Recombinant Human CD200R1 His-tag Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinan Human CD200 R1 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 2.5-15 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human CD200R1 protein Ala27-Leu266, with a C-terminal 6-His tag |
Accession # |
|
N-terminal Sequence |
Ala27 |
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 |
|
Theoretical MW |
28 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 |
43-60 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 100 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CD200R1 His-tag Protein, CF
Background
CD200
R1, also known as OX-2 receptor, is a 90 kDa transmembrane protein in the
immunoglobulin superfamily and is important in the regulation of myeloid cell
activity (1-3). The human CD200 R1 cDNA encodes a 325 amino acid (aa) precursor
that includes a 28 aa signal sequence, a 215 aa extracellular domain (ECD), a
21 aa transmembrane segment, and a 61 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, human CD200 R1 shares 56% aa sequence identity with both mouse
and rat CD200 R1. Alternate splicing of the human CD200 R1 mRNA generates four
isoforms, two of which are truncated in the Ig-C2 domain and are likely
secreted (4). In human, a separate CD200 RL gene
encodes a protein that shares 81% ECD aa identity with CD200 R1 (5). In mouse,
at least four genes for CD200 R1-like molecules have been described (5-7). CD200 R1 expression is restricted primarily
to mast cells, basophils, macrophages, and dendritic cells (8-10), while its
ligand, CD200, is widely distributed (11). 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 (12).
Association of CD200 with CD200 R1 takes place between their respective
N-terminal Ig-like domains (13). The capacity of CD200 R1-like molecules to
interact with CD200 is controversial (6, 14). CD200 R1 propagates inhibitory
signals despite lacking a cytoplasmic ITIM (immunoreceptor tyrosine-based
inhibitory motif) (9, 10, 15, 16). CD200 R1-like molecules, in contrast, are
potentially activating receptors by means of their association with DAP12 (5, 7).
CD200R1 signaling inhibits the expression of proinflammatory molecules
including TNFs, IFNs, and inducible nitric oxide synthase in response to
selected stimuli, which implicate that CD200/CD200R1 inhibitory signaling
pathway plays a prominent role in limiting inflammation in a wide range of
inflammatory diseases (17). Furthermore,
the CD200/CD200R inhibitory signaling constitutes one of the most suitable
endogenous immunoregulatory molecule candidate to restore the immune suppressive
status of the CNS altered in chronic neuroinflammatory situations (18).
- Rosenblum, M.D. et al. (2006) J. Dermatol. Sci. 41:165.
- Gorczynski, R.M. (2005) Curr. Opin. Invest. Drugs 6:483.
- Barclay, A.N. et al. (2002) Trends Immunol. 23:285.
- Vieites J.M. et al. (2003) Gene. Jun. 5; 311:99.
- Wright, G.J. et al. (2003) J. Immunol. 171:3034.
- Hatherley, D. et al. (2005) J. Immunol. 175:2469.
- Voehringer, D. et al. (2004) J. Biol. Chem. 279:54117.
- Shiratori, I. et al. (2005) J. Immunol. 175:4441.
- Cherwinski, H.M. et al. (2005) J. Immunol. 174:1348.
- Fallarino, F. et al. (2004) J. Immunol. 173:3748.
- Wright, G.J. et al. (2001) Immunology 102:173.
- Hoek, R.M. et al. (2000) Science 290:1768.
- Hatherley, D. and A.N. Barclay (2004) Eur. J. Immunol. 34:1688.
- Gorczynski, R. et al. (2004) J. Immunol. 172:7744.
- Jenmalm, M.C. et al. (2006) J. Immunol. 176:191.
- Zhang, S. et al. (2004) J. Immunol. 173:6786.
- Vaine, C.A. et al. (2014) Adv Immunol.121:191.
- Hernangómez, M. et al. (2014) Curr Pharm Des. 20:4707.
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