Recombinant Human Ficolin-1 Protein, CF Summary
Product Specifications
Gln28-Ala326, 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.
4209-FC
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and NaCl. |
| Reconstitution | Reconstitute at 100 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.
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Reconstitution Calculator
Background: Ficolin-1
Human Ficolin-1 (fibrinogen/collagen-like), also called M-ficolin, is a member of the ficolin family of secreted pattern recognition proteins in the lectin complement activation pathway (1 - 3). Ficolin-1 is expressed by monocytes, neutrophils and type II alveolar epithelial cells (2 - 5). It is proposed to be a locally-acting lectin released in a regulated manner (4). Ficolin-1 is not found in plasma, but is detected on the surface of circulating monocytes (4 - 6). The 35 kDa, 326 amino acid (aa) human Ficolin-1 contains a 28 aa signal sequence, an N-terminal collagen domain and a C-terminal fibrinogen-like (FBG) domain that includes a calcium binding site and one potential N-glycosylation site. Both the collagen and FBG domains mediate trimer formation (7). Like Ficolin-2, larger homo-multimers of Ficolin-1 exist and are likely formed by disulfide bonds at the N-terminus. Sizes corresponding to 12 or 18 subunit oligomers are reported (4, 6, 7). The FBG domain of Ficolin-1 binds microbial ligands that contain acetylated compounds (6). Ligands identified include N-acetyl glucosamine, N-acetyl galactosamine and sialyl-N-acetyllactosamine (4 - 7). Like other ficolins, Ficolin-1 associates with, and activates the MBL-associated serine protease (MASP) complex, which activates the complement pathway by cleaving C4, contributing to the innate immune response (4 - 6). Mature human Ficolin-1 shares 76%, 61%, 61%, 76% and 81% aa identity with mouse Ficolin-2 (8), and mouse, rat, canine and porcine Ficolin-1, respectively. It shares 84% and 46% aa identity with human Ficolin-2 and Ficolin-3, respectively. The Ficolin-1 gene is polymorphic, showing at least ten single nucleotide polymorphisms in the promoter and coding regions (1).
- Endo, Y. et al. (2006) Adv. Exp. Med. Biol. 586:265.
- Endo, Y. et al. (1996) Genomics 36:515.
- Lu, J. et al. (1996) Biochem. J. 313: 473.
- Liu, Y. et al. (2005) J. Immunol. 175:3150.
- Teh, C. et al. (2000) Immunology 101:225.
- Frederiksen, P. D. et al. (2005) Scand. J. Immunol. 62:462.
- Tanio, M. et al. (2007) J. Biol. Chem. 282:3889.
- Endo, Y. et al. (2004) Genomics 84:737.
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