Recombinant Human CD200R1 Avi-tag His-tag Protein, CF
Recombinant Human CD200R1 Avi-tag His-tag Protein, CF SummaryLearn more about Avi-tag Biotinylated Proteins
Accession # NP_620161.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 250 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human CD200 Fc Chimera (2724-CD) is immobilized at 0.25 µg/mL (100 µL/well), Biotinylated Recombinant Human CD200R1 Avi-tag His-tag Protein (Catalog # AVI10053) binds with an ED50 of 0.150-1.80 μg/mL.
2 μg/lane of Recombinant Human CD200R1 Avi-tag His-tag Protein (Catalog # AVI10053) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 55-65 kDa.
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). Our Avi-tag Biotinylated human CD200 R1 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.
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