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Human IL17RD Protein expressed in HEK-293 Cells - ABIN2723368
Mellett, Atzei, Bergin, Horgan, Floss, Wurst, Callanan, Moynagh: Orphan receptor IL-17RD regulates Toll-like receptor signalling via SEFIR/TIR interactions. in Nature communications 2015
miR-193a-3p is downregulated in ulcerative colitis neoplasia, and its loss promotes carcinogenesis through upregulation of IL17RD. These findings provide novel insight into inflammation-driven colorectal cancer and could suggest new therapeutic targets in this high-risk population
Low SEF expression is associated with Epithelial-Mesenchymal Transition in Breast Cancer and thus Metastasis in breast Cancer.
Taken together, these data suggest evidence that loss of hSef may be a critical event facilitating tumor dissemination of prostate cancer through alteration of EMT.
IL17RD negatively regulates Toll-like receptor (TLR)-induced responses.
Demonstrate SEF expression in a healthy ovary during folliculogenesis and suggest hormonal regulation of its expression may be an important factor involved in intra-ovarian control mechanisms.
Downregulation of Dusp6, Sprouty4, and Sef--negative modulators of FGF2/ERK1/2 signaling--was present in eutopic endometria of adenomyosis, which may play critical roles in the development of adenomyosis.
These results reveal Sef-S actives Lys63-linked TAK1 polyubiquitination on lysine 209, induces TAK1-mediated JNK and p38 activation and also results apoptosis in 293T cells.
FGF17 and IL17RD prpopsed as the two top candidates in the entire proteome on the basis of a statistical test of their protein-protein interaction patterns to proteins known to be altered in congenital hypogonadotropic hypogonadism.
Downregulation of SEF mRNA is associated with prostate cancer.
Orphan receptor IL-17RD tunes IL-17A signalling and is required for neutrophilia.
This study establishes Sef as a feedback antagonist of proinflammatory cytokines and highlights its potential to regulate the crosstalk between proinflammatory cytokine receptors and receptor tyrosine kinases.
The expression of hSef is decreased in epithelial ovarian carcinoma tissue, but the expression of FGF-2 is increased.
Findings indicate that Ras-induced nuclear accumulation of activated MEK1/2 was reliant on downregulation of the spatial regulator Sef.
Sef exerts its inhibitory effects at the level of FGFR and upstream of Ras providing an additional level of negative regulation of FGF signaling
human SEF is likely to play critical roles in endothelial or epithelial functions such as proliferation, migration, and angiogenesis
HSef acts as a spatial regulator for ERK signaling by targeting ERK to the cytoplasm.
Sef binds to TAK1 and has a role in JNK activation and apoptosis
Sef is downregulated in advanced prostate cancer and might facilitate an enhanced tumorigenic response to FGFs
Sef inhibited FGF induced, but not RasG12V mediated, signal transduction. We propose that Sef interacted with Ras in the inhibition of Ras/MAPK signaling pathway.
hSef isoforms can control signal specificity and subsequent cell fate by utilizing different mechanisms to modulate RTK signaling
Deficiency of IL-17RD expression in cells leads to enhanced pro-inflammatory signalling and gene expression in response to TLR stimulation, and Il17rd(-/-) mice are more susceptible to TLR-induced septic shock.
these studies indicate that Sef has specific roles in osteoblast and osteoclast lineages and that its absence results in increased osteoblast and osteoclast activity with a net increase in cortical bone mass.
Since expression of IL-17 is elevated in 3-month-old MRL/lpr mice, we suggest that it plays a role in the pathophysiology of autoimmune dacryoadenitis in these mice.
Over-expressing Sef specifically in the lens of transgenic mice led to impaired lens and eye development that resulted in microphthalmia.
Fgf8, Spry2 and Sef belong to a synexpression group and may functionally interact during mouse embryonic development
Sef and Sproutys function synergistically to regulate Gbx2 expression in the anterior hindbrain.
Here we demonstrated that both extracellular and transmembrane domains of Sef contributed to Sef-mediated negative regulation of FGF signaling.
Sef-S inhibits FGF-induced NIH3T3 cell proliferation via an ERK-independent mechanism and therefore suggest that alternative splice licenses sef gene to inhibit cell proliferation via multiple signaling pathways.
Sef is expressed in the lens throughout embryogenesis and becomes restricted to the lens epithelium, indicating that lens cell proliferation and fiber differentiation may be tightly regulated by this negative regulatory molecule.
These results show both increases and decreases in Sef levels affect the assembly and function of the auditory brainstem.
Sef (Il17rd) interacts with TAK1 and mediates JNK activation and apoptosis.
This gene encodes a membrane protein belonging to the interleukin-17 receptor (IL-17R) protein family. The encoded protein is a component of the interleukin-17 receptor signaling complex, and the interaction between this protein and IL-17R does not require the interleukin (PMID: 19079364). The gene product also affects fibroblast growth factor signaling, inhibiting or stimulating growth through MAPK/ERK signaling (PMID: 21663947, 18096367).
interleukin 17 receptor D
, interleukin-17 receptor D-like
, IL-17 receptor D
, interleukin-17 receptor D
, interleukin-17 receptor-like protein
, sef homolog
, similar expression to FGF genes protein