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anti-Mouse (Murine) ADAM10 Anticorps:
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody pour CyTOF, FACS - ABIN4900524
Accarias, Lugo-Villarino, Foucras, Neyrolles, Boullier, Tabouret: Pyroptosis of resident macrophages differentially orchestrates inflammatory responses to Staphylococcus aureus in resistant and susceptible mice. dans European journal of immunology 2015
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody pour CyTOF, FACS - ABIN4900523
Altmeppen, Prox, Krasemann, Puig, Kruszewski, Dohler, Bernreuther, Hoxha, Linsenmeier, Sikorska, Liberski, Bartsch, Saftig, Glatzel: The sheddase ADAM10 is a potent modulator of prion disease. dans eLife 2015
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Human Monoclonal ADAM10 Primary Antibody pour CyTOF, FACS - ABIN4900521
Zingoni, Cecere, Vulpis, Fionda, Molfetta, Soriani, Petrucci, Ricciardi, Fuerst, Amendola, Mytilineos, Cerboni, Paolini, Cippitelli, Santoni: Genotoxic Stress Induces Senescence-Associated ADAM10-Dependent Release of NKG2D MIC Ligands in Multiple Myeloma Cells. dans Journal of immunology (Baltimore, Md. : 1950) 2015
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Human Monoclonal ADAM10 Primary Antibody pour CyTOF, FACS - ABIN4900520
Breshears, Schlievert, Peterson: A disintegrin and metalloproteinase 17 (ADAM17) and epidermal growth factor receptor (EGFR) signaling drive the epithelial response to Staphylococcus aureus toxic shock syndrome toxin-1 (TSST-1). dans The Journal of biological chemistry 2012
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody pour FACS - ABIN4897869
Doi, Imai, Kressler, Yagita, Agata, Vooijs, Hamazaki, Inoue, Minato: Crucial role of the Rap G protein signal in Notch activation and leukemogenicity of T-cell acute lymphoblastic leukemia. dans Scientific reports 2015
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Human Polyclonal ADAM10 Primary Antibody pour IF (p), IHC (p) - ABIN701020
Li, Xie, He, Wang, Duan, Yang, Wang: Identification of ADAM10 and ADAM17 with potential roles in the spermatogenesis of the Chinese mitten crab, Eriocheir sinensis. dans Gene 2015
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody pour FACS - ABIN4897868
Gibb, Saleem, Kang, Subler, Conrad: ADAM10 overexpression shifts lympho- and myelopoiesis by dysregulating site 2/site 3 cleavage products of Notch. dans Journal of immunology (Baltimore, Md. : 1950) 2011
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Human Monoclonal ADAM10 Primary Antibody pour FACS - ABIN4897866
Nygaard, Pallister, Zurek, Voyich: The impact of α-toxin on host cell plasma membrane permeability and cytokine expression during human blood infection by CA-MRSA USA300. dans Journal of leukocyte biology 2013
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Human Monoclonal ADAM10 Primary Antibody pour FACS - ABIN4897865
Endsley, Somasunderam, Li, Oezguen, Thiviyanathan, Murray, Rubin, Hodge, OBrien, Lewis, Ferguson: Nuclear trafficking of the HIV-1 pre-integration complex depends on the ADAM10 intracellular domain. dans Virology 2014
the synaptic localization of APP (Montrer APP Anticorps), ADAM10, and BACE1 (Montrer BACE Anticorps) in the mouse cerebral cortex, was examined.
Pharmacological inhibition of ADAM10 reduces sEphrin-B2 levels in bronchoalveolar lavage and prevents lung fibrosis in mice. Consistent with the mouse data, ADAM10-sEphrin-B2 signaling is upregulated in fibroblasts from human subjects with idiopathic pulmonary fibrosis.
Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (Montrer EGFR Anticorps)-ligands by differentially activating ADAM17 (Montrer ADAM17 Anticorps) or ADAM10.
study confirms the importance of ICOSL (Montrer ICOSLG Anticorps) shedding in ICOS (Montrer ICOS Anticorps)/ICOSL (Montrer ICOSLG Anticorps) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (Montrer ICOSLG Anticorps) levels
Tspan3 (Montrer TSPAN3 Anticorps) is a central endocytic membrane component regulating the expression of ADAM10, presenilin and the amyloid precursor protein (Montrer APP Anticorps).
these results show that ADAM10-Notch (Montrer NOTCH1 Anticorps) signaling in ovarian somatic cells governs the primordial follicle formation by controlling the development of ovarian pregranulosa cells.
