Anti-Human CD200 Receptor Functional Grade Purified

Description: The monoclonal antibody OX108 recognizes human CD200R also known as OX2. CD200R is an inhibitory receptor with a similar structure as its ligand, CD200, yet lacks an ITIM domain typically found in inhibitory receptors. Instead the CD200R cytoplasmic domain contains a novel phosphotyrosine binding domain, NPXY, which after binding SHIP inhibits ERK, JNK and MAPK p38 pathways. In activated macrophages signaling results in inhibition of TNFα secretion. Isoforms of CD200R have been identified and are thought to play a major role in differentiation, especially in regards to tolerogenic DCs.

Expression is restricted to hematopoietic cells: myeloid cells (monocytes, macrophages, DCs, neutrophils, mast cells and basophils) and a subset of T lymphocytes as well as langerhans (LC) cells and dendritic epidermal T cells. The epitope of OX108 is thought to be near the binding site of CD200.

References: Letarte M, Voulgaraki D, Hatherley D, Foster-Cuevas M, Saunders NJ, Barclay AN. Analysis of leukocyte membrane protein interactions using protein microarrays. BMC Biochem. 2005 Mar 1;6:2. (OX108 PubMed)

Foster-Cuevas M, Wright GJ, Puklavec MJ, Brown MH, Barclay AN.Human herpesvirus 8 K14 protein mimics CD200 in down-regulating macrophage activation through CD200 receptor. J Virol. 2004 Jul;78(14):7667-76. (OX108, FC, PubMed)

Wright GJ, Cherwinski H, Foster-Cuevas M, Brooke G, Puklavec MJ, Bigler M, Song Y, Jenmalm M, Gorman D, McClanahan T, Liu MR, Brown MH, Sedgwick JD, Phillips JH, Barclay AN. Characterization of the CD200 receptor family in mice and humans and their interactions with CD200. J Immunol. 2003 Sep 15;171(6):3034-46.