LILRB2/CD85d/ILT-4 Protein, Human (HEK293, mFc)

LILRB2/CD85d/ILT-4 Protein, a receptor for class I MHC antigens, recognizes a broad range of HLA alleles. It crucially down-regulates immune responses, establishing tolerance. Specific recognition of HLA-G, with a self-peptide, leads to type 1 regulatory T cell and myeloid-derived suppressor cell differentiation, essential for maternal-fetal tolerance. LILRB2 competes with CD8A, inhibits FCGR1A-mediated responses, and interacts with PTPN6 when phosphorylated. Direct interactions with peptide-bound HLA-G-B2M and HLA-F-B2M emphasize its immune modulation role. LILRB2/CD85d/ILT-4 Protein, Human (HEK293, mFc) is the recombinant human-derived LILRB2/CD85d/ILT-4 protein, expressed by HEK293, with C-mFc labeled tag. The total length of LILRB2/CD85d/ILT-4 Protein, Human (HEK293, mFc) is 437 a.a., with molecular weight of 80-110 kDa.

The LILRB2/CD85d/ILT-4 Protein serves as a receptor for class I MHC antigens, demonstrating recognition across a broad spectrum of HLA-A, HLA-B, HLA-C, HLA-G, and HLA-F alleles. It plays a crucial role in immune response down-regulation and the establishment of tolerance. Specifically, it recognizes HLA-G in complex with B2M/beta-2 microglobulin and a nonamer self-peptide, leading to the differentiation of type 1 regulatory T cells and myeloid-derived suppressor cells, crucial for maintaining maternal-fetal tolerance. LILRB2 competes with CD8A for binding to class I MHC antigens and inhibits FCGR1A-mediated cellular responses, including phosphorylation of proteins and mobilization of intracellular calcium ions. Moreover, it interacts with PTPN6 when phosphorylated and binds to FCGR1A. The direct interactions with peptide-bound HLA-G-B2M and HLA-F-B2M further highlight its involvement in immune modulation.

Human

HEK293

C-mFc

Q8N423 (Q22-H458)

10288  [NCBI]

80-110 kDa

Greater than 95% as determined by Tris-Bis PAGE.

<1 EU/μg, determined by LAL method.