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anti-Mouse (Murine) ADAM17 Anticorps:
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Human Monoclonal ADAM17 Primary Antibody pour CyTOF, FACS - ABIN4900516
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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Human Monoclonal ADAM17 Primary Antibody pour CyTOF, FACS - ABIN4900517
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 ADAM17 Primary Antibody pour FACS - ABIN4897862
Kermarrec, Selloum, Plantefeve, Chosidow, Paoletti, Lopez, Mantz, Desmonts, Gougerot-Pocidalo, Chollet-Martin: Regulation of peritoneal and systemic neutrophil-derived tumor necrosis factor-alpha release in patients with severe peritonitis: role of tumor necrosis factor-alpha converting enzyme cleavage. dans Critical care medicine 2005
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Human Monoclonal ADAM17 Primary Antibody pour FACS - ABIN4897863
Moreira-Tabaka, Peluso, Vonesch, Hentsch, Kessler, Reimund, Dumont, Muller: Unlike for human monocytes after LPS activation, release of TNF-α by THP-1 cells is produced by a TACE catalytically different from constitutive TACE. dans PLoS ONE 2012
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Human Polyclonal ADAM17 Primary Antibody pour IHC - ABIN965510
Rabie, Strehl, Ludwig, Nieswandt: Evidence for a role of ADAM17 (TACE) in the regulation of platelet glycoprotein V. dans The Journal of biological chemistry 2005
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Human Polyclonal ADAM17 Primary Antibody pour ICC, ELISA - ABIN1003300
Moss, Jin, Milla, Bickett, Burkhart, Carter, Chen, Clay, Didsbury, Hassler, Hoffman, Kost, Lambert, Leesnitzer, McCauley, McGeehan, Mitchell, Moyer, Pahel, Rocque, Overton, Schoenen, Seaton, Su et al.: Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. ... dans Nature 1997
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Human Polyclonal ADAM17 Primary Antibody pour ELISA, WB - ABIN1531481
Bilousova, Taylor, Emirzian, Gylys, Frautschy, Cole, Teng: Parallel age-associated changes in brain and plasma neuronal pentraxin receptor levels in a transgenic APP/PS1 rat model of Alzheimer's disease. dans Neurobiology of disease 2015
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Human Polyclonal ADAM17 Primary Antibody pour ICC, ELISA - ABIN1003301
Rosendahl, Ko, Long, Brewer, Rosenzweig, Hedl, Anderson, Pyle, Moreland, Meyers, Kohno, Lyons, Lichenstein: Identification and characterization of a pro-tumor necrosis factor-alpha-processing enzyme from the ADAM family of zinc metalloproteases. dans The Journal of biological chemistry 1997
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Human Polyclonal ADAM17 Primary Antibody pour ICC, FACS - ABIN1030720
McGowan, Mullooly, Caiazza, Sukor, Madden, Maguire, Pierce, McDermott, Crown, ODonovan, Duffy: ADAM-17: a novel therapeutic target for triple negative breast cancer. dans Annals of oncology : official journal of the European Society for Medical Oncology / ESMO 2013
Human Monoclonal ADAM17 Primary Antibody pour IHC (p), PLA - ABIN563080
Kahlert, Weber, Mogler, Bergmann, Schirmacher, Kenngott, Matterne, Mollberg, Rahbari, Hinz, Koch, Aigner, Weitz: Increased expression of ALCAM/CD166 in pancreatic cancer is an independent prognostic marker for poor survival and early tumour relapse. dans British journal of cancer 2009
Overall, iRhom2 (Montrer RHBDF2 Anticorps) binds to TACE throughout its lifecycle, implying that iRhom2 (Montrer RHBDF2 Anticorps) is a primary regulator of stimulated cytokine and growth factor signalling.
Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (Montrer EGFR Anticorps)-ligands by differentially activating ADAM17 or ADAM10 (Montrer ADAM10 Anticorps).
Fhl2 (Montrer FHL2 Anticorps) anticipates the emerging inflammation and specifically the development of psoriatic arthritis by impeding the Adam17-mediated release of TNF (Montrer TNF Anticorps)
most defects in formation of the postnatal epidermal barrier upon keratinocyte-specific ADAM17 deletion are mediated via EGFR (Montrer EGFR Anticorps)
ADAM17 is either not required in T cells under homoeostatic conditions and for control of listeria infection or can be effectively compensated by other mechanisms
In a clinically relevant CADASIL (Montrer NOTCH3 Anticorps) mouse model, we show that exogenous ADAM17 or HB-EGF (Montrer HBEGF Anticorps) restores cerebral arterial tone and blood flow responses, and identify upregulated voltage-dependent potassium channel (Montrer KCNAB2 Anticorps) (KV) number in cerebral arterial myocytes as a heretofore-unrecognized downstream effector of TIMP3 (Montrer TIMP3 Anticorps)-induced deficits.
Conditional ADAM17 knockout mice lacking ADAM17 in all leukocytes had a significant survival advantage during severe polymicrobial sepsis induced by CLP, associated with enhanced neutrophil recruitment at the infectious locus along with decreased bacterial spread and circulating levels of proinflammatory factors. Its induction during sepsis may tip the balance between efficient and impaired neutrophil recruitment.
These results demonstrate a novel physiologic role for a disintegrin and metalloprotease 17 in regulating murine IL-6 (Montrer IL6 Anticorps) signals during inflammatory processes.
