Recombinant Human DC-SIGNR/CD299 Fc Chimera Protein, CF Summary
Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of ICAM-3 expressing CHO Chinese hamster ovary cells. When 5 x 104 cells/well are added to rhDC-SIGNR/Fc Chimera coated plates (5 µg/mL with 100 µL/well), approximately 40%-70% of added cells will adhere after 1 hour at room temperature. Optimal dilutions should be determined by each laboratory for each application.
Source
Mouse myeloma cell line, NS0-derived human DC-SIGNR/CD299 protein
MD
Human IgG1 (Pro100-Lys330)
IEGR
Human DC-SIGNR (Ser73-Glu376) Accession # NP_001138382
>80%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
61.4 kDa (monomer). 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
61-66 kDa, reducing conditions
Publications
Read Publications using 162-D2 in the following applications:
Human Dendritic Cell-specific ICAM-3 Grabbing Non-integrin (DC-SIGN)/CD209 is a member of the C-type lectin family (1). The canonical DC-SIGN/CD209 isoform is a 46 kDa, 404 amino acid (aa) type II transmembrane protein (2). The extracellular region contains a Ca2+-dependent carbohydrate-binding lectin domain (2). Multiple human DC-SIGN/CD209 splice forms exist, generating both membrane-bound and soluble forms (3). DC-SIGN/CD209 is not well conserved between mouse and human, with the extracellular domain sharing only 63% aa identity. The DC-SIGN/CD209 lectin domain binds mannose oligosaccharides on pathogens including HIV as well as self glycoproteins including ICAMs (2, 4). DC-SIGN/CD209 is expressed on dendritic cells (DC) and inflammatory macrophages and contributes to antigen presentation (5, 6).
Liu, W. et al. (2004) J. Biol. Chem. 279:18748.
Curtis, B.M. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8356.
Mummidi, S. et al. (2001) J. Biol. Chem. 276:33196.
Anthony, R.M. et al. (2008) Proc. Natl. Acad. Sci. USA 105:19571.
Geijtenbeek, T.B. et al. (2000) Cell 100:575.
Garcia-Vallejo, J.J. and Y. van Kooyk (2013) Trends Immunol. 34:482.
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