Recombinant Human Langerin/CD207 Fc Chimera Protein, CF

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 kDa.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human Langerin/CD207 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human Langerin/CD207 Fc Chimera (Catalog # 10401-LN) is immobilized at 0.2 µg/mL (100 µL/well), Biotinylated Mannose-Polyacrylamide binds with an ED₅₀ of 20-160 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human Langerin/CD207 protein
  

  MD	Human IgG1 (Pro100-Lys330)	IEGR	Human Langerin/CD207 (Pro65-Pro328) Accession # Q9UJ71.2
  N-terminus			C-terminus

• Accession #: Q9UJ71.2
• N-terminal Sequence: Met
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 56 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 58-71 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS and NaCl with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Langerin/CD207 Fc Chimera Protein, CF

• CD207 antigen
• CD207 antigen, langerin
• CD207 molecule, langerin
• CD207
• CLEC4KLangerhans cell specific c-type lectin
• C-type lectin domain family 4 member K
• C-type lectin domain family 4, member K
• Langerin

Background

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).

1. Valladeau, J. et al. (2000) Immunity 12:71.
2. Valladeau, J. et al. (2003) Immunol. Res. 28:93.
3. McDermott, R. et al. (2002) Mol. Biol. Cell 13:317.
4. Stambach, N. S. and M. E. Taylor (2003) Glycobiology 13:401.
5. Tada, Y. et al. (2006) J. Invest. Dermatol. 126:1549.
6. Ritter, U. and A. Osterloh (2007) Med. Microbiol. Immunol. 196:51.
7. Takahara, K. et al. (2003) Int. Immunol. 16:819.
8. Hunger, R. E. et al. (2004) J. Clin. Invest. 113:701.
9. De Witte, L. et al. (2007) Nat. Med. 13:367.
10. Verdijk, P. et al. (2005) J. Invest. Dermatol. 124:714.
11. Ward, E. M. et al. (2006) J. Biol. Chem. 281:15450.
12. Kissenpfennig, A. et al. (2005) Mol. Cell. Biol. 25:88.

Bioinformatics

• Uniprot:
  • Q9UJ71.2()