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CLEC4E encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Zusätzlich bieten wir Ihnen CLEC4E Antikörper (68) und CLEC4E Proteine (12) und viele weitere Produktgruppen zu diesem Protein an.
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Mincle has the ability to survey mycolate-derived glycolipids from actinomycetes, distinguishing non-pathogenic (e.g. Rhodococcus spp.) and pathogenic (e.g. Mycobacterium tuberculosis) species on the basis of alpha-chain (zeige FCGRT ELISA Kits) length.
combination adjuvant systems demonstrate markedly different immune activation with age, with combined DC activation via Macrophage-inducible C-type lectin and TLR7 (zeige TLR7 ELISA Kits)/8 representing a novel approach to enhance the efficacy of early-life vaccines.
We here show that Mincle gene expression was induced in alveolar macrophages and neutrophils in bronchoalveolar lavage fluids of mice and patients with pneumococcal pneumonia
a nonredundant role for Clec4e in coordinating major biological pathways involved in atherosclerosis
CLEC4E expression is significantly upregulated in human masticatory mucosa during wound healing
The expression of Mincle increases significantly during the early period of Aspergillus fumigatus infection, while expression of eight corresponding cytokines changes. Mincle, as a pattern recognition receptor, may play a role in the early innate immune response of the corneal resistance against fungus.
Induction of Mincle by Helicobacter pylori and consequent anti-inflammatory signaling denote a bacterial survival strategy.
our findings identify mincle as a contributor to the inflammatory response after traumatic brain injury
Data indicate that MINCLE receptor is able to mediate the response to trehalose-6,6-dimycolate (TDM) dependent on SYK (zeige SYK ELISA Kits) kinase and CARD9 (zeige CARD9 ELISA Kits) protein.
mincle is a fungal receptor that can suppress antifungal immunity and, as such, is a potential therapeutic target.
our results indicate that Mincle plays an important role in neutrophil infiltration and suggest that Mincle signaling may provide a therapeutic target for treating sepsis
Mincle activation by cholesterol sulfate causes the secretion of a range of proinflammatory mediators in response to skin damage.
this study shows that mincle inhibits neutrophils and macrophages apoptosis in Aspergillus fumigatus keratitis
Mincle is induced specifically on M1 macrophages, where Mincle-Syk (zeige SYK ELISA Kits) signaling promotes and maintains inflammatory phenotypes of M1 macrophages in acute renal inflammation.
work implicates a novel innate immune driver of Con (zeige KITLG ELISA Kits) A hepatitis and, more broadly, suggests a potential role for Mincle in diseases governed by sterile inflammation.
Mincle deletion results in TLR4 (zeige TLR4 ELISA Kits)-mediated inflammation.
Priming by Mincle-deficient dendritic cells (DCs).
Thus, macrophage activation by the corynebacterial cell wall relies on TLR2-driven robust Mincle expression and the cooperative action of both receptors.
this study shows that immune activation in vitro and in vivo by trehalose esters of simple fatty acids requires two acyl chains of length and involves Mincle
Attenuated neutrophil extracellular trap formation in Mincle-/- neutrophils correlates with impaired autophagy activation in vitro and in vivo, whereas reactive oxygen species formation in these neutrophils remained intact.
The structure of an extended portion of the extracellular domain of mincle, beyond the minimal C-type carbohydrate recognition domain, also constrains the way the binding domains may interact on the surface of macrophages.
The data demonstrate how mincle bridges between the surfaces of the macrophage and the mycobacterium.
the function of the guinea pig homologue of Mincle (gpMincle) and MCL (zeige CLEC4D ELISA Kits) (gpMCL). gpMincle directly bound to trehalose-6,6'-dimycolate
This gene encodes a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signalling, glycoprotein turnover, and roles in inflammation and immune response. The encoded type II transmembrane protein is a downstream target of CCAAT/enhancer binding protein (C/EBP), beta (CEBPB) and may play a role in inflammation. Alternative splice variants have been described but their full-length sequence has not been determined. This gene is closely linked to other CTL/CTLD superfamily members on chromosome 12p13 in the natural killer gene complex region.
C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamily member 9
, C-type lectin domain family 4 member E
, C-type lectin superfamily member 9
, macrophage-inducible C-type lectin
, C-type (calcium dependent, carbohydrate recognition domain) lectin, superfamily member 9
, C-type lectin, superfamily member 9
, C-type lectin domain family 4, member E