Findings provide evidence that ADAM10, and not ADAM17 (Montrer ADAM17 Anticorps), is indispensable for proper retinal development as a regulator of NOTCH (Montrer NOTCH1 Anticorps) signaling.
this study shows that during positive selection in the spleen, B-cell receptor signaling causes immature type 1 transitional B cells to become receptive to Notch (Montrer NOTCH1 Anticorps) ligands via Taok3 (Montrer TAOK3 Anticorps)-mediated surface expression of ADAM10
Thus, Leda-1/Pianp (Montrer C12orf53 Anticorps) is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.
ADAM10 was dispensable for alpha-toxin (Montrer PLC Anticorps)-dependent xenophagic targeting of S. aureus, whereas a role for alpha-toxin (Montrer PLC Anticorps) attack on the plasma membrane was confirmed.
therapies against ADAM10 and ADAM17 (Montrer ADAM17 Anticorps) may promote cancer stem cell migration away from the tumourigenic niche resulting in a differentiated phenotype that is more susceptible to treatment.
Presence of anti-ADAM10 auto-Antibodies seems to reflect the increased tumor expression of the immunogenic immature-ADAM10 in a group of Colorectal cancer patients, and is associated with a favourable prognosis in patients at stage III of the disease.
ADAM10 and ADAM17 (Montrer ADAM17 Anticorps) are the best characterized members of the ADAM (A Disintegrin and Metalloproteinase) - family of transmembrane proteases. Both are involved diverse physiological and pathophysiological processes.For ADAM17 (Montrer ADAM17 Anticorps) phosphatidylserine exposure is required to then induce its shedding function.
A better understanding of the regulatory mechanisms controlling the expression, subcellular localization and activity of ADAM10 will likely uncover suitable drug targets which will allow a more specific and fine-tuned modulation of its proteolytic activity
In the present study, the authors show that deletion of a triple serine (3S) motif (Ser (Montrer SIGLEC1 Anticorps)-359 to Ser (Montrer SIGLEC1 Anticorps)-361) adjacent to the cleavage site is sufficient to prevent IL-6R cleavage by ADAM17 (Montrer ADAM17 Anticorps), but not ADAM10. We find that the impaired shedding is caused by the reduced distance between the cleavage site and the plasma membrane.
Here, I review some of the proposed functions of ADAM10 associated with intestinal crypt homeostasis and tumorigenesis within the gastrointestinal tract in vivo.
Study reports the structure of the ADAM10 ectodomain, providing fundamental insights into how substrate selectivity and regulation of catalytic activity is achieved in this important representative of the ADAM family of metalloproteases.
Data suggest that ADAM10 associates directly with all members of a subgroup of tetraspanins having eight cysteines in the large extracellular domain ('TspanC8'): Tspan5 (Montrer TSPAN5 Anticorps), Tspan10, Tspan14, Tspan15 (Montrer TSPAN15 Anticorps), Tspan17, and Tspan33 (Montrer TSPAN33 Anticorps). [REVIEW]
Results found ADAM10 expression under the regulation of MIR (Montrer MLXIP Anticorps)-655 which binds the 3'-UTR (Montrer UTS2R Anticorps) of ADAM10 mediating the progression of hepatocellular carcinoma.
Data suggest that activation of the metalloproteinase ADAM10 by signal peptide peptidase-like 3 (SPPL3 (Montrer SPPL3 Anticorps)) triggered by mutant BRAF (Montrer BRAF Anticorps)(V600E) was a critical transformation event.
A dramatic decline in ephrinB2 (Montrer EFNB2 Anticorps) protein levels on the absence of flotillin-1 (Montrer FLOT1 Anticorps) expression is specific, and is partly the result of an increased susceptibility to cleavage by the metalloprotease ADAM10.
significantly increased expression of ADAM10 in the ISR versus non-ISR segment in diabetic minipigs
Data show that ADAM10 and APLP2 (Montrer APLP2 Anticorps) are expressed in proximal tubule cells, and that ADAM10 activity has a pronounced effect on expression of specific brush-border proteins.
Intracellular trafficking of ADAM10 critically requires a novel sorting signal within its cytoplasmic domain.
N-glycosylation is crucial for ADAM10 processing and resistance to proteolysis, and results suggest that it is required for full-enzyme activity.
Members of the ADAM family are cell surface proteins with a unique structure possessing both potential adhesion and protease domains. This gene encodes and ADAM family member that cleaves many proteins including TNF-alpha and E-cadherin.
a disintegrin and metalloprotease domain 10a
, ADAM metallopeptidase domain 10
, disintegrin and metalloproteinase domain-containing protein 10
, ADAM10 metallopeptidase
, disintegrin and metalloproteinase domain-containing protein 10-like
, ADAM 10
, a disintegrin and metalloprotease domain (ADAM) 10
, a disintegrin and metalloprotease domain 10
, kuzbanian protein homolog
, mammalian disintegrin-metalloprotease
, a disintegrin and metalloproteinase domain 10
, a disintegrin and metallopeptidase domain 10
, myelin-associated metalloproteinase