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anti-Mouse (Murine) ADAM10 Antikörper:
anti-Human ADAM10 Antikörper:
anti-Rat (Rattus) ADAM10 Antikörper:
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody für CyTOF, FACS - ABIN4900523
Accarias, Lugo-Villarino, Foucras, Neyrolles, Boullier, Tabouret: Pyroptosis of resident macrophages differentially orchestrates inflammatory responses to Staphylococcus aureus in resistant and susceptible mice. in European journal of immunology 2015
Show all 6 Pubmed References
Mouse (Murine) Monoclonal ADAM10 Primary Antibody für CyTOF, FACS - ABIN4900524
Altmeppen, Prox, Krasemann, Puig, Kruszewski, Dohler, Bernreuther, Hoxha, Linsenmeier, Sikorska, Liberski, Bartsch, Saftig, Glatzel: The sheddase ADAM10 is a potent modulator of prion disease. in eLife 2015
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Human Monoclonal ADAM10 Primary Antibody für 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. in Journal of immunology (Baltimore, Md. : 1950) 2015
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Human Monoclonal ADAM10 Primary Antibody für 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). in The Journal of biological chemistry 2012
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody für 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. in Scientific reports 2015
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody für FACS - ABIN4897868
Gibb, Saleem, Kang, Subler, Conrad: ADAM10 overexpression shifts lympho- and myelopoiesis by dysregulating site 2/site 3 cleavage products of Notch. in Journal of immunology (Baltimore, Md. : 1950) 2011
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Human Polyclonal ADAM10 Primary Antibody für 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. in Gene 2015
Human Monoclonal ADAM10 Primary Antibody für 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. in Journal of leukocyte biology 2013
Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (zeige EGFR Antikörper)-ligands by differentially activating ADAM17 (zeige ADAM17 Antikörper) or ADAM10.
study confirms the importance of ICOSL (zeige ICOSLG Antikörper) shedding in ICOS (zeige ICOS Antikörper)/ICOSL (zeige ICOSLG Antikörper) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (zeige ICOSLG Antikörper) levels
Tspan3 (zeige TSPAN3 Antikörper) is a central endocytic membrane component regulating the expression of ADAM10, presenilin and the amyloid precursor protein (zeige APP Antikörper).
these results show that ADAM10-Notch (zeige NOTCH1 Antikörper) 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 (zeige ADAM17 Antikörper), is indispensable for proper retinal development as a regulator of NOTCH (zeige NOTCH1 Antikörper) 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 (zeige NOTCH1 Antikörper) ligands via Taok3 (zeige TAOK3 Antikörper)-mediated surface expression of ADAM10
Thus, Leda-1/Pianp (zeige C12orf53 Antikörper) is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.
ADAM10 was dispensable for alpha-toxin (zeige PLC Antikörper)-dependent xenophagic targeting of S. aureus, whereas a role for alpha-toxin (zeige PLC Antikörper) attack on the plasma membrane was confirmed.
ADAM10 was essentially involved in maxillofacial bone development. ADAM10 conditional knock-out KO mice present craniofacial dysmorphia and bone defects. Impaired osteoblast differentiation,proliferation and apoptosis underlie the bone deformity.
Newborn mice deficient in ADAM10 exhibited organ-specific vascular defects.
Results found ADAM10 expression under the regulation of MIR (zeige MLXIP Antikörper)-655 which binds the 3'-UTR (zeige UTS2R Antikörper) of ADAM10 mediating the progression of hepatocellular carcinoma.
Data suggest that activation of the metalloproteinase ADAM10 by signal peptide peptidase-like 3 (SPPL3 (zeige SPPL3 Antikörper)) triggered by mutant BRAF (zeige BRAF Antikörper)(V600E) was a critical transformation event.
The ADAM17 (zeige ADAM17 Antikörper) messenger RNA (mRNA) and protein levels were significantly higher in the inferior turbinate than in nasal polyps (p < 0.05). The ADAM10 mRNA and protein levels did not differ significantly between NPs (zeige NPS Antikörper) and inferior turbinates (p > 0.05). ADAM10 and ADAM17 (zeige ADAM17 Antikörper) were expressed primarily in inflammatory cells, submucosal glandular cells, and lining epithelial cells.
study confirms the importance of ICOSL (zeige ICOSLG Antikörper) shedding in ICOS (zeige CTLA4 Antikörper)/ICOSL (zeige ICOSLG Antikörper) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (zeige ICOSLG Antikörper) levels
Inhibition of ADAM10 suppressed the expansion of NK cells and reduced the expression of CD16 (zeige CD16 Antikörper).
Platelet ADAM10 protein expression in patients with AD [Alzheimer's Disease] was positively influenced by serotoninergic medication
Endothelial Tspan5 (zeige TSPAN5 Antikörper)- and Tspan17-ADAM10 complexes may regulate inflammation by maintaining normal VE-cadherin (zeige CDH5 Antikörper) expression and promoting T lymphocyte transmigration.
Regulation of ADAM10 by the TspanC8 subgroup of tetraspanins, namely Tspan5 (zeige TSPAN5 Antikörper), 10, 14, 15, 17 and 33 is reviewed.
active ADAM10 form marks cancer stem-like cells with active Notch (zeige NOTCH1 Antikörper) signaling, known to mediate chemoresistance.
A dramatic decline in ephrinB2 (zeige EFNB2 Antikörper) protein levels on the absence of flotillin-1 (zeige FLOT1 Antikörper) 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 (zeige APLP2 Antikörper) 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