Recombinant Human CD300a/LMIR1 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its ability to inhibit anti-CD3-induced proliferation of stimulated human T cells. The ED50 for this effect is 1-5 µg/mL. Optimal dilutions should be determined by each laboratory for each application. |
Source |
Mouse myeloma cell line, NS0-derived human CD300a/LMIR1 protein
Human CD300a (Leu18-Gln178) Accession # Q9UGN4 |
IEGRMD |
Human IgG1 (Pro100-Lys330) |
N-terminus |
|
C-terminus |
|
|
Accession # |
|
N-terminal Sequence |
Leu18 |
Structure / Form |
Disulfide-linked homodimer
|
Protein/Peptide Type |
Recombinant Proteins |
Gene |
CD300A |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
44.0 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
60-80 kDa, reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD300a/LMIR1 Fc Chimera Protein, CF
Background
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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