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ADAM9 encodes a member of the ADAM (a disintegrin and metalloprotease domain) family. Additionally we are shipping ADAM9 Kits (25) and ADAM9 Proteins (8) and many more products for this protein.
Showing 10 out of 67 products:
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 references for ABIN391640
Human Monoclonal ADAM9 Primary Antibody for WB - ABIN393227
Xu, Liu, Cai, Yu, Chen: RNAi-mediated ADAM9 gene silencing inhibits metastasis of adenoid cystic carcinoma cells. in Tumour biology 2010
Show all 5 references for ABIN393227
Human Polyclonal ADAM9 Primary Antibody for EIA, WB - ABIN359600
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 3 references for ABIN359600
Human Polyclonal ADAM9 Primary Antibody for FACS, IHC (p) - ABIN652337
McKie, Edwards, Dallas, Houghton, Stringer, Graham, Russell, Croucher: Expression of members of a novel membrane linked metalloproteinase family (ADAM) in human articular chondrocytes. in Biochemical and biophysical research communications 1997
Show all 3 references for ABIN652337
Human Monoclonal ADAM9 Primary Antibody for 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
Show all 2 references for ABIN968156
Dog (Canine) Polyclonal ADAM9 Primary Antibody for WB - ABIN2782602
Zigrino, Steiger, Fox, Löffek, Schild, Nischt, Mauch: Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration. in The Journal of biological chemistry 2007
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 (show TBCE Antibodies) surfaces where it degrades some ECM (show MMRN1 Antibodies) proteins, and it promotes alveolar-capillary barrier injury during ALI
Stromal expression of ADAM-9 during melanoma development modulates the expression of TIMP-1 (show TIMP1 Antibodies) and sTNFR1, which in turn affect tumor cell proliferation and apoptosis.
The data revealed a regulatory paradigm for FGRF2 signaling and identified MT1-MMP (show MMP14 Antibodies) as a critical negative modulator of ADAM9 activity to maintain FGFR2 (show FGFR2 Antibodies) 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 (show ADAM8 Antibodies),-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 (show PRNP Antibodies)) but that this enzyme acts indirectly, likely by contributing to the shedding of ADAM10 (show ADAM10 Antibodies) disintegrin
ADAM9 does not behave as a genuine alpha-secretase but rather acts as an important upstream regulator of ADAM10 (show ADAM10 Antibodies) activity.
ADAM9 enhances CDCP1 (show CDCP1 Antibodies) protein expression by suppressing miR (show MLXIP Antibodies)-218 for lung tumor metastasis
ADAM9 and ROS1 (show ROS1 Antibodies) are direct downstream targets of miR (show MLXIP Antibodies)-33a
Activation of ERalpha (show ESR1 Antibodies) but not ERbeta (show ESR2 Antibodies) increases ADAM9 expression in cultured human neuronal cells.
miR (show MLXIP Antibodies)-126 may act as a tumor suppressor via inhibition of cell invasion by downregulating ADAM9 in breast cancer development.
This study has identified tenascin-C (show TNC Antibodies) as a promoter of the invasiveness of brain tumor-initiating cells through a mechanism involving ADAM-9 proteolysis via the c-Jun NH2-terminal kinase (show MAPK8 Antibodies) pathway.
Whole exome sequencing was performed, which identified a novel, homozygous mutation in ADAM9, c.967delT; p.Ser323Glnfs*33.
ADAM9 plays an important role in gastric cancer proliferation and invasion, and that while expressed at high levels in some cancer cells that are responsive to functional inhibition and antitumor activity of a catalytic site-directed antibody.
Given the significant correlation between tumor ADAM9 expression and serum RCAS1 (show EBAG9 Antibodies) concentration in both cervical and endometrial cancer as well as the role for ADAM9 in RCAS1 (show EBAG9 Antibodies) shedding.
our data indicated that miR (show MLXIP Antibodies)-126 inhibits cell growth, invasion, and migration of OS cells by downregulating ADAM-9.
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)
, disintegrin and metalloproteinase domain-containing protein 9
, ADAM metallopeptidase domain 9
, disintegrin and metalloproteinase domain-containing protein 9-like
, ADAM 9
, a disintegrin and metalloprotease domain 9
, a disintegrin and metalloproteinase domain 9 (meltrin gamma)
, metalloprotease/disintegrin/cysteine-rich protein 9
, myeloma cell metalloproteinase
, cellular disintegrin-related protein
, cone rod dystrophy 9
, a disintegrin and metallopeptidase domain 9 (meltrin gamma)
, meltrin gamma
, a disintegrin and metalloproteinase domain 9
, metalloprotease/disintegrin xMDC9
, disintegrin and metalloproteinase domain 9