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Human Monoclonal CLEC2D Primary Antibody pour IHC (p), ELISA - ABIN565412
Roth, Mittelbronn, Wick, Meyermann, Tatagiba, Weller: Malignant glioma cells counteract antitumor immune responses through expression of lectin-like transcript-1. dans Cancer research 2007
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Human Monoclonal CLEC2D Primary Antibody pour FACS - ABIN4897676
Chalan, Bijzet, Huitema, Kroesen, Brouwer, Boots: Expression of Lectin-Like Transcript 1, the Ligand for CD161, in Rheumatoid Arthritis. dans PLoS ONE 2015
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Human Monoclonal CLEC2D Primary Antibody pour ELISA, WB - ABIN949236
Williams, Eaton, Jones, Rengan, Burshtyn: Vaccinia virus Western Reserve induces rapid surface expression of a host molecule detected by the antibody 4C7 that is distinct from CLEC2D. dans Microbiology and immunology 2016
Human Monoclonal CLEC2D Primary Antibody pour FACS - ABIN4897677
Dupuy, Lambert, Zucman, Choukem, Tognarelli, Pages, Lebbé, Caillat-Zucman: Human Herpesvirus 8 (HHV8) sequentially shapes the NK cell repertoire during the course of asymptomatic infection and Kaposi sarcoma. dans PLoS pathogens 2012
Human Polyclonal CLEC2D Primary Antibody pour CyTOF, FACS - ABIN4900423
Llibre, Garner, Partridge, Freeman, Klenerman, Willberg: Expression of lectin-like transcript-1 in human tissues. dans F1000Research 2017
REVIEW: Biological and Clinical Significance of Human NKRP1A/LLT1 Receptor/Ligand Interactions
These results show that susceptibility of normal articular chondrocytes to lysis by NK cells is modulated by NKR-P1A/LLT1 interactions. Thus, NKR-P1A/LLT1 interaction might provide some novel target for therapeutic interventions in the course of pathological cartilage injury.
Blocking LLT1-NKRP1A interaction will make prostate cancer cells susceptible to killing by NK cells, suggesting a therapeutic option for treatment of prostate cancer.
these data suggest that LLT1-CD161 interactions play a novel and important role in B cell maturation within the Germinal center in humans.
In RA joints, LLT1 is expressed by cells of the monocyte/macrophage lineage.
The hexamer of glycosylated LLT1 consists of three classical dimers. The hexameric packing may indicate a possible mode of interaction of C-type lectin-like proteins in the glycosylated form.
One polymorphism in LLT1 was found to be associated with our Crohn's Disease population (P<0.034).Our Ulcerative Colitis cohort was not associated with the variation in LLT1 (P=0.33)
LLT1 and CD161 have roles in modulating immune responses to pathogens; and interferon-gamma contributes to modulate immune responses
Molecular basis for LLT1 protein recognition by human CD161 protein (NKRP1A/KLRB1).
Data show that only CLEC2D isoform 1 (LLT1) is expressed on the cell surface.
LLT1 used Src-PTK, p38 and ERK signalling pathways, but not PKC, PI3K or calcineurin pathways, to increase production of IFN-gamma by human natural killer cells.
LLT1 induces Interferon Type II production by natural killer cells.
Data show that osteoclast inhibitory lectin (OCIL) binds a range of physiologically important glycosaminoglycans, and this property may modulate OCIL actions upon other cells [OCIL].
Engagement of CD161 on NK cells with LLT1 expressed on target cells inhibited NK cell-mediated cytotoxicity and IFN-gamma secretion. LLT1/CD161 interaction in the presence of a TCR signal enhanced IFN-gamma production by T cells
LLT1 on target cells can inhibit NK cytotoxicity via interactions with CD161. LLT1 activates NFAT-GFP reporter cells expressing a CD3zeta-CD161 chimeric receptor; reciprocally, reporter cells with a CD3zeta-LLT1 chimeric receptor are stimulated by CD161
Expression of LLT1 on activated dendritic cells and B cells suggests that it might regulate the cross-talk between NK cells and APCs
Women with a lysine (GG genotype) at position 19 of the OCIL protein displayed lower bone mineral density at femoral neck and at lumbar spine sites than women having an asparagine residue.
these findings demonstrate that Clr-b is an IFN-stimulated gene on healthy bystander cells, in addition to a missing-self marker on MCMV-infected cells, and thereby enhances the dynamic range of innate self-nonself discrimination by NK cells
Data suggest that killer cell lectin-like receptors NKR-P1B:Clr-b (Klrb1:Clec2d) interactions may provide a model for human hematopoietic cell transplants.
Reductions of Clr-b may be involved in sensitizing poxvirus-infected cells to natural killer (NK) cells.
cloning and characterization of a cognate ligand, Ocil, for the inhibitory NK receptors (NKR)-P1B and NKR-P1D. Ocil/Clr-b is displayed at high levels on nearly all hematopoietic cells, in a pattern that is similar to that of class I MHC molecules.
Data show that osteoclast inhibitory lectin (OCIL) binds a range of physiologically important glycosaminoglycans, and this property may modulate OCIL actions upon other cells.
Limited divergence of the BALB/c Nkrp1-Ocil/Clr region helps explain a longstanding confusion regarding the strain-specific NK1.1 alloantigen reactivity of mouse natural killer cells.
OCIL is a physiological negative regulator of bone.
PTHrp(1-34) regulates OCIL expression in vitro through cAMP/PKA, Ca(2+)/CaMK II, and MAPK signaling pathways.
Identification of a novel family of genes, named Clr, encoding C-type lectin-like molecules, which maps in the natural killer (NK) gene complex (NKC) on mouse Chromosome 6.
Mouse Nkrp1d and Nkrp1f bind specific C-type lectin-related (Clr) molecules. Nkrp1d mediated inhibition when recognizing Clrb, a molecule expressed in dendritic cells and macrophages. Nkrp1 and Clr are intertwined in a genetically conserved NKC region.
This gene encodes a member of the natural killer cell receptor C-type lectin family. The encoded protein inhibits osteoclast formation and contains a transmembrane domain near the N-terminus as well as the C-type lectin-like extracellular domain. Several alternatively spliced transcript variants have been identified for this gene.
C-type lectin domain family 2 member D
, C-type lectin related f
, C-type lectin superfamily 2, member D
, lectin-like NK cell receptor
, lectin-like transcript 1
, osteoclast inhibitory lectin
, C-type lectin-domain family 2 member D
, C-type lectin-related protein B
, lectin-like transmembrane protein
, C-type lectin domain family 2 member D5
, C-type lectin domain family 2, member D
, C-type lectin domain family 2 member H-like