Human CD300a/LMIR1 Antibody Summary
Accession # Q9UGN4
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of Human CD300a/LMIR1 by Western Blot. Western blot shows lysates of human spleen tissue and human granulocytes. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human CD300a/LMIR1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF2640) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for CD300a/LMIR1 at approximately 55-60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
CD300a, also known as LMIR1 (in rodents), 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 crosslinking 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). Crosslinking 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 crosslinking also limits the in vivo activities of these cells with a subsequent reduction of allergic inflammation symptoms (4, 11, 12).
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