These results show that TACE is a target of, and is downregulated by, soluble TNF (Montrer TNF Anticorps)-induced AP-2alpha (Montrer TFAP2A Anticorps) transcription factor in dendritic cells
the critical role of the transmembrane domains of ADAM17 and Rhbdf2 (Montrer RHBDF2 Anticorps) in the regulation of the ADAM17 and EGFR (Montrer EGFR Anticorps), and ADAM17 and TNFalpha (Montrer TNF Anticorps) signaling pathways, was examined.
ADAM10 (Montrer ADAM10 Anticorps) and ADAM17 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 phosphatidylserine exposure is required to then induce its shedding function.
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, but not ADAM10 (Montrer ADAM10 Anticorps). We find that the impaired shedding is caused by the reduced distance between the cleavage site and the plasma membrane.
ADAM17 is a Western diet-inducible enzyme activated by CXCL12 (Montrer CXCL12 Anticorps)-CXCR4 (Montrer CXCR4 Anticorps) signaling, suggesting the pathway: Western diet-->CXCL12 (Montrer CXCL12 Anticorps)-->CXCR4 (Montrer CXCR4 Anticorps)-->ADAM17-->TGFalpha-->EGFR (Montrer EGFR Anticorps). ADAM17 might serve as a druggable target in chemoprevention strategies
The regulation of the shedding activity of ADAM17 is multilayered and different regions of the protease are involved. Intriguingly, its extracellular domains play crucial roles in different regulatory mechanisms. We will discuss the role of these domains in the control of ADAM17 activity.
We show ADAM17 expression in human dopaminergic neurons derived from induced pluripotent stem cells and we discuss how this state-of-the-art technology can be further exploited to study the function of this important protease in the brain and other tissues.
High ADAM17 expression is associated with radioresistance in liver cancer.
inhibition of autophagy led to the decrease in stemness, restoration of mitochondrial proteins and reduced expression of CD44 (Montrer CD44 Anticorps), ABCB1 (Montrer ABCB1 Anticorps) and ADAM17
FoxM1 (Montrer FOXM1 Anticorps) regulates the expression of ADAM-17, which is upregulated in gastric carcinoma.
Glypican-1 (Montrer GPC1 Anticorps) was validated as a novel substrate for ADAM17, with important function in adhesion, proliferation and migration of carcinoma cells.
the chaperone 78-kDa glucose-regulated protein (GRP78 (Montrer HSPA5 Anticorps)) protects the MPD (Montrer MVD Anticorps) against PDI (Montrer PADI1 Anticorps)-dependent disulfide-bond isomerization by binding to this domain and, thereby, preventing ADAM17 inhibition.
these findings provide the direct evidence that ADAM17 cleaves porcine TNFalpha (Montrer TNF Anticorps), which represents a new view for identifying potential therapeutic targets in anti-porcine reproductive and respiratory syndrome virus therapy
ADAM17 was involved in porcine CD16 (Montrer CD16 Anticorps) shedding in porcine reproductive and respiratory syndrome virus-infected pigs.
Overexpression of ADAM17 induced downregulation of CD163 (Montrer CD163 Anticorps) expression and a reduction in reproductive and respiratory syndrome virus infection.
activation of TACE/ADAM17 via a PKC (Montrer FYN Anticorps)-induced c-Src (Montrer SRC Anticorps)-dependent manner mediates proteolytic activation of the EGF (Montrer EGF Anticorps)-like factors that are involved in the induction of granulosa cell differentiation, cumulus expansion, and meiotic maturation of porcine oocytes
Data indicate that TNF-alpha (Montrer TNF Anticorps) stimulates Rac (Montrer AKT1 Anticorps), ADAM17/TACE, and RhoA (Montrer RHOA Anticorps) through the guanine nucleotide exchange factor (Montrer ARHGEF12 Anticorps) (GEF)-H1 (Montrer ARHGEF2 Anticorps).
progesterone-induced TACE/ADAM17 leads to production of soluble EGF (Montrer EGF Anticorps) domain from cumulus cells, which enhances functional changes of cumulus cells and progresses meiotic maturation of oocytes
This gene encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Members of this family are membrane-anchored proteins structurally related to snake venom disintegrins, and have been implicated in a variety of biologic processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene functions as a tumor necrosis factor-alpha converting enzyme\; binds mitotic arrest deficient 2 protein\; and also plays a prominent role in the activation of the Notch signaling pathway.
ADAM metallopeptidase domain 17 (tumor necrosis factor, alpha, converting enzyme)
, a disintegrin and metalloproteinase domain 17 (tumor necrosis factor, alpha, converting enzyme)
, disintegrin and metalloproteinase domain-containing protein 17
, tumor necrosis factor alpha converting enzyme
, a disintegrin and metallopeptidase domain 17
, ADAM metallopeptidase domain 17
, a disintegrin and metalloprotease domain 17
, disintegrin metalloproteinase
, disintegrin and metalloproteinase domain-containing protein 17-like
, ADAM 17
, TNF-alpha convertase
, TNF-alpha converting enzyme
, TNF-alpha-converting enzyme
, a disintegrin and metalloprotease domain 17; TNF-alpha converting enzyme
, a disintegrin and metalloproteinase domain 17
, ADAM metallopeptidase domain 18
, snake venom-like protease
, tumor necrosis factor, alpha, converting enzyme