详细说明
- Purity>90%, by SDS-PAGE with silver staining
- Endotoxin Level<0.10 EU per 1 μg of the protein by the LAL method.
- ActivityMeasured by its binding ability in a functional ELISA. When Recombinant Human LILRB5/CD85c/LIR-8 is coated at 2 μg/mL, Recombinant Human Angiopoietin-like Protein 7/ANGPTL7 (Catalog # ) binds with an apparent K d <4 nM.
- SourceMouse myeloma cell line, NS0-derived Arg18-His456, with a C-terminal 6-His tag
- Accession #
- N-terminal Sequence
AnalysisArg18 - Predicted Molecular Mass49 kDa
- SDS-PAGE64-77 kDa, reducing conditions
| 8487-T4 | | |
| Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
| Reconstitution Reconstitute at 100 μg/mL in PBS. | ||
| Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
| Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: LILRB5/CD85c/LIR-8
LIR-8, also known as CD85c and LILRB5, belongs to a family of transmembrane glycoproteins that negatively regulate immune cell activation (1). Mature human
LIR-8 consists of a 435 amino acid (aa) extracellular domain with four Ig-like domains, a 21 aa transmembrane segment, and a 111 aa cytoplasmic domain with two immunoreceptor tyrosine-based inhibitory motifs (ITIM) (2). Alternative splicing of human LIR-8 generates an isoform that lacks the second Ig-like domain. LIR-8 is expressed on NK cells and in the tryptic granules of mast cells (2, 3). Following cell activation and degranulation, it is present on the mast cell surface (3). Activated mast cells may also release soluble forms of LIR-8 (3). Consistent with the demonstrated binding of LILRB2 to Angiopoietin-like 2 and 5 (4), R&D Systems in-house testing indicates that LIR-8 binds to Angiopoietin-like 7.
LIR-8 consists of a 435 amino acid (aa) extracellular domain with four Ig-like domains, a 21 aa transmembrane segment, and a 111 aa cytoplasmic domain with two immunoreceptor tyrosine-based inhibitory motifs (ITIM) (2). Alternative splicing of human LIR-8 generates an isoform that lacks the second Ig-like domain. LIR-8 is expressed on NK cells and in the tryptic granules of mast cells (2, 3). Following cell activation and degranulation, it is present on the mast cell surface (3). Activated mast cells may also release soluble forms of LIR-8 (3). Consistent with the demonstrated binding of LILRB2 to Angiopoietin-like 2 and 5 (4), R&D Systems in-house testing indicates that LIR-8 binds to Angiopoietin-like 7.
- References:
- Thomas, R. et al. (2010) Clin. Rev. Allergy Immunol. 38:159.
- Borges, L. et al. (1997) J. Immunol. 159:5192.
- Tedla, N. et al. (2008) J. Leukoc. Biol. 83:334.
- Zheng, J. et al. (2012) Nature 485:656.
- Long Name:Leukocyte Immunoglobulin-Like Receptor, Subfamily B (With TM And ITIM Domains), Member 5
- Entrez Gene IDs:10990 (Human)
- Alternate Names:CD85 antigen-like family member C; CD85c antigen; CD85c; Leukocyte immunoglobulin-like receptor 8; leukocyte immunoglobulin-like receptor, subfamily B (with TM and ITIM domains); LILRB5; LIR8; LIR-8; LIR8CD85C; LIR-8leukocyte immunoglobulin-like receptor subfamily B member 5; member 5
400-6226-992