Recombinant Mouse CD300f/LMIR3 Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by its ability to inhibit anti-CD3 antibody induced IL-2 or IFN-gamma secretion by human T cells. The ED50 for this effect 1.50‑15.0 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse CD300f/LMIR3 protein CD300f/LMIR-3 (Cys16-Gly188) Accession # Q6SJQ7.1 | IEGRMDP | Mouse IgG2a (Glu98-Lys330) | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Cys16 & Glu20 |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
46 kDa. 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 |
55-65 kDa, under 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 |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 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 Mouse CD300f/LMIR3 Fc Chimera Protein, CF
Background
Leukocyte mono-immunoglobulin-like receptor 3 (LMIR3), also called
CD300f and CLM-1, is a member of the paired immune receptor
family within the immunoglobulin superfamily (1). Mature mouse LMIR3 consists
of an extracellular domain (ECD) with one Ig-like V-type domain, a
transmembrane segment, and a cytoplasmic domain that contains two
immunoreceptor tyrosine-based inhibitory motifs (ITIMs) and immunoreceptor
tyrosine-based switch motif (ITSM) (2). Alternate splicing generates additional
isoforms with varying length C-terminal tails following the ECD (3). Within the
ECD, mouse LMIR3 shares 43% amino acid (aa) sequence identity with human LMIR3.
LMIR3 is expressed on the surface of dendritic cells, monocytes, granulocytes,
and mast cells as well as on acute myeloid leukemia (AML) blasts (3, 4). Pervanadate
treatment or antibody cross‑linking of LMIR3 induces phosphorylation of
tyrosine residues in the cytoplasmic domain and the subsequent recruitment of
phosphatases SHIP, SHP-1, SHP-2, and the p85 alpha subunit of PI3K
(3, 5, 6). LMIR3 appears to exhibit a dual function in mast cells.
LMIR3 functions as a negative regulator of MC activation through an inhibitory
effect on Fc epsilon RI-mediated cytokine production in mast cells (5). Conversely, it
enhances TLR4‑mediated signaling/cytokine production in mast cells through
association with the activating signaling protein FcR gamma (5). Additionally, LMIR3
ligation can induce cell death and inhibit signaling through multiple receptors
including Fc epsilon RI, LMIR4, SCF R, TLR2, TLR3, and TLR9 (3-8). In mouse, a
splice variant of LMIR3 (known as DIgR2, with a 7 aa insertion in the ECD)
inhibits CD4+ T cell activation and in vivo Th1
and CTL responses (9). LMIR3 is up‑regulated on monocytes surrounding
experimentally-induced spinal cord demyelination and functions as a negative
regulator of inflammation in the CNS (10).
- Clark, G.J. et al. (2009) Trends Immunol. 30:209.
- Izawa, K. et al. (2012) Immunity 37:827.
- Alvarez-Errico, D. et al. (2004) Eur. J. Immunol. 34:3690.
- Korver, W. et al. (2009) Leukemia 23:1587.
- Izawa, K. et al. (2009) J. Immunol. 183:925.
- Alvarez-Errico, D. et al. (2007) J. Immunol. 178:808.
- Can, I. et al. (2008) J. Immunol. 180:207.
- Izawa, K. et al. (2007) J. Biol. Chem. 282:17997.
- Shi, L. et al. (2006) Blood 108:2678.
- Xi, H. et al. (2010) J. Exp. Med. 207:7.
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