Recombinant Human CD300a/LMIR1 Fc Chimera Protein, CF Summary
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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.
2640-LM
| 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: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Reconstitution Calculator
Background: CD300a/LMIR1
LMIR1, also known as CD300a, CMRF-35H, IRp60, CLM-8, and MAIR-I, is a 60 kDa glycoprotein member of the immunoglobulin superfamily (1). Human LMIR1 consists of a 163 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain, a 21 aa transmembrane segment, and a 98 aa cytoplasmic domain that contains three immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and a non-canonical ITIM (2). Alternate splicing may generate additional isoforms that either lack the Ig-like domain or contain only the cytoplasmic domain. Within the ECD, human LMIR1 shares 40% and 43% aa sequence identity with mouse and rat LMIR1, respectively. In human, LMIR1 is expressed on peripheral blood eosinophils, mast cells, neutrophils, plasmacytoid dendritic cells, and various T cell subsets (3-7). Antibody cross‑linking of LMIR1 induces phosphorylation of tyrosine residues in the cytoplasmic domain. This leads to the recruitment of phosphatases SHIP, SHP-1, and SHP-2 and inhibition of NK cell, eosinophil, and mast cell activation (2, 3, 5-7). Cross‑linking of LMIR1 to other surface proteins such as SCF R or Fc epsilon RI on mast cells, Fc gamma RIIA on neutrophils, or CCR3 on mast cells and eosinophils inhibits downstream signaling from those receptors (5, 10‑12). LMIR1
cross‑linking also limits the in vivo activities of these cells with a subsequent reduction of allergic inflammation symptoms (4, 11, 12).
- Clark, G.J. et al. (2009) Trends Immunol. 30:209.
- Cantoni, C. et al. (1999) Eur. J. Immunol. 29:3148.
- Munitz, A. et al. (2006) Blood 107:1996.
- Bachelet, I. et al. (2005) J. Immunol. 175:7989.
- Alvarez, Y. et al. (2008) Mol. Immunol. 45:253.
- Ju, X. et al. (2008) Blood 112:1184.
- Clark, G.J. et al. (2007) J. Leukoc. Biol. 82:1126.
- Kumagai, H. et al. (2003) Biochem. Biophys. Res. Commun. 307:719.
- Yotsumoto, K. et al. (2003) J. Exp. Med. 198:223.
- Bachelet, I. et al. (2008) J. Immunol. 180:6064.
- Bachelet, I. et al. (2006) J. Allergy Clin. Immunol. 117:1314.
- Munitz, A. et al. (2006) J. Allergy Clin. Immunol. 118:1082.
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