Recombinant Human Ficolin-2 Protein, CF Summary
Leu26-Ala313, with a C-terminal 10-His tag
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.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 500 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Human Ficolin-2 (fibrinogen/collagen-like; previously called L-ficolin or ficolin-B) is a member of the ficolin family of secreted pattern recognition proteins that participate in the lectin complement activation pathway (1 - 4). Ficolin-2 is expressed in the liver and released into the circulation (2). The 35 - 40 kDa, 313 amino acid (aa) human Ficolin-2 contains a 25 aa 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. The collagen domain mediates trimer formation. Larger homo-multimers are formed by disulfide links at the N-terminus, the most prominent of which is a 12 subunit oligomer (3, 5). Ficolin-2 binds microbial ligands that contain acetylated compounds (6). Notably, this includes N-acetyl glucosamine in compounds such as lipoteichoic acid in gram-positive bacteria. It also binds fungal 1,3-beta -D-glucan (4, 7, 8). Pathogen recognition by Ficolin-2 initiates an immune response that involves calcium-dependent interaction of Ficolin-2 with the MBL-associated serine protease (MASP) complex. This complex cleaves C4 to activate the complement pathway (4, 7, 8). In a secondary role, Ficolin-2 is known to bind late apoptotic and necrotic cells, probably through the recognition of exposed DNA. This also activates the complement cascade that assists in clearance of cells (9, 10). Mature human Ficolin-2 shares 70%, 72%, 76% and 78% aa identity with mouse, rat, cow and pig Ficolin-2, respectively. It shares 84% and 52% aa identity with human ficolin-1 and ficolin-3, respectively. Single nucleotide polymorphisms are common in human Ficolin-2. Some affect serum concentration, while others can increase or decrease ligand binding (11).
- Endo, Y. et al. (2006) Adv. Exp. Med. Biol. 586:265.
- Endo, Y. et al. (1996) Genomics 36:515.
- Matsushita, M. et al. (1996) J. Biol. Chem. 271:2448.
- Ma, Y. G. et al. (2004) J. Biol. Chem. 279:25307.
- Hummelshoj, T. et al. (2007) Mol. Immunol. 44:401.
- Krarup, A. et al. (2004) J. Biol. Chem. 279:47513.
- Garlatti, V. et al. (2007) EMBO J. 26:623.
- Lynch, N. J. et al. (2004) J. Immunol. 172:1198.
- Jensen, M. L. et al. (2007) Mol. Immunol. 44:856.
- Kuraya, M. et al. (2005) Immunobiology 209:689.
- Hummelshoj, T. et al. (2005) Hum. Mol. Genet. 14:1651.
Citation for Recombinant Human Ficolin-2 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.
1 Citation: Showing 1 - 1
Novel findings on the role of ficolins and colectins in the innate response against Leishmania braziliensis
Authors: AR Ambrosio, L Bavia, BS Borges, PM Hiraiwa, JLM Pietsch, MCVDC Ribeiro, FB Figueiredo, IJ Messias-Re
Acta Trop., 2020;212(0):105673.
Species: Parasite - Leishmania braziliensis
Sample Types: Whole Cells
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