Recombinant Human CD200 His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
The biotin to protein ratio is greater than 0.7 as determined by the HABA assay. Measured by its binding ability in a functional ELISA. When Recombinant Human CD200R1 Fc Chimera
(Catalog #
3414-CD) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human CD200 His-tag
Avi-tag (Catalog # AVI10032) binds with an ED 50 of 0.1-0.6 μg/mL.
|
Source |
Human embryonic kidney cell, HEK293-derived human CD200 protein Human CD200 (Gln31-Lys232) Accession # AAH22522.1 | HHHHHH | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln31 inferred from enzymatic pyroglutamate treatment revealing Val32. |
Structure / Form |
Biotinylated via Avi-tag |
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 |
26 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 |
40-50 kDa, under 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 with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 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 CD200 His-tag Avi-tag Protein, CF
Background
Cluster
of Differentiation-200 (CD200), also known as OX-2, is a transmembrane
immunoregulatory protein that belongs to the immunoglobulin superfamily (1, 2).
Mature human CD200 consists of an extracellular domain (ECD) with one Ig-like
V-type domain and one Ig-like C2-type domain, a transmembrane segment, and a
short cytoplasmic domain (3). Within the mature ECD, human CD200 shares 76% amin
acid (aa) sequence identity with mouse and rat CD200. A splice variant of CD200
has been identified lacking the first 43 aa of the ECD and characterized as a
functional antagonist to full-length CD200 (4). CD200 is widely expressed by
numerous cell types including neurons, B cells, activated T cells, thymocytes,
dendritic cells and endothelium (5). Its receptor, CD200R, is restricted
primarily to mast cells, basophils, macrophages, and dendritic cells, which
suggests CD200 is an important inhibitory ligand for myeloid cell regulation (6-8). CD200 knockout mice are characterized by increased macrophage number and
activation and are predisposed to autoimmune disorders (9). CD200 and CD200R
associate via their respective N-terminal Ig-like domains (10). In myeloid
cells, CD200R initiates inhibitory signals following receptor-ligand contact (7,
8, 11). In T cells, however, CD200 functions as a costimulatory molecule
independent of the CD28 pathway (12). Several additional CD200R-like molecules
have been identified in human and mouse, but their capacity to interact with
CD200 is controversial (13, 14). Several viruses encode CD200 homologs which
are expressed on infected cells during the lytic phase (15, 16). Like CD200
itself, viral CD200 homologs also suppress myeloid cell activity, enabling
increased viral propagation (6, 15-17). Our Avi-tag Biotinylated human CD200 features
biotinylation at a single site contained within the Avi-tag, a unique 15 amino
acid peptide. Protein orientation will be uniform when bound to
streptavidin-coated surface due to the precise control of biotinylation and the
rest of the protein is unchanged so there is no interference in the protein's
bioactivity.
- Gorczynski, R.M. (2005) Curr. Opin. Invest. Drugs 6:483.
- Barclay, A.N. et al. (2002) Trends Immunol. 23:285.
- McCaughan, G.W. et al. (1987) Immunogenetics 25:329.
- Chen, Z. et al. (2008) Transplantation. 86:1116
- Wright, G.J. et al. (2001) Immunology 102:173.
- 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.
- Hoek, R.M. et al. (2000) Science 290:1768.
- Hatherley, D. and A.N. Barclay (2004) Eur. J. Immunol. 34:1688.
- Jenmalm, M.C. et al. (2006) J. Immunol. 176:191.
- Borriello, F. et al. (1997) J. Immunol. 158:4548.
- Gorczynski, R. et al. (2004) J. Immunol. 172:7744.
- Hatherley, D. et al. (2005) J. Immunol. 175:2469.
- Foster-Cuevas, M. et al. (2004) J. Virol. 78:7667.
- Cameron, C.M. et al. (2005) J. Virol. 79:6052.
- Langlais, C.L. et al. (2006) J. Virol. 80:3098.
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