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anti-Mouse (Murine) ADAM10 Antibodies:
anti-Human ADAM10 Antibodies:
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Mouse (Murine) Monoclonal ADAM10 Primary Antibody for 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 for 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
Show all 6 Pubmed References
Human Monoclonal ADAM10 Primary Antibody for CyTOF, FACS - ABIN4900520
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
Show all 5 Pubmed References
Human Monoclonal ADAM10 Primary Antibody for CyTOF, FACS - ABIN4900521
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
Show all 5 Pubmed References
Mouse (Murine) Monoclonal ADAM10 Primary Antibody for 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
Show all 4 Pubmed References
Mouse (Murine) Monoclonal ADAM10 Primary Antibody for 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
Show all 2 Pubmed References
Human Polyclonal ADAM10 Primary Antibody for 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 for 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
study confirms the importance of ICOSL (show ICOSLG Antibodies) shedding in ICOS (show ICOS Antibodies)/ICOSL (show ICOSLG Antibodies) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (show ICOSLG Antibodies) levels
Tspan3 (show TSPAN3 Antibodies) is a central endocytic membrane component regulating the expression of ADAM10, presenilin and the amyloid precursor protein (show APP Antibodies).
these results show that ADAM10-Notch (show NOTCH1 Antibodies) 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 (show ADAM17 Antibodies), is indispensable for proper retinal development as a regulator of NOTCH (show NOTCH1 Antibodies) 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 (show NOTCH1 Antibodies) ligands via Taok3 (show TAOK3 Antibodies)-mediated surface expression of ADAM10
Thus, Leda-1/Pianp (show C12orf53 Antibodies) is constitutively processed by proprotein convertases, sheddases including MMPs and ADAM10/17 and intramembrane protease gamma-secretase.
ADAM10 was dispensable for alpha-toxin (show PLC Antibodies)-dependent xenophagic targeting of S. aureus, whereas a role for alpha-toxin (show PLC Antibodies) 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.
Findings demonstrate the direct requirement of ADAM10 in cortical radial migration and reveal the underlying mechanism by linking ADAM10-initiated regulated intramembrane proteolysis of Notch (show NOTCH1 Antibodies) to the regulation of microtubule cytoskeleton through transcriptional control of Dcx (show DCX Antibodies) expression
The ADAM17 (show ADAM17 Antibodies) 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 (show NPS Antibodies) and inferior turbinates (p > 0.05). ADAM10 and ADAM17 (show ADAM17 Antibodies) were expressed primarily in inflammatory cells, submucosal glandular cells, and lining epithelial cells.
study confirms the importance of ICOSL (show ICOSLG Antibodies) shedding in ICOS (show CTLA4 Antibodies)/ICOSL (show ICOSLG Antibodies) function and expression and it identifies ADAM10 as the most important sheddase for controlling ICOSL (show ICOSLG Antibodies) levels
Inhibition of ADAM10 suppressed the expansion of NK cells and reduced the expression of CD16 (show CD16 Antibodies).
Platelet ADAM10 protein expression in patients with AD [Alzheimer's Disease] was positively influenced by serotoninergic medication
Endothelial Tspan5 (show TSPAN5 Antibodies)- and Tspan17-ADAM10 complexes may regulate inflammation by maintaining normal VE-cadherin (show CDH5 Antibodies) expression and promoting T lymphocyte transmigration.
Regulation of ADAM10 by the TspanC8 subgroup of tetraspanins, namely Tspan5 (show TSPAN5 Antibodies), 10, 14, 15, 17 and 33 is reviewed.
active ADAM10 form marks cancer stem-like cells with active Notch (show NOTCH1 Antibodies) signaling, known to mediate chemoresistance.
Data show that tetraspanin 33 (tspan33 (show TSPAN33 Antibodies)) is an early activation marker, and that disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) protein expression does not correlate with Tspan33 (show TSPAN33 Antibodies) expression in B cells.
High ADAM10 expression is associated with metastasis of hepatocellular carcinoma.
A dramatic decline in ephrinB2 (show EFNB2 Antibodies) protein levels on the absence of flotillin-1 (show FLOT1 Antibodies) 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 (show APLP2 Antibodies) 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