Human DC-SIGNR/CD299 (Fc Tag) recombinant protein

Human DC-SIGNR/CD299 (Fc Tag) recombinant protein

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C-type lectin domain family 4, member M, also known as DC-SIGNR and CLEC4M, is a type II integral membrane protein that is 77% amino acid identical to DC-SIGN, an HIV gp120-binding protein. Though the encoded gene located in the same chromosome, DC-SIGN is expressed solely on dendritic cells, while DC-SIGNR is predominantly found in liver sinusoidal endothelial cells and lymph node, as well as placental endothelium. DC-SIGNR exists as a homotetramer, and the tandem repeat domain, also called neck domain, mediates oligermerization. DC-SIGNR is ragarded as a pathogen-recognition receptor involved in peripheral immune surveillance in liver, and probably mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. DC-SIGNR appears to selectively recognize and bind many viral surface glycoproteins containing high mannose N-linked oligosaccharides in a calcium-dependent manner, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, HCV E2, and human SARS coronavirus protein S, as well as the cellular adhesion protein ICAM3. DC-SIGNR have been thought to play an important role in establishing HIV infection by enhancing trans-infection of CD4(+)T cells in the regional lymph nodes. It may affect susceptibility to HIV infection by a mechanism that is different in females and males. DC-SIGNR can bind to hepatitis C virus (HCV), and its polymorphism might affect HCV loads supporting the concept that DC-SIGNR contributes to HCV replication efficacy.

C-type lectin domain family 4 member M

HP10347; CD299; DC-SIGNR; MGC47866; MGC129964; L-SIGN; CLEC4M; DCSIGNR; LSIGN; CD209L; DC-SIGN2

Q9H2X3

CLEC4M; CD209L; CD209L1; CD299

Human Cells

A DNA sequence encoding the extracellular domain (Ser 78-Glu 399) of human DC-SIGNR (NP_055072.3) was fused with the Fc region of human IgG1 at the N-terminus.

Human

The recombinant human DC-SIGNR/Fc is a disulfide-linked homodimer after removal of the signal peptide. The reduced monomer consists of 580 amino acids and has a predicted molecular mass of 65 kDa. As a result of glycosylation, the apparent molecular mass of rhDC-SIGNR/Fc is approximately 110-140 kDa & 65-70 kDa corresponding to the homodimer and monomer respectively in SDS-PAGE under non-reduced conditions.

> 90 % as determined by SDS-PAGE