Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species and application
anti-Human ADAM9 Antibodies:
anti-Mouse (Murine) ADAM9 Antibodies:
anti-Rat (Rattus) ADAM9 Antibodies:
Go to our pre-filtered search.
Human Polyclonal ADAM9 Primary Antibody for CyTOF, FACS - ABIN4899544
Tam, Au, Ma: The association between laminin and microglial morphology in vitro. in Scientific reports 2016
Show all 7 Pubmed References
Human Polyclonal ADAM9 Primary Antibody for 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
Human Polyclonal ADAM9 Primary Antibody for FACS, IHC (p) - ABIN652337
Hotoda, Koike, Sasagawa, Ishiura: A secreted form of human ADAM9 has an alpha-secretase activity for APP. in Biochemical and biophysical research communications 2002
Show all 4 Pubmed References
our results showed that ADAM9 is an important mediator of IL-6-induced hepatocellular carcinoma cell migration and invasion
ADAM9 knock-out cells failed to produce viral progeny when incubated with encephalomyocarditis virus. However, bypassing encephalomyocarditis virus entry into cells through delivery of viral RNA directly to the cytosol yielded infectious virions from ADAM9 knock-out cells, suggesting that ADAM9 is not required for encephalomyocarditis virus replication post-entry.
ADAM9 regulates beta1 integrin endocytosis. Reduced migration of ADAM9-silenced cells is, at least in part, caused by the accumulation and altered activity of beta1 integrin at the cell surface
SNX9 knockdown revealed a nonredundant effect on overall ADAM9 protein levels, resulting in increased ADAM9 levels at the cell surface
miR-129-5p suppressed cell proliferation and invasion ability through regulating ADAM9.
Studies indicate that a disintegrin and a metalloprotease 9 (ADAM9) is involved in solid cancers with the different mechanisms which it employ to drive tumor progression [Review].
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-543 serves as a tumor suppressor in glioblastoma multiforme through ADAM9 regulation.
Study demonstrates that diabetes-mediated decrease in miR-126 leads to a corresponding increase in its target, ADAM9, which in turn cleaves MERTK (inactivates downstream engulfment signaling), thus resulting in defective macrophage efferocytosis of apoptotic cardiomyocytes.
These results revealed that ADAM9 down-regulates miR-1 via activating EGFR signaling pathways, which in turn enhances CDCP1 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-dependent Akt activation by upregulating maspin and Snail-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-126-ADAM9 pathway-based therapeutic targeting may represent a novel approach for the inhibition of hepatitis B virus-related hepatocellular carcinoma metastases.
miR-520f inhibited tumor cell invasion by directly targeting ADAM9 and the TGFbeta receptor TGFBR2.
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-126 in GC, ADAM9 may be a potential target for GC therapeutic treatment which warrants intensive study
ADAM9 is a direct target of miR-20b and that miR-20b decreased the 5-FU resistance of HCT116-R cells.
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 surfaces where it degrades some ECM proteins, and it promotes alveolar-capillary barrier injury during ALI
Stromal expression of ADAM-9 during melanoma development modulates the expression of TIMP-1 and sTNFR1, which in turn affect tumor cell proliferation and apoptosis.
The data revealed a regulatory paradigm for FGRF2 signaling and identified MT1-MMP as a critical negative modulator of ADAM9 activity to maintain FGFR2 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) but that this enzyme acts indirectly, likely by contributing to the shedding of ADAM10 disintegrin
ADAM9 does not behave as a genuine alpha-secretase but rather acts as an important upstream regulator of ADAM10 activity.
endogenous ADAM9 and/or ADAM12 present in wild type mouse embryonic fibroblasts contribute to Dll1 processing
amyloid precursor protein processing in ADAM9 deficient neurons is unaltered--REVIEW
ADAM10 performs a dual role in cells, as a metalloprotease when it is membrane-bound, and as a potential signaling protein once cleaved by ADAM9/15 and the gamma-Secretase
Results suggest that ADAM9 could be an attractive target for the prevention of proliferative retinopathies, choroidal neovascularization, and cancer.
ADAM9 is a CRD gene and also is a form of pathology wherein retinal disease first manifests at the POS-RPE junction.
ADAM9 and ADAM10 can both contribute to collagen XVII shedding in skin.
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