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The protein encoded by ADAM15 is a member of the ADAM (a disintegrin and metalloproteinase) protein family. Additionally we are shipping ADAM15 Antibodies (111) and ADAM15 Proteins (13) and many more products for this protein.
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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.
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 (show SRC ELISA Kits) 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 (show LCK ELISA Kits) 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,-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 (show ADAM9 ELISA Kits) silencing affected MMP2 (show MMP2 ELISA Kits) and ADAM15 expression.
ADAM15 promotes lung cancer cell invasion through directly targeting MMP9 (show MMP9 ELISA Kits) 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.
The severity of intrauterine adhesions positively correlates to the protein and transcript expression levels of ADAM-15 and ADAM-17 (show ADAM17 ELISA Kits) in uterine tissue.
ADAM15 contributes to apoptosis resistance in rheumatoid arthritis synovial fibroblasts by activating the Src (show SRC ELISA Kits)/FAK (show PTK2 ELISA Kits) pathway upon FasL (show FASL ELISA Kits) exposure.
ADAM15 acts as a negative regulator of TRIF (show TRIM69 ELISA Kits)-mediated NF-kappaB (show NFKB1 ELISA Kits) and IFN-beta (show IFNB1 ELISA Kits) reporter gene activity via TLR3 (show TLR3 ELISA Kits) and TLR4 (show TLR4 ELISA Kits) 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