CD200 R1 / CRTR2 Recombinant Protein Cat. No.: 11-121

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psi-iconSpecifications
SPECIES:Human
SOURCE SPECIES:HEK293 cells
SEQUENCE:Ala 27 - Leu 266
FUSION TAG:His Tag
TESTED APPLICATIONS:ELISA, WB
APPLICATIONS:This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 28.7 kDa. The protein migrates as 48-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
psi-iconProperties
PURITY:>90% as determined by SDS-PAGE.
PREDICTED MOLECULAR WEIGHT:28.7 kDa
PHYSICAL STATE:Lyophilized
BUFFER:PBS, pH7.4
STORAGE CONDITIONS:Lyophilized Protein should be stored at -20˚C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20˚C or -70˚C. Avoid repeated freeze-thaw cycles.
psi-iconAdditional Info
ALTERNATE NAMES:CD200R,CRTR2,MOX2R,OX2R
ACCESSION NO.:AAQ19772.1
OFFICIAL SYMBOL:CD200R1
GENE ID:131450
psi-iconBackground and References
BACKGROUND:Cell surface glycoprotein CD200 receptor 1 is a protein that in humans is encoded by the CD200R1 gene. This gene encodes a receptor for the OX-2 membrane glycoprotein. Both the receptor and substrate are cell surface glycoproteins containing two immunoglobulin-like domains. This receptor is restricted to the surfaces of myeloid lineage cells and the receptor-substrate interaction may function as a myeloid downregulatory signal. CD200 and its receptor CD200R are both type-1 membrane glycoproteins, which are members of the immunoglobulin superfamily (IgSF). Besides the inhibitory effect on macrophages, CD200/CD200R also play an important role in regulating the regulatory T cells, allergicreaction, autoimmune diseases, allograft, neurological diseases and other autoimmune-related diseases. The interaction between CD200, which is mainly present in neurons but also in astrocytes, and CD200R1, which is mainly present in microglia, is one of the mechanisms involved in keeping the microglial proinflammatory phenotype under control in physiological conditions. Alterations in the expression of CD200 and CD200R1 have been described in neurodegenerative diseases, but little is known about the mechanism of regulation of these proteins under physiological or pathological conditions.

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