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Rat (Rattus) ADAM17 Protein expressed in Human Cells - ABIN2009530
Wang, Huang, Nayak, Matthews, Warburton, Shi, Sanchez-Esteban: Strain-induced differentiation of fetal type II epithelial cells is mediated via the integrin ?6?1-ADAM17/tumor necrosis factor-?-converting enzyme (TACE) signaling pathway. in The Journal of biological chemistry 2013
Overall, iRhom2 (show RHBDF2 Proteins) binds to TACE throughout its lifecycle, implying that iRhom2 (show RHBDF2 Proteins) is a primary regulator of stimulated cytokine and growth factor signalling.
Xenoestrogens biphenol-A and nonylphenol stimulate the release of EGFR (show EGFR Proteins)-ligands by differentially activating ADAM17 or ADAM10 (show ADAM10 Proteins).
Fhl2 (show FHL2 Proteins) anticipates the emerging inflammation and specifically the development of psoriatic arthritis by impeding the Adam17-mediated release of TNF (show TNF Proteins)
most defects in formation of the postnatal epidermal barrier upon keratinocyte-specific ADAM17 deletion are mediated via EGFR (show EGFR Proteins)
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 (show NOTCH3 Proteins) mouse model, we show that exogenous ADAM17 or HB-EGF (show HBEGF Proteins) restores cerebral arterial tone and blood flow responses, and identify upregulated voltage-dependent potassium channel (show KCNAB2 Proteins) (KV) number in cerebral arterial myocytes as a heretofore-unrecognized downstream effector of TIMP3 (show TIMP3 Proteins)-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 (show IL6 Proteins) signals during inflammatory processes.
These results show that TACE is a target of, and is downregulated by, soluble TNF (show TNF Proteins)-induced AP-2alpha (show TFAP2A Proteins) transcription factor in dendritic cells
the critical role of the transmembrane domains of ADAM17 and Rhbdf2 (show RHBDF2 Proteins) in the regulation of the ADAM17 and EGFR (show EGFR Proteins), and ADAM17 and TNFalpha (show TNF Proteins) signaling pathways, was examined.
Cullin 3 (show CUL3 Proteins) regulates ADAM17-mediated ectodomain shedding of AREG (show AREG Proteins).
ADAM17 may be a key enzyme that regulates the generation of TNF-alpha (show TNF Proteins) in oral keratinocytes.
therapies against ADAM10 (show ADAM10 Proteins) and ADAM17 may promote cancer stem cell migration away from the tumourigenic niche resulting in a differentiated phenotype that is more susceptible to treatment.
ADAM10 (show ADAM10 Proteins) 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 (show SIGLEC1 Proteins)-359 to Ser (show SIGLEC1 Proteins)-361) adjacent to the cleavage site is sufficient to prevent IL-6R cleavage by ADAM17, but not ADAM10 (show ADAM10 Proteins). 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 (show CXCL12 Proteins)-CXCR4 (show CXCR4 Proteins) signaling, suggesting the pathway: Western diet-->CXCL12 (show CXCL12 Proteins)-->CXCR4 (show CXCR4 Proteins)-->ADAM17-->TGFalpha-->EGFR (show EGFR Proteins). 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 (show CD44 Proteins), ABCB1 (show ABCB1 Proteins) and ADAM17
these findings provide the direct evidence that ADAM17 cleaves porcine TNFalpha (show TNF Proteins), 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 (show CD16 Proteins) shedding in porcine reproductive and respiratory syndrome virus-infected pigs.
Overexpression of ADAM17 induced downregulation of CD163 (show CD163 Proteins) expression and a reduction in reproductive and respiratory syndrome virus infection.
activation of TACE/ADAM17 via a PKC (show FYN Proteins)-induced c-Src (show SRC Proteins)-dependent manner mediates proteolytic activation of the EGF (show EGF Proteins)-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 (show TNF Proteins) stimulates Rac (show AKT1 Proteins), ADAM17/TACE, and RhoA (show RHOA Proteins) through the guanine nucleotide exchange factor (show ARHGEF12 Proteins) (GEF)-H1 (show ARHGEF2 Proteins).
progesterone-induced TACE/ADAM17 leads to production of soluble EGF (show EGF Proteins) 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