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CLEC4G encodes a glycan-binding receptor and member of the C-type lectin family which plays a role in the T-cell immune response. Additionally we are shipping CLEC4G Proteins (6) and CLEC4G Kits (1) and many more products for this protein.
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In this study, there was experimentally identified the cDNA and the gene encoding porcine CLEC4G.
Japanese encephalitis virus infected cells through three virus receptors: DC-SIGN (show CD209 Antibodies), DC-SIGNR (show CLEC4M Antibodies) and LSECtin.
The results indicate that LSECtin plays an important role in colorectal carcinoma liver metastasis and may be a promising new target for intervention in metastasis formation.
The mobility of LSECtin-carbohydrate recognition domain increased after addition of Ca(2 (show CA2 Antibodies)+) and N-acetylglucosamine.
Axl (show AXL Antibodies),Tyro3 (show TYRO3 Antibodies),DC-SIGN (show CD209 Antibodies) and LSECtin are identified as new virus receptors for Lassa virus cell entry.
The human LSECtin have been shown to bind Ebola virus glycoprotein with equivalent affinities, and the GlcNAcbeta1-2Man disaccharide has been demonstrated to be an effective inhibitor of this interaction.
The interaction between CD44 (show CD44 Antibodies) & LSECtin is dependent on protein-glycan recognition. CD44 (show CD44 Antibodies) is the 1st identified endogenous ligand of LSECtin, & similarly, LSECtin is a novel ligand of CD44 (show CD44 Antibodies).
results indicate that LSECtin is a novel member of a family of proteins comprising CD23, DC-SIGN, and DC-SIGNR and might function in vivo as a lectin receptor
LSECtin is a pathogen-associated molecular pattern receptor in human myeloid cells; results suggest that LSECtin participates in antigen uptake and internalization
Our results reveal important differences between Ebola virus and HIV-1 capture by DC-SIGN (show CD209 Antibodies)/R and LSECtin and hint towards different biological functions of these lectins.
LSECtin is expressed by liver myeloid cells, and its expression is dependent on the PU.1 transcription factor.
This study shows that C-type lectin LSECtin, a member of the DC-SIGN (show CD209 Antibodies) family, is a novel liver regulator for natural killer cells (NK cells). LSECtin could bind to NK cells in a carbohydrate-dependent manner and could regulate the number of hepatic NK cells.
Data show that C-type lectin-like domain family 4, member g (Clec4g) suppresses beta-Site amyloid precursor protein cleaving enzyme-1 (BACE1 (show BACE Antibodies))-mediated amyloid-beta (Abeta (show APP Antibodies)) peptides generation.
When expressed in B16 melanoma cells, LSECtin promoted tumor growth, whereas its blockade slowed tumor growth in either wild-type or LSECtin-deficient mice.
LSECtin-mediated signaling up-regulates the threshold of CD4(+) T cell activation via tuning the expression of Cbl-b.
LSECtin may facilitate the reduction of liver inflammation at the cost of delaying virus clearance, an effect that might be hijacked by the virus as an escape mechanism.
The studies provide a basis for using mouse LSECtin, and knockout mice lacking this receptor, to model the biological properties of the human receptor.
Liver sinusoidal endothelial cell lectin, LSECtin, negatively regulates hepatic T-cell immune response.
This gene encodes a glycan-binding receptor and member of the C-type lectin family which plays a role in the T-cell immune response. Multiple transcript variants encoding different isoforms have been found for this gene.
C-type lectin domain family 4, member G
, C-type lectin superfamily 4, member G
, C-type lectin domain family 4 member G
, DC-SIGN related C-type lectin
, liver and lymph node sinusoidal endothelial cell C-type lectin