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in northeastern Brazilian children and adolescents, FCN1 rs1071583 SNP was correlated with earlier age of type 1 diabetes mellitus (T1D) diagnosis; the SNP combination rs2989727 and rs1071583 was involved with T1D protection
Ficolin-1 could provide an alternative receptor-mediated mechanism for enhancing Ebola Virus infection, thereby contributing to viral subversion of the host innate immune system.
systemic lupus erythematosus patients with high ficolin-1 plasma levels had an increased risk of end-stage renal disease; there was no significant association between ficolin-1 and ficolin-3 (show FCN3 ELISA Kits) with lupus nephritis
Ficolin-1 was decreased in patients compared with controls measured at 6 h (median 0.13 vs 0.33 mug/ml, respectively, p < 0.0001). At 48 h, ficolin-1 was significantly higher
Data indicate differences in the plasma concentrations of collectin liver 1 (show COLEC10 ELISA Kits) and collectin (show MBL2 ELISA Kits) kidney 1 (show ZNF354A ELISA Kits), M-ficolin and H-ficol in systemic lupus erythematosus (SLE) patients compared to a group of healthy controls.
This study aims to investigate whether an association exists between the ficolins that are part of the lectin complement pathway and systemic lupus erythematosus.
the differential binding of ficolin-1 to lymphocyte subsets suggests ficolin-1 as a novel link between innate and adaptive immunity.
In patients with early rheumatoid arthritis, elevated plasma M-ficolin levels correlated with a high disease activity score at baseline and 1 year. A low M-ficolin level was the strongest predictor of remission and low disease activity.
Data show that a photodynamic therapy (PDT (show TWIST1 ELISA Kits)) dose-dependent upregulation of CRP (show CRP ELISA Kits) gene, as well as of PTX3 (show PITX3 ELISA Kits) and ficolin 1 genes in lung tumor A549 cells, and indicate critical role played by PI3K (show PIK3CA ELISA Kits)/Akt (show AKT1 ELISA Kits)/AP-1 (show FOSB ELISA Kits) pathway.
These results demonstrate that ficolin-1 and PTX3 (show PITX3 ELISA Kits) heterocomplex formation acts as a noninflammatory "find me and eat me" signal to sequester altered-host cells.
Ficolin-2 (show FCN2 ELISA Kits) induces macrophage activation, promotes M1 polarization and facilitates proliferation and antigen-specific cytotoxicity of CD8 (show CD8A ELISA Kits)(+) T cells. Ficolin-2 (show FCN2 ELISA Kits) binds to Toll-like receptor 4 (TLR4 (show TLR4 ELISA Kits)) on macrophages and DCs and promotes their antigen-presenting abilities to CD8 (show CD8A ELISA Kits)(+) T cells.
this study shows that FCN-A/2 exacerbated the inflammatory pathogenesis of inflammatory bowel disease by stimulating M1 polarization through the TLR4 (show TLR4 ELISA Kits)/MyD88 (show MYD88 ELISA Kits)/MAPK (show MAPK1 ELISA Kits)/NF-kappaB (show NFKB1 ELISA Kits) signalling pathway in macrophages
FcnA-deficient and FcnA/ficolin B double-deficient mice lack FcnA-mediated complement activation in the sera, because of absence of complexes comprising FcnA and MBL-associated serine proteases.
the binding properties of the murine serum ficolin-A towards a panel of different clinical relevant microorganisms
binds to the glycoproteins hemagglutinin (show HA ELISA Kits) and neuraminidase (show NEU ELISA Kits) and inhibits influenza A virus infection both in vitro and in vivo
Recombinant mouse ficolin A, mannose-binding lectin-A, and mannose-binding lectin-C bound to fibrinogen in a dose-dependent manner. The lectin pathway, through mannose-binding lectins, synchronized with blood coagulation.
the expression pattern of ficolin A expression was closely similar to that of mannose-binding lectin-associated serine proteases, suggesting that these molecules may function in coordination as components of the lectin complement pathway
Ficolin A protein (smapshowed a potent complement activating capacity.These results suggest that ficolin A and its variant function as recognition molecules of the lectin pathway.
A functionally relevant signal peptide of ficolin A was identified by using mass spectrometry analysis to determine the N-terminal sequence of secreted ficolin A.
The ficolin family of proteins are characterized by the presence of a leader peptide, a short N-terminal segment, followed by a collagen-like region, and a C-terminal fibrinogen-like domain. The collagen-like and the fibrinogen-like domains are also found separately in other proteins such as complement protein C1q, C-type lectins known as collectins, and tenascins. However, all these proteins recognize different targets, and are functionally distinct. Ficolin 1 encoded by FCN1 is predominantly expressed in the peripheral blood leukocytes, and has been postulated to function as a plasma protein with elastin-binding activity.
, collagen/fibrinogen domain-containing protein 1
, ficolin (collagen/fibrinogen domain-containing) 1
, ficolin B
, collagen/fibrinogen domain-containing protein 2
, ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)
, ficolin 2
, ficolin A