumor immunosuppression control axis for the body. The inhibitory signal pathway mediated by LILRB1 can dynamically balance the physiological self-tolerance and the pathological immune escape process of tumor according to the HLA expression level of tumor tissue. This molecule is widely involved in many physiological and pathological processes, such as the establishment of placental immune tolerance, the maintenance of chronic inflammation and the immune escape of tumor metastasis. The loss or blocking of LILRB1 function can effectively restore the potent anti-tumor activity of NK cells and cytotoxic T cells. To sum up, LILRB1 is the key core target for the study of leukocyte immune checkpoint mechanism and the research and development of tumor combined immunotherapy.
Fig. 1 Tri-panel signaling schematic for studying LILRB1/2/3 inhibitory function in myeloid cell pathogen immune evasion across malaria, bacterial and dengue virus infection.1
The biological functions of four-Ig domain inhibitory LILRB1 receptor are fully focused on β2m-HLA capture and SHP phosphatase signal inhibition:
Creative Biolabs offers high-quality LILRB1 proteins through optimized myeloid eukaryotic expression systems, including full-length four-Ig receptor and isolated HLA-binding extracellular domain variants. These products retain native broad MHC-I binding and SHP recruitment dual activity, suitable for combinatorial checkpoint inhibitor screening assays. All LILRB1 proteins undergo strict quality control to ensure consistent performance and reliable application across immuno-oncology research platforms.
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Creative Biolabs provides custom-engineered LILRB1 stable cell lines, including myeloid mimic overexpression and blank empty vector control models. These cell lines are optimized for inhibitory checkpoint profiling and NK cytotoxic signal functional analysis. Each cell line undergoes stringent validation to ensure stable expression profiles during long-term tumor co-culture, and can be widely deployed for large-scale combination immunotherapy compound screening experiments.
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High-specificity recombinant antibodies targeting LILRB1 are developed via advanced antibody engineering technologies, with no cross-reactivity with LILRB2/3 inhibitory paralogs. These antibodies are validated for macrophage/NK cell membrane localization detection and tumor stromal expression profiling, and can be combined with HLA-A detection reagents to analyze complete LILRB1 immune inhibitory complexes in myeloid models.
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Beyond catalog products, Creative Biolabs offers specialized custom services for LILRB1 research:
LILRB1 is an ITIM inhibitory receptor that binds broad HLA-I molecules to suppress NK and CD8+ T cell anti-tumor cytotoxicity.
LILRB1 mediates tumor immune escape and serves as promising target for PD-1 combination immunotherapy.
No, all LILRB1 products and services are strictly for research use only, not intended for clinical immunotherapy trials.
Offerings include full-length LILRB1 inhibitory receptors, isoform-specific detection antibodies and custom stable cell lines for myeloid research.
LILRB1 proteins are validated via broad HLA-I ligand binding and SHP phosphatase co-binding functional testing.