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anti-Human ADAM9 Antikörper:
anti-Mouse (Murine) ADAM9 Antikörper:
anti-Rat (Rattus) ADAM9 Antikörper:
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Human Polyclonal ADAM9 Primary Antibody für CyTOF, FACS - ABIN4899544
Tam, Au, Ma: The association between laminin and microglial morphology in vitro. in Scientific reports 2016
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Human Polyclonal ADAM9 Primary Antibody für FACS, WB - ABIN391640
Weskamp, Krätzschmar, Reid, Blobel: MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. in The Journal of cell biology 1996
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Human Monoclonal ADAM9 Primary Antibody für 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. in 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 (zeige SNAI1 Antikörper)-dependent Akt (zeige AKT1 Antikörper) activation by upregulating maspin (zeige SERPINB5 Antikörper) and Snail (zeige SNAI1 Antikörper)-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 (zeige MLXIP Antikörper)-126-ADAM9 pathway-based therapeutic targeting may represent a novel approach for the inhibition of hepatitis B virus-related hepatocellular carcinoma metastases.
miR (zeige MLXIP Antikörper)-520f inhibited tumor cell invasion by directly targeting ADAM9 and the TGFbeta (zeige TGFB1 Antikörper) receptor TGFBR2 (zeige TGFBR2 Antikörper).
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 (zeige MLXIP Antikörper)-126 in GC, ADAM9 may be a potential target for GC therapeutic treatment which warrants intensive study
ADAM9 is a direct target of miR (zeige MLXIP Antikörper)-20b and that miR (zeige MLXIP Antikörper)-20b decreased the 5-FU resistance of HCT116-R cells.
the present study demonstrated the expression and clinical roles of miR (zeige MLXIP Antikörper)-140 in glioma and suggested that miR (zeige MLXIP Antikörper)-140 inhibited proliferation, migration and invasion of glioma cells, partially at least via suppressing ADAM9 expression. Therefore, miR (zeige MLXIP Antikörper)-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 (zeige TBCE Antikörper) surfaces where it degrades some ECM (zeige MMRN1 Antikörper) proteins, and it promotes alveolar-capillary barrier injury during ALI
Stromal expression of ADAM-9 during melanoma development modulates the expression of TIMP-1 (zeige TIMP1 Antikörper) and sTNFR1, which in turn affect tumor cell proliferation and apoptosis.
The data revealed a regulatory paradigm for FGRF2 signaling and identified MT1-MMP (zeige MMP14 Antikörper) as a critical negative modulator of ADAM9 activity to maintain FGFR2 (zeige FGFR2 Antikörper) 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 (zeige PRNP Antikörper)) but that this enzyme acts indirectly, likely by contributing to the shedding of ADAM10 (zeige ADAM10 Antikörper) 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