Recombinant Human Leukocyte immunoglobulin-like receptor subfamily A member 2 (LILRA2), partial

Product Details

Abbreviation
LILRA2
Purity
>85% (SDS-PAGE)
Target Names
LILRA2
Uniprot NO.
Alternative Names
LILRA2; ILT1; LIR7; Leukocyte immunoglobulin-like receptor subfamily A member 2; CD85 antigen-like family member H; Immunoglobulin-like transcript 1; ILT-1; Leukocyte immunoglobulin-like receptor 7; LIR-7; CD antigen CD85h
Species
Homo sapiens (Human)
Source
Yeast
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage Condition
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)
Part of the innate immune responses against microbial infection. Specifically recognizes a set of N-terminally truncated immunoglobulins that are produced via cleavage by proteases from a range of pathogenic bacteria and fungi, including L.pneumophila, M.hyorhinis, S.pneumoniae, S.aureus and C.albicans. Recognizes epitopes that are in part in the variable region of the immunoglobulin light chains, but requires also the constant region for signaling. Binds to a subset of cleaved IgM, IgG3 and IgG4 molecules, but does not bind cleaved IgA1. Binding of N-terminally truncated immunoglobulins mediates activation of neutrophils. In monocytes, activation leads to the release of CSF2, CF3, IL6, CXCL8 and CCL3 and down-regulates responses to bacterial lipopolysaccharide (LPS), possibly via down-regulation of TLR4 expression and reduced signaling via TLR4. In eosinophils, activation by ligand binding leads to the release of RNASE2, IL4 and leukotriene C4. Does not bind class I MHC antigens.
Gene References into Functions
  1. findings demonstrate that LILRA2 is a type of innate immune receptor in the host immune system that detects immunoglobulin abnormalities caused by microbial pathogens. PMID:27572839
  2. LILRA2 recognizes microbially cleaved antibodies and activates innate immunity, suggesting that LILRA2 detects dangerous immunological situations in which antibodies are destroyed by pathogens. PMID:27572839
  3. LILRA2-mediated activation of monocytes is significantly different to LPS and that LILRA2 selectively modulates LPS-mediated monocyte activation and FcgammaRI-dependent phagocytosis. PMID:22479404
  4. LIR7 is an activating receptor for eosinophils that elicited the release of cytotoxic granule proteins, de novo lipid mediator generation, and cytokine release through vesicular transport PMID:12529506
  5. Cross-linking of basophil LIR7 resulted in the concentration-dependent net release of histamine and cysteinyl leukotrienes that were maximal at 30 minutes, and of IL-4 that was maximal at 4 hours PMID:15242876
  6. Progenitor mast cells expressed cell surface activating LILRA2. Mature cord-blood-derived mast cells had detectable mRNA encoding multiple LILRs, none were expressed on the cell surface. PMID:17998301
  7. LILRA2 activation, by altering GM-CSF-induced monocyte differentiation into immature DC, provides a mechanism for down-regulating the ability of the innate immune system to activate the adaptive T cell response while promoting an inflammatory response. PMID:18056355
  8. LILRA2 Delta 419-421 isoform encoded by the splice site SNP may play a role in systemic lupus erythematosus and microscopic polyangiitis. PMID:18273033
  9. The authors report the LILRA2 extracellular D1D2 domain crystal structure, which reveals structural shifts of the corresponding MHC-binding amino acid residues in comparison with LILR B1/B2, explaining its non-binding to MHC molecules. PMID:19230061

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Subcellular Location
Cell membrane; Single-pass type I membrane protein.; [Isoform 4]: Secreted.
Tissue Specificity
Detected on the surface of all peripheral blood monocytes, neutrophils, basophils and eosinophils (at protein level). Expression levels are very low or not detectable on monocytes, T-cells, B-cells, dendritic cells and natural killer (NK) cells.
Database Links

HGNC: 6603

UNIGENE: Hs.655593

KEGG: hsa:11027

STRING: 9606.ENSP00000251377

OMIM: 604812

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