Human DC-SIGN/CD209 (Fc Tag) recombinant protein

Human DC-SIGN/CD209 (Fc Tag) recombinant protein

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• Material Safety Data Sheets (MSDS)

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.

cDNA, FLJ94149, highly similar to Homo sapiens CD209 antigen (CD209)

DCSIGN; DC-SIGN1; CIRE; CLEC4L; SIGNR5; CD209; CDSIGN; SIGN-R1; MGC130443; MGC129965; DC-SIGN; CD209A

Q9NNX6

Human Cells

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.

Human

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.

> 97 % as determined by SDS-PAGE