Sf9, Baculovirus cells.
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Greater than 95.0% as determined by SDS-PAGE.
LILRB1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 446 amino acids (24-461 a.a) and having a molecular mass of 48.5kDa.
LILRB1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Leukocyte Immunoglobulin Like Receptor B1 (LILRB1), a member of the leukocyte immunoglobulin-like receptor (LIR) family, is found on immune cells. It binds to MHC class I molecules on antigen-presenting cells, transmitting a negative signal that suppresses immune responses. This inhibitory action helps regulate inflammation, cytotoxicity, and self-reactivity. LILRB1 is present on various immune cells, including B cells, monocytes, subsets of NK cells, gamma delta T cells, memory/effector CD8+ T cells, and monocyte-derived dendritic cells.
Recombinant human LILRB1, produced in Sf9 Baculovirus cells, is a single, glycosylated polypeptide chain. It comprises 446 amino acids (24-461 a.a), resulting in a molecular weight of 48.5 kDa. The protein includes an 8 amino acid His-tag at the C-terminus and is purified using proprietary chromatographic methods.
The LILRB1 solution is provided at a concentration of 0.25 mg/ml in a buffer containing 10% glycerol and Phosphate-Buffered Saline (pH 7.4).
For short-term storage (2-4 weeks), the LILRB1 solution can be stored at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. To maintain protein integrity, avoid repeated freeze-thaw cycles.
The purity of LILRB1 is determined to be greater than 95.0% using SDS-PAGE analysis.
The biological activity of LILRB1 is greater than 50%. This activity is assessed by the protein's ability, when immobilized, to support the adhesion of HSB2 human peripheral blood acute lymphoblastic leukemia cells. The cells are introduced to LILRB1-coated plates at a concentration of 5 µg/ml.
Leukocyte immunoglobulin-like receptor subfamily B member 1,
Leukocyte immunoglobulin-like receptor 1, leucocyte Ig-like receptor B1, CD85 antigen-like family member J, Immunoglobulin-like transcript 2, myeloid inhibitory receptor 7, Monocyte/macrophage immunoglobulin-like receptor 7, Ig-like transcript 2, MIR-7, LILRB1, ILT2, LIR1, MIR7, LIR-1, ILT-2, PIRB, PIR-B
Sf9, Baculovirus cells.
GHLPKPTLWA EPGSVITQGS PVTLRCQGGQ ETQEYRLYRE KKTAPWITRI PQELVKKGQF PIPSITWEHT GRYRCYYGSD TAGRSESSDP LELVVTGAYI KPTLSAQPSP VVNSGGNVTL QCDSQVAFDG FILCKEGEDE HPQCLNSQPH ARGSSRAIFS VGPVSPSRRW WYRCYAYDSN SPYEWSLPSD LLELLVLGVS KKPSLSVQPG PIVAPEETLT LQCGSDAGYN RFVLYKDGER DFLQLAGAQP QAGLSQANFT LGPVSRSYGG QYRCYGAHNL SSEWSAPSDP LDILIAGQFY DRVSLSVQPG PTVASGENVT LLCQSQGWMQ TFLLTKEGAA DDPWRLRSTY QSQKYQAEFP MGPVTSAHAG TYRCYGSQSS KPYLLTHPSD PLELVVSGPS GGPSSPTTGP TSTSGPEDQP LTPTGSDPQS GLGRHLGVLE HHHHHH
Leukocyte Immunoglobulin-Like Receptor B1 (LILRB1), also known as CD85j, LIR1, and ILT2, is a transmembrane glycoprotein that plays a crucial role in the immune system. It is a member of the leukocyte immunoglobulin-like receptor (LILR) family, which includes both activating and inhibitory receptors that regulate immune cell activity .
LILRB1 is a protein-coding gene that belongs to the subfamily B class of LIR receptors. The encoded protein contains two or four extracellular immunoglobulin domains, a transmembrane domain, and two to four cytoplasmic immunoreceptor tyrosine-based inhibitory motifs (ITIMs) . These ITIMs are essential for the inhibitory function of LILRB1, as they recruit phosphatases that dephosphorylate signaling molecules, thereby downregulating immune cell activation .
LILRB1 is expressed on various immune cells, including neutrophils, monocytes, macrophages, dendritic cells, and some subsets of T and B cells . It serves as a receptor for human leukocyte antigen G (HLA-G), a non-classical major histocompatibility complex (MHC) class I molecule that plays a role in immune tolerance . By binding to HLA-G, LILRB1 can inhibit the activation of immune cells, thereby preventing excessive inflammation and tissue damage .
Elevated expression of LILRB1 has been associated with poor prognosis in certain cancers, such as glioma . In glioma, higher LILRB1 expression is linked to increased tumor immune infiltration and poorer patient outcomes. This suggests that LILRB1 may play a role in tumor immune evasion and could be a potential target for immunotherapy .
Recombinant human LILRB1 is produced using recombinant DNA technology, which involves inserting the gene encoding LILRB1 into a suitable expression system, such as bacteria or mammalian cells. This allows for the large-scale production of the protein for research and therapeutic purposes . Recombinant LILRB1 can be used to study its structure, function, and interactions with other molecules, as well as to develop potential therapeutic interventions targeting LILRB1.