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anti-Human ADAM9 Anticorps:
anti-Mouse (Murine) ADAM9 Anticorps:
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Human Polyclonal ADAM9 Primary Antibody pour CyTOF, FACS - ABIN4899544
Tam, Au, Ma: The association between laminin and microglial morphology in vitro. dans Scientific reports 2016
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Human Polyclonal ADAM9 Primary Antibody pour FACS, WB - ABIN391640
Weskamp, Krätzschmar, Reid, Blobel: MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. dans The Journal of cell biology 1996
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Human Monoclonal ADAM9 Primary Antibody pour IF, IP - ABIN968156
Wolfsberg, Primakoff, Myles, White: ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions. dans The Journal of cell biology 1995
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Data show that ADAM9 is over-expressed in an activated form in human ovarian clear cell carcinomas, and suggest that it plays a key role in cisplatin resistance.
Mechanistic investigations found that quercetin suppressed Snail (Montrer SNAI1 Anticorps)-dependent Akt (Montrer AKT1 Anticorps) activation by upregulating maspin (Montrer SERPINB5 Anticorps) and Snail (Montrer SNAI1 Anticorps)-independent a disintegrin and metalloproteinase (ADAM) 9 expression pathways to modulate the invasive ability of NSCLC cells
ADAM9 is a component of cell-cell junctions. ADAM9 must be expressed by both adjacent cells for cell junction localisation. ADAM9 can self-associate via its ectodomain. The soluble ADAM9 ectodomain inhibits monocyte-endothelial transmigration.
hese results emphasize the critical influence of ADAM9 on lung cancer progression and aggressiveness. ADAM9 should at least be a marker of cancer aggressiveness and a potential therapeutic target for cancer treatment.
MiR (Montrer MLXIP Anticorps)-126-ADAM9 pathway-based therapeutic targeting may represent a novel approach for the inhibition of hepatitis B virus-related hepatocellular carcinoma metastases.
miR (Montrer MLXIP Anticorps)-520f inhibited tumor cell invasion by directly targeting ADAM9 and the TGFbeta (Montrer TGFB1 Anticorps) receptor TGFBR2 (Montrer TGFBR2 Anticorps).
The results suggest that ADAM9 mRNA expression is associated with tumor grade and histological type in gliomas and can serve as an independent prognostic factor, specifically in LGG patients.
ADAM9 could possibly be regarded as a biomarker for GC diagnosis and prevention. Moreover, as directly targeted by miR (Montrer MLXIP Anticorps)-126 in GC, ADAM9 may be a potential target for GC therapeutic treatment which warrants intensive study
ADAM9 is a direct target of miR (Montrer MLXIP Anticorps)-20b and that miR (Montrer MLXIP Anticorps)-20b decreased the 5-FU resistance of HCT116-R cells.
the present study demonstrated the expression and clinical roles of miR (Montrer MLXIP Anticorps)-140 in glioma and suggested that miR (Montrer MLXIP Anticorps)-140 inhibited proliferation, migration and invasion of glioma cells, partially at least via suppressing ADAM9 expression. Therefore, miR (Montrer MLXIP Anticorps)-140 may be a novel candidate target for the development of therapeutic strategies for patients with glioma
ADAM9 silencing inhibits the tumor growth of non-small lung cancer in vitro and in vivo.
analysis of how ADAM9, 10, and 17 maturation requires processing at a newly identified Proprotein Convertase cleavage site
ADAM9 is expressed in an inducible fashion on PMN (Montrer TBCE Anticorps) surfaces where it degrades some ECM (Montrer MMRN1 Anticorps) proteins, and it promotes alveolar-capillary barrier injury during ALI
Stromal expression of ADAM-9 during melanoma development modulates the expression of TIMP-1 (Montrer TIMP1 Anticorps) and sTNFR1, which in turn affect tumor cell proliferation and apoptosis.
The data revealed a regulatory paradigm for FGRF2 signaling and identified MT1-MMP (Montrer MMP14 Anticorps) as a critical negative modulator of ADAM9 activity to maintain FGFR2 (Montrer FGFR2 Anticorps) signaling in calvarial osteogenesis.
ADAM-9 expression plays an important role in mediating cell-cell contacts between fibroblasts and melanoma cells and that these interactions contribute to proteolytic activities required during invasion of melanoma cells.
results show the previously unreported role of ADAM-9 in wound repair by regulating keratinocyte migration through modulation of collagen XVII shedding
observations suggest that a disintegrin and metalloproteinase (ADAM)-8,-9,-10,-12,-15,and -17 play an important role in mouse uterine tissue remodelling during the oestrous cycle
data provide evidence that ADAM9 disintegrin is an important regulator of the physiological processing of cellular prion protein PrP(c (Montrer PRNP Anticorps)) but that this enzyme acts indirectly, likely by contributing to the shedding of ADAM10 (Montrer ADAM10 Anticorps) disintegrin
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 biological processes involving cell-cell and cell-matrix interactions, including fertilization, muscle development, and neurogenesis. The protein encoded by this gene interacts with SH3 domain-containing proteins, binds mitotic arrest deficient 2 beta protein, and is also involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. Several alternatively spliced transcript variants have been identified for this gene.
ADAM metallopeptidase domain 9 (meltrin gamma)
, cellular disintegrin-related protein
, cone rod dystrophy 9
, disintegrin and metalloproteinase domain-containing protein 9
, metalloprotease/disintegrin/cysteine-rich protein 9
, myeloma cell metalloproteinase
, ADAM 9
, a disintegrin and metalloprotease domain 9
, a disintegrin and metalloproteinase domain 9 (meltrin gamma)
, a disintegrin and metallopeptidase domain 9 (meltrin gamma)
, meltrin gamma
, a disintegrin and metalloproteinase domain 9
, metalloprotease/disintegrin xMDC9
, disintegrin and metalloproteinase domain 9
, ADAM metallopeptidase domain 9
, disintegrin and metalloproteinase domain-containing protein 9-like