Recombinant Cynomolgus Monkey CD200 Fc Chimera Protein, CF

• Reactivity: Pm-Cm
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Cynomolgus Monkey CD200 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human CD200 R1 Fc Chimera (Catalog # 3414-CD) is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Cynomolgus Monkey CD200 Fc Chimera that produces 50% of the optimal binding response is 5-35 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey CD200 protein
  

  Cynomolgus Monkey CD200 (Gln56-Gly257) Accession # EHH51019	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: EHH51019
• N-terminal Sequence: No results obtained. Gln56 inferred from enzymatic pyroglutamate treatment revealing Val57
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 49 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 64-73 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 1 mg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Cynomolgus Monkey CD200 Fc Chimera Protein, CF

• antigen identified by monoclonal MRC OX-2
• CD200 antigenMOX1
• CD200 molecule
• CD200
• MOX1
• MOX2
• MOX2MRC
• MRC OX-2 antigen
• MRC
• OX-2 membrane glycoprotein
• OX-2

Background

CD200, also known as OX-2, is a 45 kDa transmembrane immunoregulatory protein that belongs to the immunoglobulin superfamily. Mature cynomolgus CD200 consists of a 202 aa extracellular domain (ECD) with one Ig-like V-type domain and one Ig-like C2-type domain, a 27 aa transmembrane segment, and a 19 aa cytoplasmic domain. Within the ECD, cynomolgus CD200 shares 95%, 78%, and 78% aa sequence identity with human, mouse, and rat CD200, respectively. CD200 is widely but not ubiquitously expressed (2). Its receptor (CD200 R1) is restricted primarily to mast cells, basophils, macrophages, and dendritic cells, which suggests myeloid cell regulation as the major function of CD200 (3-5). CD200 knockout mice are characterized by increased macrophage number and activation and are predisposed to autoimmune disorders (6). CD200 and CD200 R associate via their respective N-terminal Ig-like domains (7). In myeloid cells, CD200 R initiates inhibitory signals following receptor-ligand contact (4, 5, 8). In T cells, however, CD200 functions as a costimulatory molecule independent of the CD28 pathway (9). Several additional CD200 R-like molecules have been identified in human and mouse, but their capacity to interact with CD200 is controversial (10, 11). Several viruses encode CD200 homologs which are expressed on infected cells during the lytic phase (12, 13). Like CD200 itself, viral CD200 homologs also suppress myeloid cell activity, enabling increased viral propagation (3, 12-14).

1. Vaine, C.A. and R.J. Soberman (2014) Adv. Immunol. 121:191.
2. Wright, G.J. et al. (2001) Immunology 102:173.
3. Shiratori, I. et al. (2005) J. Immunol. 175:4441.
4. Cherwinski, H.M. et al. (2005) J. Immunol. 174:1348.
5. Fallarino, F. et al. (2004) J. Immunol. 173:3748.
6. Hoek, R.M. et al. (2000) Science 290:1768.
7. Hatherley, D. and A.N. Barclay (2004) Eur. J. Immunol. 34:1688.
8. Jenmalm, M.C. et al. (2006) J. Immunol. 176:191.
9. Borriello, F. et al. (1997) J. Immunol. 158:4548.
10. Gorczynski, R. et al. (2004) J. Immunol. 172:7744.
11. Hatherley, D. et al. (2005) J. Immunol. 175:2469.
12. Foster-Cuevas, M. et al. (2004) J. Virol. 78:7667.
13. Cameron, C.M. et al. (2005) J. Virol. 79:6052.
14. Langlais, C.L. et al. (2006) J. Virol. 80:3098.

Bioinformatics

• Uniprot:
  • EHH51019()