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The protein encoded by CD207 is expressed only in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. Additionally we are shipping CD207 Antibodies (116) and CD207 Kits (4) and many more products for this protein.
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Data show that Candida albicans and Candida tropicalis preferentially localized in (and persisted within) a sub- population of Peyer's patch Langerin-positive dendritic cells.
Langerin is expressed by the XCR1(+) "DC1" populat (show CD1C Proteins)ion of mice.
Langerin+ dermal dendritic cells appear to be site- and strain-specific
TLR7 (show TLR7 Proteins)-activated langerin(neg) dendritic cells trigger psoriatic plaque formation via IL-23 (show IL23A Proteins)-mediated activation of innate IL-17 (show IL17A Proteins)/IL-22 (show IL22 Proteins)-producing lymphocytes, independently of IFN-I.
model of epicutaneous ovalbumin (show OVA Proteins) sensitization inducing an inflammatory skin resembling atopic dermatitis (AD) to explore the role of CD207 in the pathogenesis of AD
Langerin-positive dendritic cells appear to be the predominant, though not exclusive, population responsible for in vivo transport of anti-DEC-205 (show LY75 Proteins) antibodies from the skin to the draining lymph nodes in steady state and inflammation.
Data demonstrated that CD207(+) CD8alpha(+) thymic DCs do not share a common origin with T cells but originate from intrathymic precursors.
The normal corneal epithelium is endowed with CD11c (show ITGAX Proteins)(+) Langerin+ cells that are LCs, whereas the stroma is endowed with a separate population of (non-LC) Langerin+ DCs.
Comparable T helper 1 (Th1 (show HAND1 Proteins)) and CD8 (show CD8A Proteins) T-cell immunity by targeting HIV gag p24 to CD8 (show CD8A Proteins) dendritic cells within antibodies to Langerin, DEC205 (show LY75 Proteins), and Clec9A (show CLEC9A Proteins).
Langerhan cells and (Langerin(+)) dermal dendritic cells thus seem to have a redundant function in regulating contact hypersensitivity
We suggest that CD207 gene polymorphisms rs13421115 and rs17718987 increase the risk of development of end-stage renal disease.
This study shows that mutations in the Langerin gene are present in the analysed populations at different genotypic and allelic frequencies and further studies should be conducted to verify the role of these mutations in HIV-1 susceptibility.
This study is the first to demonstrate that langerin represents an authentic receptor that binds and internalizes influenza A virus to facilitate infection.
Data suggest that Langerin (CD207)-mediated binding of Yersinia pestis to antigen-presenting cells (APCs (show APCS Proteins)) may promote its dissemination and infection.
Langerin binds heparin (HEP)-like oligosaccharides in two different binding sites depending on the ligand size.
The authors not only show that langerin and caveolin-1 (show CAV1 Proteins) co-localize at the cell membrane and in vesicles but that caveolin-1 (show CAV1 Proteins) mediated HIV-1 uptake is an intrinsic restriction mechanism present in human Langerhans cells that prevents HIV-1 infection.
The impact of two carbohydrate recognition domains mutations, W264R and F241L, on langerin structure, function, and Birbeck granules assembly.
Langerin is not expressed by freshly isolated CD1c (show CD1C Proteins)(+) blood DCs but is rapidly induced on CD1c (show CD1C Proteins)(+) DCs by serum or TGF-beta (show TGFB1 Proteins) via an ALK-3 (show BMPR1A Proteins)-dependent pathway.
Cell-sorting experiments demonstrated that IDO1 (show IDO1 Proteins) expression is found in a subset of CD1a (show CD1A Proteins)(+)CD14 (show NDUFA2 Proteins)(-)langerin(+) cells, expressing CD103 (show ITGAE Proteins)
However, the superoxide dismutase (show SOD1 Proteins) C (SodC (show SOD1 Proteins)) protein of the Mycobacterium leprae cell wall was identified as a langerin-reactive ligand.
The protein encoded by this gene is expressed only in Langerhans cells which are immature dendritic cells of the epidermis and mucosa. It is localized in the Birbeck granules, organelles present in the cytoplasm of Langerhans cells and consisting of superimposed and zippered membranes. It is a C-type lectin with mannose binding specificity, and it has been proposed that mannose binding by this protein leads to internalization of antigen into Birbeck granules and providing access to a nonclassical antigen-processing pathway. Mutations in this gene result in Birbeck granules deficiency or loss of sugar binding activity.
CD207 molecule, langerin
, CD207 antigen, langerin
, C-type lectin domain family 4 member K
, Langerhans cell specific c-type lectin
, C-type lectin domain family 4, member K
, CD 207 antigen