Recombinant Mouse CD300a/LMIR1 Fc Chimera Protein, CF
Recombinant Mouse CD300a/LMIR1 Fc Chimera Protein, CF Summary
Optimal dilutions should be determined by each laboratory for each application.
Accession # BAC80268.1
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.
|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.
LMIR1, also known as CD300a, CMRF-35H, IRp60, CLM-8, and MAIR-I, is a 60 kDa glycoprotein member of the immunoglobulin superfamily (1). Mouse LMIR1 consists of a 158 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain, a 21 aa transmembrane segment, and a 112 aa cytoplasmic domain that contains three immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and a non-canonical ITIM (2, 3). Within the ECD, mouse LMIR1 shares 40% and 66% aa sequence identity with human and rat LMIR1, respectively. Alternate splicing generates an additional mouse LMIR1 isoform with a 4 aa deletion following the Ig-like domain (3). In mouse, LMIR1 is expressed on peripheral eosinophils, mast cells, neutrophils, dendritic cells, macrophages, and some B cells (2-4). 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 (4, 8‑10). LMIR1 cross‑linking also limits the in vivo activities of these cells with a subsequent reduction of allergic inflammation symptoms (4, 7, 9).
- Clark, G.J. et al. (2009) Trends Immunol. 30:209.
- Kumagai, H. et al. (2003) Biochem. Biophys. Res. Commun. 307:719.
- Yotsumoto, K. et al. (2003) J. Exp. Med. 198:223.
- Munitz, A. et al. (2006) J. Allergy Clin. Immunol. 118:1082.
- 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.
- Bachelet, I. et al. (2008) J. Immunol. 180:6064.
- Bachelet, I. et al. (2006) J. Allergy Clin. Immunol. 117:1314.
- Alvarez, Y. et al. (2008) Mol. Immunol. 45:253.
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