Recombinant Human CD300f/LMIR3 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to stimulate human T cell proliferation. The ED50 for this effect is 0.75-4.5 µg/mL. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human CD300f/LMIR3 protein
>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
Bioactivity
Theoretical MW
42.4 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
57-62 kDa, reducing conditions
Publications
Read Publications using 2774-LM in the following applications:
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 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 CD300f/LMIR3 Fc Chimera Protein, CF
CMRF35-like molecule 1
CD300 molecule-like family member f
CD300f
CD300LF
CLIM1
CLM1
CLM-1
DIgR2
IGSF13
IREM1
IREM-1
LMIR3
NKIR
Pigr3
Background
LMIR3, also known as CD300f, CD300LF, IREM-1, CLM-1, IgSF13, DIgR1, and MAIR-V, is a 50‑60 kDa glycoprotein member of the immunoglobulin superfamily (1). Human LMIR3 consists of a 137 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain, a 21 aa transmembrane segment, and a 113 aa cytoplasmic domain that contains multiple immunoreceptor tyrosine-based inhibitory motifs (ITIMs) or ITIM-like sequences (2, 3). Alternate splicing generates additional isoforms that carry substituted C-terminal tails of varying lengths and sequences following the ECD or transmembrane segment (3). Within the ECD, human LMIR3 shares 43% aa sequence identity with mouse and rat LMIR3. LMIR3 is expressed on the surface of dendritic cells, monocytes, granulocytes, and mast cells as well as on acute myeloid leukemia (AML) blasts (2-4). 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 (2, 3, 5, 6). 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 contrast, it enhances TLR4‑mediated signaling/cytokine production in mast cells through association with the activating signaling protein FcR gamma (5). 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.
Sui, L. et al. (2004) Biochem. Biophys. Res. Commun. 319:920.
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.
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