LMIR5, also known as CD300LB, CLM-7, and IREM-3, is a 26kD-32kD glycoprotein member of the immunoglobulin superfamily. Mouse LMIR5 consists of a 140aa extracellular domain (ECD) with one Ig-like V-type domain, a 21aa transmembrane segment, and a 31aa cytoplasmic domain. Within the ECD, mouse LMIR5 shares 51% and 86% aa sequence identity with human and rat LMIR5, respectively. The transmembrane segment contains a positively charged lysine which enables the association of LMIR5 with DAP12, DAP10, and potentially other adaptor proteins. The cytoplasmic domain of human LMIR5 contains a phosphorylatable tyrosine motif, while that of mouse LMIR5 does not. LMIR5 is expressed on the surface of myeloid lineage cells. It forms noncovalent cis-homodimers and cis-heterodimers with other CD300 family proteins, and the composition of these dimers affects the cellular response. Antibody cross-linking of LMIR5 induces mast cell granule release and cytokine production as well as its tyrosine phosphorylation of LMIR5 (in human). LMIR5 interacts with TIM1 and TIM4 which regulate T cell activation and are themselves binding partners. 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.
Source:
Recombinant corresponding to aa18-157 from mouse LMIR5 expressed in mouse myeloma cell line, NS0.
Molecular Weight:
~43.2kD
Biological Activity:
Measured by its ability to inhibit CD3-induced proliferation of stimulated human T cells. The ED50 for this effect is typically 0.3-1.8ug/ml
Endotoxin: ~1EU/1ug (LAL)
Storage and Stability:
Lyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Aliquot to avoid repeated freezing and thawing. Store at -20 degrees C. Reconstituted product is stable for 3 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
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