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Human DC-SIGN / CD209 Protein (Fc Tag)

CD209,CDSIGN,CLEC4L,DC-SIGN,DC-SIGN1,MGC129965

Catalog Number P10200-H01H
Organism Species Human
Host Human Cells
Synonyms CD209,CDSIGN,CLEC4L,DC-SIGN,DC-SIGN1,MGC129965
Molecular Weight The recombinant human Fc/DC-SIGN chimera is a disulfide-linked homodimeric protein. The reduced monomer consists of 580 amino acids and has a calculated molecular mass of 65.8 kDa. As a result of glycosylation, the apparent molecular mass of rh Fc/DC-SIGN is approximately 75 kDa in SDS-PAGE under reducing conditions.
predicted N Glu 20
SDS-PAGE
Purity > 97 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the N-terminally truncated extracellular domain (Lys 62-Ala 404) of human DC-SIGN (NP_066978.1) was expressed with the fused Fc region of human IgG1 at the N-terminus.
Bio-activity
Research Area Cancer |Invasion microenvironment |Adhesion molecule |Cell adhesion |Lectin |C-tyep lectin |
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Dendritic cell (DC)-specific intercellular adhesion molecule 3 (ICAM-3) grabbing nonintegrin (DC-SIGN), also known as CD209, is a type II transmembrane protein on DCs with a C-type lectin extracellular domain, is capable of binding ICAM-3 on resting T cells in the secondary lymphoid organs, providing the initial contact between these cells during the establishment of cell-mediated immunity. It is not only a pattern recognition receptor but implicated in immunoregulation of DCs. It has important role in mediating DC adhesion, migration, inflammation, activating primary T cell, triggering immune response and participating in immune escape of pathogens and tumors. DC-SIGN also mediates capture and internalization of viral, bacterial, and fungal pathogens by dendritic cells, such as HIV-1, Ebola virus, cytomegalovirus, Dengue virus, and hepatitis C virus. DC-SIGN is unique in that it regulates adhesion processes, such as DC trafficking and T-cell synapse formation, as well as antigen capture. Moreover, even though several C-type lectins have been shown to bind HIV-1, DC-SIGN does not only capture HIV-1 but also protects it in early endosomes allowing HIV-1 transport by DC to lymphoid tissues, where it enhances trans infection of T cells.
Reference
  • Geijtenbeek TB, et al. (2002) DC-SIGN, a C-type lectin on dendritic cells that unveils many aspects of dendritic cell biology. J Leukoc Biol. 71(6): 921-31.
  • Masso M. (2003) DC-SIGN points the way to a novel mechanism for HIV-1 transmission. MedGenMed. 5(2): 2.
  • Zhou T, et al. (2006) DC-SIGN and immunoregulation. Cell Mol Immunol. 3(4): 279-83.