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OX-2 Membrane Glycoprotein; MOX2

Protein

CHO cells

The extracellular domain of mouse CD200 (aa 31-236) is fused to the N-terminus of the Fc region of a mutant mouse IgG2a.

Mouse

Shows the biological function of the CD200 moiety and exerts a prolonged circulating half-life caused by the modified Fc domain.

≥98% (SDS-PAGE)

Reconstitute at 100μg/ml in sterile PBS.

Lyophilized from 0.2μm-filtered solution in PBS.

Non-lytic: Acts as a long lasting fusion protein which only binds to the receptor. Mutations to the complement (C1q) and FcgR I binding sites of the IgGs Fc fragment render the fusion proteins incapable of antibody directed cytotoxicity (ADCC) and complement directed cytotoxicity (CDC).NCBI reference NP_034948.3: CD200 (mouse)

Manufactured by Chimerigen.

BLUE ICE

+4°C

-20°C

Avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -20°C.Working aliquots are stable for up to 3 months when stored at -20°C.

No

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CD200, also known as OX-2, is a 45 kDa transmembrane immunoregulatory protein that belongs to the immunoglobulin superfamily. CD200 is widely but not ubiquitously expressed. Its receptor (CD200R) is restricted primarily to mast cells, basophils, macrophages, and dendritic cells, which suggests myeloid cell regulation as the major function of CD200. CD200 knockout mice are characterized by increased macrophage number and activation and are predisposed to autoimmune disorders. In T cells, CD200 functions as a costimulatory molecule independent of the CD28 pathway. Several viruses encode CD200 homologs which are expressed on infected cells during the lytic phase. Like CD200 itself, viral CD200 homologs also suppress myeloid cell activity, enabling increased viral propagation.