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anti-Mouse (Murine) 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 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
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
the synaptic localization of APP (show APP Antibodies), ADAM10, and BACE1 (show BACE Antibodies) 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 (show EGFR Antibodies)-ligands by differentially activating ADAM17 (show ADAM17 Antibodies) or ADAM10.
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 and ADAM17 (show ADAM17 Antibodies) 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 (show ADAM17 Antibodies) 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 (show SIGLEC1 Antibodies)-359 to Ser (show SIGLEC1 Antibodies)-361) adjacent to the cleavage site is sufficient to prevent IL-6R cleavage by ADAM17 (show ADAM17 Antibodies), 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 (show TSPAN5 Antibodies), Tspan10, Tspan14, Tspan15 (show TSPAN15 Antibodies), Tspan17, and Tspan33 (show TSPAN33 Antibodies). [REVIEW]
Results found ADAM10 expression under the regulation of MIR (show MLXIP Antibodies)-655 which binds the 3'-UTR (show UTS2R Antibodies) of ADAM10 mediating the progression of hepatocellular carcinoma.
Data suggest that activation of the metalloproteinase ADAM10 by signal peptide peptidase-like 3 (SPPL3 (show SPPL3 Antibodies)) triggered by mutant BRAF (show BRAF Antibodies)(V600E) was a critical transformation event.
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
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