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anti-Human F2RL1 Antikörper:
anti-Mouse (Murine) F2RL1 Antikörper:
anti-Rat (Rattus) F2RL1 Antikörper:
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Human Monoclonal F2RL1 Primary Antibody für FACS - ABIN4898819
Amiable, Tat, Lajeunesse, Duval, Pelletier, Martel-Pelletier, Boileau: Proteinase-activated receptor (PAR)-2 activation impacts bone resorptive properties of human osteoarthritic subchondral bone osteoblasts. in Bone 2009
Show all 2 Pubmed References
Dog (Canine) Polyclonal F2RL1 Primary Antibody für WB - ABIN2788314
Yau, Liu, Fairlie: Toward drugs for protease-activated receptor 2 (PAR2). in Journal of medicinal chemistry 2013
PAR2 signaling from endosomes underlies the persistent hyperexcitability of nociceptors that mediates chronic pain of irritable bowel syndrome.
PAR2 plays an important role in the proliferation and metastasis of hepatocellular carcinoma.
PAR2 expression is crucial for TGF-beta1 (zeige TGFB1 Antikörper)-induced ERK (zeige EPHB2 Antikörper) activation and cell motility. Functional cooperation of PAR2 and TGF-beta1 (zeige TGFB1 Antikörper) involves a physical interaction between PAR2 and ALK5 (zeige TGFBR1 Antikörper).
Activation of PAR2 inhibits the expression of IL-10 (zeige IL10 Antikörper) in B cells, which can be reversed by treating B cells with Bcl2L12 (zeige BCL2L12 Antikörper) shRNA-carrying liposomes.
High Expressions of PAR2 is associated with cancer.
activation of PAR2 compromises the vascular endothelial barrier function by suppressing the expression of Ve-cadherin (zeige CDH5 Antikörper).
plays a direct role in melanogenesis by increasing stem cell factor (zeige KITLG Antikörper) secretion from keratinocytes
Neutrophil elastase (zeige ELANE Antikörper) enhances IL-12p40 production by lipopolysaccharide-stimulated macrophages via transactivation of the PAR-2/EGFR (zeige EGFR Antikörper)/TLR4 (zeige TLR4 Antikörper) signaling pathway
PAR2 is crucial for TGF-beta1 (zeige TGFB1 Antikörper)-induced cell motility by its ability to sustain expression of ALK5 (zeige TGFBR1 Antikörper). Therapeutically targeting PAR2 may thus be a promising approach in preventing TGF-beta (zeige TGFB1 Antikörper)-dependent driven metastatic dissemination in PDAC and possibly other stroma-rich tumour types.
Protease-activated receptor 2 (PAR2) is present in human skin.
PAR2 activation in the prostate may contribute to the development of lower urinary tract dysfunction through proinflammatory as well as profibrotic pathways.
Our data show that PAR2 counterbalanced enhanced contractions to ET-1 (zeige EDN1 Antikörper) in aortas from Tsk (zeige FBN1 Antikörper) mice. PAR2 could represent a possible target for novel drugs in the treatment of vascular complications in fibrosis.
thrombin (zeige F2 Antikörper) is increased in a mouse model of cancer cachexia in a partially interleukin-6 (zeige IL6 Antikörper) dependent manner
Data show that activated protein C (zeige PROC Antikörper) signals via protease activated receptors PAR2/PAR3 (zeige F2RL2 Antikörper) to expand Treg cells, mitigating the disease in mice.
PAR2 plays an important and previously unrecognised anti-apoptotic role in T cell development
thrombin (zeige F2 Antikörper) has a role in diet-induced obesity through fibrin-driven inflammation
PAR2 modulation was sufficient to induce islet cell transdifferentiation in the absence of beta-cells.
Our results are suggestive that PAR2 inhibition may play a role in the treatment of diseases with increased inflammatory responses in renal systems
PAR2/GSK3beta is a novel pathway that plays a critical role in the regulation of stem/progenitor cell survival and proliferation in normal colon crypts and colon cancer.
Enhanced FXa (zeige F10 Antikörper) and PAR2 exacerbate DN and that both are promising targets for preventing diabetic nephropathy.
PAR1 (zeige F2R Antikörper) and PAR2 regulate endothelial NO synthase (zeige NOS Antikörper) phosphorylation and activity through G(12/13) and G(q), delineating the signaling pathways by which the proteases act on protease-activated receptors to modulate endothelial functions.
Coagulation factor II (thrombin) receptor-like 1 (F2RL1) is a member of the large family of 7-transmembrane-region receptors that couple to guanosine-nucleotide-binding proteins. F2RL1 is also a member of the protease-activated receptor family. It is activated by trypsin, but not by thrombin. It is activated by proteolytic cleavage of its extracellular amino terminus. The new amino terminus functions as a tethered ligand and activates the receptor. The F2RL1 gene contains two exons and is widely expressed in human tissues. The predicted protein sequence is 83% identical to the mouse receptor sequence.
Proteinase-activated receptor 2
, G-protein coupled receptor 11
, coagulation factor II receptor-like 1
, protease-activated receptor 2
, proteinase-activated receptor 2
, thrombin receptor-like 1
, Protease-activated receptor-2
, proteinase-activated receptor-2
, Proteinase-activated receptor-2 G protein-coupled receptor 11
, Proteinase-activated receptor-2, G protein-coupled receptor 11