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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
Show all 5 Pubmed References
Collective results suggested that galangin may act as an effective chemotherapeutic agent for glioma cancer depending on its ability to bring about ADAM9 and Erk1/2 activation.
miR (zeige MLXIP Antikörper)-543 serves as a tumor suppressor in glioblastoma multiforme through ADAM9 regulation.
Study demonstrates that diabetes-mediated decrease in miR (zeige MLXIP Antikörper)-126 leads to a corresponding increase in its target, ADAM9, which in turn cleaves MERTK (zeige MERTK Antikörper) (inactivates downstream engulfment signaling), thus resulting in defective macrophage efferocytosis of apoptotic cardiomyocytes.
These results revealed that ADAM9 down-regulates miR-1 (zeige FSD1 Antikörper) via activating EGFR (zeige EGFR Antikörper) signaling pathways, which in turn enhances CDCP1 (zeige CDCP1 Antikörper) expression to promote lung cancer progression.
These findings suggested that miR302a inhibited osteosarcoma cell growth and metastasis by targeting ADAM9.
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.
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