Recombinant Human Ficolin-3 Protein, CF Summary
Product Specifications
Lys22-Arg299, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
2367-FC
| Formulation | Supplied as a 0.2 μm filtered solution in PBS and NaCl. |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
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Background: Ficolin-3
Human Ficolin-3 (fibrinogen/collagen-like), also called H-ficolin and, previously, Hakata antigen or thermolabile beta -2 macroglycoprotein, is a member of the ficolin family of secreted pattern recognition proteins that belong to the lectin complement activation pathway (1, 2). Ficolin-3 is expressed by bile duct epithelial cells and hepatocytes, and is released into the bile and circulation, where it averages 18 μg/mL (3, 4). It is also secreted by bronchial and alveolar epithelial cells in the lung (3). Mature human Ficolin-3 shares 46% and 52% amino acid (aa) identity with human Ficolin-1 and Ficolin-2, respectively. Ficolin-3 has only been identified in primates and is likely a pseudogene in other species (5). The 35 kDa, 288 aa human Ficolin-3 (isoform 2) contains a signal sequence, an N-terminal collagen domain and a C-terminal fibrinogen-like domain that includes a calcium binding site and two potential N-glycosylation sites. Isoform 1 contains an additional 11 aa between the collagen and fibrinogen-like domains. The collagen domain mediates trimer formation, and a ~650 kDa, 18 subunit oligomer is formed by disulfide links at the N-terminus (2, 6, 7). Ficolin-3 binds a limited set of carbohydrates containing mannose, galactose or D-fucose (2, 6). Binding of microbial carbohydrates has been clearly demonstrated only for the PSA antigen of Aerococcus viridans (4, 8, 9). Pathogen recognition initiates an immune response involving the calcium-dependent interaction of Ficolin-3 with the MBL-associated serine protease (MASP) complex. This cleaves C4 to activate the complement pathway (4, 9). In a secondary role, Ficolins 2 and 3 bind apoptotic cells, activating complement cascades that assist in clearance of the cells (10). Circulating antibodies to Ficolin-3 have been identified in systemic lupus erythematosus (7).
- Endo, Y. et al. (2006) Adv. Exp. Med. Biol. 586:265.
- Sugimoto, R. et al. (1998) J. Biol. Chem. 273:20721.
- Akaiwa, M. et al. (1999) J. Histochem. Cytochem. 47:777.
- Krarup, A. et al. (2005) Inf. Immun. 72:1052.
- Endo, Y. et al. (2004) Genomics 84:737.
- Garlatti, V. et al. (2007) EMBO J. 26:623.
- Yae, Y. et al. (1991) Biochim. Biophys. Acta 1078:369.
- Tsujimura, M. et al. (2001) Clin. Diag. Lab. Immunol. 8:454.
- Matsushita, M. et al. (2002) J. Immunol. 168:3502.
- Kuraya, M. et al. (2005) Immunobiology 209:689.
Citations for Recombinant Human Ficolin-3 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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FCN3 functions as a tumor suppressor of lung adenocarcinoma through induction of endoplasmic reticulum stress
Authors: H Jang, Y Jun, S Kim, E Kim, Y Jung, BJ Park, J Lee, J Kim, S Lee, J Kim
Cell Death & Disease, 2021-04-15;12(4):407.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense
Authors: D Wolf, N Anto-Miche, H Blankenbac, A Wiedemann, K Buscher, JD Hohmann, B Lim, M Bäuml, A Marki, M Mauler, D Duerschmie, Z Fan, H Winkels, D Sidler, P Diehl, DM Zajonc, I Hilgendorf, P Stachon, T Marchini, F Willecke, M Schell, B Sommer, C von Zur Mu, J Reinöhl, T Gerhardt, EF Plow, V Yakubenko, P Libby, C Bode, K Ley, K Peter, A Zirlik
Nat Commun, 2018-02-06;9(1):525.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins
Authors: Aleksandra Man-Kupisi
PLoS ONE, 2016-05-27;11(5):e0156691.
Species: Human
Sample Types: Plasma
Applications: ELISA (Standard) -
Ficolin-3 activity towards the opportunistic pathogen, Hafnia alvei.
Authors: Michalski M, St Swierzko A, Lukasiewicz J, Man-Kupisinska A, Karwaciak I, Przygodzka P, Cedzynski M
Immunobiology, 2014-08-19;220(1):117-23.
Species: Bacteria, Human
Sample Types: Whole Cells
Applications: Bioassay -
New functional ligands for ficolin-3 among lipopolysaccharides of Hafnia alvei.
Authors: Swierzko A, Lukasiewicz J, Cedzynski M
Glycobiology, 2011-09-02;22(2):267-80.
Species: Bacteria
Sample Types: Whole Cells
Applications: Binding Assay
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