抗Human Langerin/CD207 Phycoerythrin抗体(Anti-Human Langerin/CD207 Phycoerythrin antibody)

• 価格
• Product Details
• Applications and Data
• Related Product & Information
• Citations

価格

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Product Details

Species Reactivity	Human
Label	Phycoerythrin
Immunogen	Mouse myeloma cell line NS0-derived recombinant human Langerin/CD207Tyr64-Pro328Accession # Q9UJ71
Source	Monoclonal Mouse IgG1 Clone # 343828
Purification	Protein A or G purified from hybridoma culture supernatant
Specificity	Detects human Langerin/CD207 in direct ELISAs and Western blots.

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Applications and Data

	Recommended Concentration	Sample
Flow Cytometry	10 µL/106 cells	See below

Flow Cytometry

Detection of Langerin/CD207 in Human Monocyte-derived Langerhans Dendritic Cells by Flow Cytometry. Human monocyte-derived Langerhans dendritic cells were treated with 20 ng/mL Recombinant Human IL‑4 (Catalog # 204-IL) and 50 ng/mL Recombinant Human GM‑CSF (Catalog # 215-GM) for 6‑7 days and then stained stained with Mouse Anti-Human Langerin/CD207 PE‑conjugated Monoclonal Antibody (Catalog # FAB2088P, filled histogram) or isotype control antibody (Catalog # IC002P, open histogram). View our protocol for Staining Membrane-associated Proteins.

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Related Product & Information

Background

Langerin/CD207

background_content

Background: Langerin/CD207 Langerin (also known as CD207) is a type II transmembrane glycoprotein which is member K of the C-type lectin domain family 4 (1). 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). The 328 amino acid (aa) human langerin sequence contains a 43 aa cytoplasmic domain, a 21 aa transmembrane domain and a 264 aa extracellular domain (ECD) that contains a coiled-coil domain and a single C-type lectin domain. 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 Mycobacterium 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). Human langerin shares 68%, 62%, 71% aa identity with mouse, rat and bovine langerin ECD, respectively.

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Citations

1. Severe dermatitis with loss of epidermal Langerhans cells in human and mouse zinc deficiency.
   Authors: Kawamura T, Ogawa Y, Nakamura Y
   J. Clin. Invest., 2012;122(2):722-32.
   Species: Human
   Sample Type: Whole Tissue
   Application: IHC Frozen


2. Transcutaneous immunization as preventative and therapeutic regimens to protect against experimental otitis media due to nontypeable Haemophilus influenzae.
   Authors: Novotny LA, Clements JD, Bakaletz LO
   Mucosal Immunol, 2011;4(4):456-67.
   Species: Chinchilla
   Sample Type: Whole Cells
   Application: Flow

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