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The protein encoded by ADAM15 is a member of the ADAM (a disintegrin and metalloproteinase) protein family. 再加上，我们可以发ADAM15 试剂盒 (16) 和 ADAM15 蛋白 (13)和数多这个蛋白质的别的产品。
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Human Monoclonal ADAM15 Primary Antibody for FACS, ICC - ABIN4900519
Ungerer, Doberstein, Bürger, Hardt, Boehncke, Böhm, Pfeilschifter, Dummer, Mihic-Probst, Gutwein: ADAM15 expression is downregulated in melanoma metastasis compared to primary melanoma. in Biochemical and biophysical research communications 2010
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Cow (Bovine) Polyclonal ADAM15 Primary Antibody for IHC, WB - ABIN2782601
Zhong, Poghosyan, Pennington, Scott, Handsley, Warn, Gavrilovic, Honert, Krüger, Span, Sweep, Edwards: Distinct functions of natural ADAM-15 cytoplasmic domain variants in human mammary carcinoma. in Molecular cancer research : MCR 2008
ADAM15 attenuates the progression of atherosclerosis; in contrast, a mutated form of ADAM15, created by ablation of the protease function, has no significant effect on atherosclerosis.
findings indicated that silencing ADAM15 had antiinflammatory effects in FLSs and efficiently inhibited the development of CIA (显示 NCOA5 抗体).
the catalytic activity of ADAM15 is not crucial for its function in promoting pathological neovascularization in the mouse OIR model, most likely because of the very limited substrate repertoire of ADAM15.
ADAM15 upregulation contributes to inflammatory lung injury by promoting endothelial hyperpermeability and neutrophil transmigration.
A disintegrin and metalloproteinase 15 contributes to atherosclerosis by mediating endothelial barrier dysfunction via Src (显示 SRC 抗体) family kinase activity.
Adult Adam15(-/-) mice displayed an increase in bone volume and thickness with an increase in the number and activity of osteoblasts, whereas osteoclasts were apparently unaffected.
ADAM15 has a role in pathological neovascularization in mice
cytoplasmic domain of ADAM15v2 strongly interacts with Lck (显示 LCK 抗体) and plays an important role in T lymphocytes
The accelerated development of murine osteoarthritis in ADAM15 deficiency and the proadhesive and cell survival-promoting in vitro effect of ADAM15 overexpression suggest a homeostatic role of ADAM15 in cartilage remodeling.
observations suggest that a disintegrin and metalloproteinase (ADAM)-8 (显示 ADAM8 PLURAL_@27060@),-9,-10,-12,-15,and -17 play an important role in mouse uterine tissue remodelling during the oestrous cycle
found modest expression of ADAM15 in pericytes in normal retina and strong up-regulation of ADAM15 in retinal vascular endothelial cells in ischemic retina
The results of our study demonstrate that ADAM15 is strongly up regulated in a small but highly aggressive fraction of prostate cancers.
Data show that ADAM9 (显示 ADAM9 抗体) silencing affected MMP2 (显示 MMP2 抗体) and ADAM15 expression.
ADAM15 promotes lung cancer cell invasion through directly targeting MMP9 (显示 MMP9 抗体) activation.
the results revealed an undescribed role of ADAM15 in the invasion of human bladder cancer and suggested that the ADAM15 catalytic domain may represent a viable therapeutic target in patients with advanced disease.
present a tumor suppressive mechanism for ADAM15 exosomes and provide insight into the functional significance of exosomes that generate tumor-inhibitory factors
these data suggest the potential role of miR147b in regulating endothelial barrier function by targeting ADAM15 expression.
findings indicated that silencing ADAM15 had antiinflammatory effects in FLSs and efficiently inhibited the development of CIA (显示 ASF1A 抗体).
The severity of intrauterine adhesions positively correlates to the protein and transcript expression levels of ADAM-15 and ADAM-17 (显示 ADAM17 抗体) in uterine tissue.
ADAM15 contributes to apoptosis resistance in rheumatoid arthritis synovial fibroblasts by activating the Src (显示 SRC 抗体)/FAK (显示 PTK2 抗体) pathway upon FasL (显示 FASL 抗体) exposure.
ADAM15 acts as a negative regulator of TRIF (显示 TRIM69 抗体)-mediated NF-kappaB (显示 NFKB1 抗体) and IFN-beta (显示 IFNB1 抗体) reporter gene activity via TLR3 (显示 TLR3 抗体) and TLR4 (显示 TLR4 抗体) signaling.
The protein encoded by this gene is a member of the ADAM (a disintegrin and metalloproteinase) protein family. ADAM family members are type I transmembrane glycoproteins known to be involved in cell adhesion and proteolytic ectodomain processing of cytokines and adhesion molecules. This protein contains multiple functional domains including a zinc-binding metalloprotease domain, a disintegrin-like domain, as well as a EGF-like domain. Through its disintegrin-like domain, this protein specifically interacts with the integrin beta chain, beta 3. It also interacts with Src family protein-tyrosine kinases in a phosphorylation-dependent manner, suggesting that this protein may function in cell-cell adhesion as well as in cellular signaling. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed.
ADAM metallopeptidase domain 15
, a disintegrin and metalloproteinase domain 15
, metalloproteinase ADAM15
, disintegrin and metalloproteinase domain-containing protein 15-like
, ADAM 15
, a disintegrin and metalloprotease domain 15 (metargidin)
, a disintegrin and metalloproteinase domain 15 (metargidin)
, disintegrin and metalloprotease 15
, disintegrin and metalloproteinase domain-containing protein 15
, metalloprotease RGD disintegrin protein
, metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15
, a disintegrin and metallopeptidase domain 15 (metargidin)
, tMDC VI