Detection of CD200 R1 in MC/9‑2 Mouse Cell Line by Flow Cytometry.
MC/9‑2 mouse mast cell line was stained with Goat Anti-Mouse CD200 R1 APC‑conjugated Antigen Affinity-purified Polyclonal Antibody (Catalog # FAB2554A, filled histogram) or isotype control antibody (Catalog # IC108A, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: CD200 R1
CD200 R1, also known as OX-2 receptor, is a 90 kDa, type I transmembrane protein that belongs to the immunoglobulin superfamily. CD200 R1 is important in the regulation of myeloid cell activity (1‑3). The mouse CD200 R1 cDNA encodes a 326 aa precursor that includes a 25 aa signal sequence, a 213 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 67 aa cytoplasmic domain. The ECD is composed of one Ig-like V-type domain and one Ig-like C2-type domain (4). Within the ECD, mouse CD200 R1 shares 56% and 70% aa sequence identity with human and rat CD200 R1, respectively. The ECD of mouse CD200 R1 shares 69%, 38%, 79%, and 83% aa sequence identity with the ECD of CD200 R2, 3, 4, and a CD200 R-like molecule, respectively. CD200 R1 is expressed primarily on mast cells, basophils, macrophages, and dendritic cells, (5‑7) while its ligand, CD200, is widely distributed (8). Disruption of this receptor-ligand pair by knockout of the CD200 gene leads to increased macrophage number and activation, plus a predisposition to autoimmune disorders (9). Association of CD200 with CD200 R1 takes place between their respective N-terminal Ig-like domains (10). The CD200 R-like molecules may interact differently with CD200 (11, 12). The cytoplasmic domain of CD200 R1 contains two non-ITIM tyrosine residues which are required for propagating its inhibitory signals (13‑15). CD200 R-like molecules, in contrast, are potentially activating receptors by means of their association with DAP12 (4, 16).
Rosenblum, M.D. et al. (2006) J. Dermatol. Sci. 41:165.
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