Mouse CD200R1 Biotinylated Antibody
Mouse CD200R1 Biotinylated Antibody Summary
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.
CD200R1 in Mouse Splenocytes. CD200R1 was detected in immersion fixed mouse splenocytes using Goat Anti-Mouse CD200R1 Biotinylated Antigen Affinity-purified Polyclonal Antibody (Catalog # BAF2554) at 15 µg/mL for 3 hours at room temperature. Cells were stained using the NorthernLights™ 557-conjugated Streptavidin (red; NL999) and counterstained with DAPI (blue). Specific staining was localized to cytoplasm and cell surface. Staining was performed using our protocol for Fluorescent ICC Staining of Non-adherent Cells.
Preparation and Storage
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).
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