Recombinant Human LILRB5/CD85c/LIR-8 Protein, CF
Recombinant Human LILRB5/CD85c/LIR-8 Protein, CF Summary
Product Specifications
Arg18-His456, with a C-terminal 6-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
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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Scientific Data
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When Recombinant Human LILRB5/CD85c/LIR-8 is coated at 2 µg/mL, Recombinant Human Angiopoietin-like Protein 7/ANGPTL7 (Catalog # 914-AN) binds with an apparent Kd<4 nM.
Reconstitution Calculator
Background: LILRB5/CD85c/LIR-8
LIR8, also known as CD85c and LILRB5, belongs to the Leukocyte immunoglobulin-like receptors (LILR) family of transmembrane glycoproteins involved in regulating immune responses (1,2). There are at least thirteen LILR family members and are divided into activating (LILRA) or inhibiting (LILRB) molecules (1,2). Mature human LIR8 consists of an extracellular domain (ECD) with four Ig-like domains, a transmembrane segment, and a cytoplasmic domain with two immunoreceptor tyrosine-based inhibitory motifs (ITIM). Alternative splicing of human LIR8 generates at least 2 isoforms, one lacking the second Ig-like domain. The LILR family appears to be primate-specific receptors in terms of sequence homology. LIR8 is expressed on NK cells and in the tryptic granules of mast cells and negatively regulates immune cell activation (3, 4). It is present on the mast cell surface following cell activation and degranulation (4). Activated mast cells may also release soluble forms of LIR8 (3). LIR8 has also been shown to be expressed on T cells and induce CD8+ T cell proliferation (5). Consistent with the demonstrated binding of LILRB2 to Angiopoietin-like 2 and 5 (6), R&D Systems in-house testing indicates that LIR8 binds to Angiopoietin-like 7. Recently, a common missense variant of LIR8 was found to be associated with statin intolerance and myalgia (7).
- Brown, D. et al. (2004) Tissue antigens. 64:215.
- 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.
- Hogan, H. E. et al. (2016) Sci Rep. 6:21780.
- Zheng, J. et al. (2012) Nature 485:656.
- Siddigui, M. et al. (2017) Eur. Heart J. 38:3569.
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Average Rating: 5 (Based on 1 Review)
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Reason for Rating: good material/ no binding observed on our lead molecule
Performed binding specificity experiments for the lead molecule (xLILRA6) on its ligand family panels (RA1, RA2, RA5, RA6, RB1, RB2, RB3, RB4, RB5)
