|Other Names||Ficolin-1, Collagen/fibrinogen domain-containing protein 1, Ficolin-A, Ficolin-alpha, M-ficolin, FCN1, FCNM|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Extracellular lectin functioning as a pattern- recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, FFAR2, inducing the secretion of interleukin-8/IL-8 (PubMed:21037097). Binds preferentially to 9-O-acetylated 2-6- linked sialic acid derivatives and to various glycans containing sialic acid engaged in a 2-3 linkage.|
|Cellular Location||Secreted. Cell membrane; Peripheral membrane protein; Extracellular side. Note=Found on the monocyte and granulocyte surface|
|Tissue Location||Peripheral blood leukocytes, monocytes and granulocytes. Also detected in spleen, lung, and thymus, may be due to the presence of tissue macrophages or trapped blood in these tissues. Not detected on lymphocytes|
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Provided below are standard protocols that you may find useful for product applications.
The ficolin family of proteins are characterized by thepresence of a leader peptide, a short N-terminal segment, followedby a collagen-like region, and a C-terminal fibrinogen-like domain.The collagen-like and the fibrinogen-like domains are also foundseparately in other proteins such as complement protein C1q, C-typelectins known as collectins, and tenascins. However, all theseproteins recognize different targets, and are functionallydistinct. Ficolin 1 encoded by FCN1 is predominantly expressed inthe peripheral blood leukocytes, and has been postulated tofunction as a plasma protein with elastin-binding activity.
Honore, C., et al. J. Leukoc. Biol. 88(1):145-158(2010)Davila, S., et al. Genes Immun. 11(3):232-238(2010)Gout, E., et al. J. Biol. Chem. 285(9):6612-6622(2010)Wittenborn, T., et al. J Innate Immun 2(2):167-180(2010)Tanio, M., et al. Mol. Immunol. 47 (2-3), 215-221 (2009) :
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