Recombinant Human Langerin/CD207 Fc Chimera Protein, CF Summary
Accession # Q9UJ71.2
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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 and NaCl with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in 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.
When Recombinant Human Langerin/CD207 Fc Chimera (10401-LN) is immobilized at 0.2 μg/mL (100 μL/well), Biotinylated Mannose-Polyacrylamide binds with an ED50 of 20-160 ng/mL.
2 μg/lane of Recombinant Human Langerin/CD207 Fc Chimera (Catalog # 10401-LN) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 58-71 kDa and 116-142 kDa, respectively.
Langerin (also known as CD207) is a transmembrane glycoprotein within the type II C-Type lectin receptor family and has been identified as a pathogen binding receptor for immune regulation (1). Human langerin consists of an extracellular domain (ECD) containing a coiled-coil domain and a single C-type lectin domain, a transmembrane domain and a short cytoplasmic domain with a proline-rich motif. The mature ECD of human langerin shares 68%, 62%, 71% amino acid identity with mouse, rat and bovine langerin ECD, respectively. Langerin is used as a marker for Langerhans cells (LCs) which represent the immature dendritic cells in the epidermis (1, 2). LCs uniquely contain "tennis racket"-shaped endosomal recycling compartment subdomains with pentalamellar membranes termed Birbeck granules (1-3). Langerin is necessary and sufficient for Birbeck granule formation (1). Trimerization greatly increases the lectin binding affinity (4). Langerin internalizes endogenous proteins such as type I procollagen. Internalization by LC is thought to lead to suppression of self-reactions (4-6). Langerin also mediates endocytosis of non-peptide antigens containing mannose, N-acetyl glucosamine and fucose that are expressed by mycobacteria and fungae (4, 7). Some antigens, such as the M. leprae glycolipid arabinomycolate, are ultimately presented by human LC CD1a in cutaneous-draining lymph nodes (8). Langerin performs a barrier-like function to HIV-1 transmission due to its internalization of virus particles for destruction (9). A rare human polymorphism within the lectin domain, W264R, abolishes both carbohydrate recognition and Birbeck granule formation (10, 11). Genetic deletion of mouse langerin was not shown to have functional consequence other than abolishing Birbeck granule formation (12).
- Valladeau, J. et al. (2000) Immunity 12:71.
- Valladeau, J. et al. (2003) Immunol. Res. 28:93.
- McDermott, R. et al. (2002) Mol. Biol. Cell 13:317.
- Stambach, N. S. and M. E. Taylor (2003) Glycobiology 13:401.
- Tada, Y. et al. (2006) J. Invest. Dermatol. 126:1549.
- Ritter, U. and A. Osterloh (2007) Med. Microbiol. Immunol. 196:51.
- Takahara, K. et al. (2003) Int. Immunol. 16:819.
- Hunger, R. E. et al. (2004) J. Clin. Invest. 113:701.
- De Witte, L. et al. (2007) Nat. Med. 13:367.
- Verdijk, P. et al. (2005) J. Invest. Dermatol. 124:714.
- Ward, E. M. et al. (2006) J. Biol. Chem. 281:15450.
- Kissenpfennig, A. et al. (2005) Mol. Cell. Biol. 25:88.
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