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C2548-96W9 Mouse Anti-CD200R1 (Cell Surface Glycoprotein CD200 Receptor 1, CD200 Cell Surface Glycoprotein Receptor, Cell Surface Glycoprotein OX2 Receptor 1, CD200R, CRTR2, MOX2R, OX2R, UNQ2522/PRO6015) (Carboxyfluorescein)

Specifications
Clone Type
Monoclonal
Host
Mouse
Source
Human
Conjugate
Carboxyfluorescein
Isotype
IgG2b
Clone Number
11C4
Grade
Affinity Purified
Applications
FC
Crossreactivity
Hu
Accession #
NP_620161
Shipping Temp
Blue Ice
Storage Temp
-20°C

CD200 R1, also known as OX-2 receptor, is one of four CD200 R-related proteins within the immunoglobulin superfamily. CD200 R1 is a type I transmembrane protein with a PTB-signaling motif in its cytoplasmic domain. Engagement of CD200 R1 by CD200 elicits an inhibitory signal in mast cells, basophils, macrophages, and dendritic cells. 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. Within the ECD, human CD200 R1 shares 56% aa sequence identity with mouse and rat CD200 R1.

Applications
Suitable for use in Flow Cytometry. Other applications not tested.
Recommended Dilutions
Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Carboxyfluorescein conjugates are sensitive to light. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
NS0-derived, recombinant human CD200 R1 (rhCD200 R1; Ala27-Leu266 (predicted): Accession # NP_620161).
Form
Supplied as a liquid in saline, 0.5% BSA, 0.09% sodium azide. Labeled with Carboxyfluorescein.
Purity
Purified by Protein A affinity chromatography from hybridoma culture supernatant.
Specificity
Recognizes human CD200 R1. No cross-reactivity with recombinant mouse CD200 R1.
Conjugates
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