Recombinant Human CD300b/LMIR5 Fc Chimera Protein, CF
Recombinant Human CD300b/LMIR5 Fc Chimera Protein, CF Summary
Product Specifications
| Human CD300b (Ile55-His187) Accession # AAH28091 | IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
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.
1522-LM
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 200 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.
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Scientific Data
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When Recombinant Human CD300b/LMIR5 Fc Chimera (Catalog # 1522-LM) is immobilized at 2 µg/mL (100 µL/well), Recombinant Human LMIR2/CD300C Fc Chimera (Catalog # 3256-LM) binds with an ED50 of 1.5-9 µg/mL.
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2 μg/lane of Recombinant Human CD300b/LMIR5 Fc Chimera (Catalog # 1522-LM) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 46-59 kDa and 95 -120 kDa, respectively.
Reconstitution Calculator
Background: CD300b/LMIR5
LMIR5, also known as CD300b, CD300LB, CLM-7, and IREM‑3, is a glycoprotein member of the immunoglobulin superfamily (1). Human LMIR5 consists of a 134 amino acid (aa) extracellular domain (ECD) with one Ig-like V-type domain, a 21 amino acid (aa) transmembrane segment, and a 29 aa cytoplasmic domain (2). Within the ECD, human LMIR5 shares 51 % sequence identity with mouse and 57% aa sequence identity with rat LMIR5. The transmembrane segment contains a positively charged lysine which enables the association of LMIR5 with DAP12, DAP10, and potentially other adaptor proteins (2, 3). The cytoplasmic domain of human LMIR5 contains a phosphorylatable tyrosine motif, while that of mouse LMIR5 does not (2). LMIR5 is expressed on the surface of myeloid lineage cells (2-4). It forms noncovalent cis‑homodimers and cis-heterodimers with other CD300 family proteins, and the composition of these dimers affects the cellular response (2, 5). Antibody cross‑linking of LMIR5 induces mast cell granule release and cytokine production as well as its tyrosine phosphorylation of LMIR5 (in human) (2, 3). LMIR5 interacts with TIM1 and TIM4 which regulate T cell activation and are themselves binding partners (6). TIM1 interactions with LMIR5 mediate mast cell activation and the accumulation of neutrophils at sites of TIM1 up‑regulation on damaged renal tubule epithelial cells (6).
- Clark, G.J. et al. (2009) Trends Immunol. 30:209.
- Martinez-Barriocanal, A. et al. (2006) J. Immunol. 177:2819.
- Yamanishi, Y. et al. (2008) Blood 111:688.
- Wu, Y. et al. (2011) Cell. Immunol. 268:68.
- Martinez-Barriocanal, A. et al. (2010) J. Biol. Chem. 285:41781.
- Yamanishi, Y. et al. (2010) J. Exp. Med. 207:1501.
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