LILRA2/CD85h/ILT1 Protein, Human (Biotinylated, HEK293, His-Avi)

LILRA2/CD85h/ILT1 protein plays a crucial role in innate immune responses against microbial infection. It specifically recognizes a subset of N-terminally truncated immunoglobulins resulting from protease cleavage in various pathogenic bacteria and fungi, including L. pneumophila, M. hyorhinis, S. pneumoniae, S. aureus, and C. albicans. The protein binds to epitopes located partly in the variable region of immunoglobulin light chains, requiring the constant region for signaling. LILRA2 interacts with cleaved IgM, IgG3, and IgG4 but does not bind to cleaved IgA1. Activation through the binding of N-terminally truncated immunoglobulins triggers neutrophil activation, leading to the release of various cytokines and chemokines. In monocytes, this activation induces the release of CSF2, CF3, IL6, CXCL8, and CCL3, while down-regulating responses to bacterial lipopolysaccharide (LPS), potentially through the down-regulation of TLR4 expression. Additionally, in eosinophils, ligand binding results in the release of RNASE2, IL4, and leukotriene C4. Importantly, LILRA2 does not bind to class I MHC antigens and exists as a homodimer.