Recombinant Cynomolgus CD200R1 Fc Chimera Protein, CF

When Recombinant Cynomolgus CD200 R1 Fc Chimera (Catalog #9357-CD) is immobilized at 2 μg/mL, 100 μL/well, Recombinant Human CD200Fc Chimera Recombinant Human CD200 Fc Chimera (Catalog # 2724‑CD) binds with an ED50 of 1.5-9 ng/mL.

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

Recombinant Cynomolgus CD200R1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey CD200 R1 Fc Chimera is immobilized at 2 μg/mL, 100 μL/well, the concentration of Recombinant Human CD200 Fc Chimera (Catalog # 2724-CD) that produces 50% of the optimal binding response is 1.5-9 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived cynomolgus monkey CD200 R1 protein
  

  Human Cynomolgus Monkey CD200 R1 (Ala27-Leu267) Accession # XP_005548208	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: XP_005548208
• N-terminal Sequence: Ala27
• 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: 53 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: 85-102 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 CD200R1 Fc Chimera Protein, CF

• CD200 R1
• CD200 receptor 1
• CD200R1
• CD200RMOX2Rcell surface glycoprotein CD200 receptor 1
• Cell surface glycoprotein OX2 receptor 1
• cell surface glycoprotein receptor CD200
• CRTR2
• HCRTR2
• MOX2 receptor
• MOX2R
• OX2RCD200 cell surface glycoprotein receptor

Background

CD200 R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the immunoglobulin superfamily. CD200 R1 is important in the regulation of myeloid cell activity (1-3). The cynomolgus CD200 R1 cDNA encodes a 241 aa extracellular domain (ECD) and 61 aa cytoplasmic tail. The ECD is composed of one Ig-like V‑type domain and one Ig-like C2-type domain (4). Within the ECD, cynomolgus CD200 R1 shares 91%, 54%, and 57% aa sequence identity with human, mouse, and rat CD200 R1, respectively. At least two alternate splice isoforms exist that differ in their cytoplasmic domains. CD200 R1 expression is restricted primarily to mast cells, basophils, macrophages, and dendritic cells (5-7), while its ligand, CD200, is widely distributed (8). Disruption of this receptor-ligand system by knockout of the CD200 gene in mice leads to increased macrophage number and activation and predisposition to autoimmune disorders (9). Association of CD200 with CD200 R1 takes place between their respective N-terminal Ig-like domains (10). CD200 R1 propagates inhibitory signals despite its lacking a cytoplasmic ITIM (immunoreceptor tyrosine-based inhibitory motif) (6, 7, 11, 12).

1. Rosenblum, M.D. et al. 2006, J. Dermatol. Sci. 41:165.
2. Gorczynski, R.M. (2005) Curr. Opin. Invest. Drugs 6:483.
3. Barclay, A.N. et al. (2002) Trends Immunol. 23:285.
4. Wright, G.J. et al. (2003) J. Immunol. 171:3034.
5. Shiratori, I. et al. (2005) J. Immunol. 175:4441.
6. Cherwinski, H.M. et al. (2005) J. Immunol. 174:1348.
7. Fallarino, F. et al. (2004) J. Immunol. 173:3748.
8. Wright, G.J. et al. (2001) Immunology 102:173.
9. Hoek, R.M. et al. (2000) Science 290:1768.
10. Hatherley, D. and A.N. Barclay (2004) Eur. J. Immunol. 34:1688.
11. Jenmalm, M.C. et al. (2006) J. Immunol. 176:191.
12. Zhang, S. et al. (2004) J. Immunol. 173:6786.

Bioinformatics

• Uniprot:
  • XP_005548208()