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anti-Mouse (Murine) ADAM12 Anticorps:
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Human Polyclonal ADAM12 Primary Antibody pour IHC (p), IHC - ABIN268655
Isozaki, Rabquer, Ruth, Haines, Koch: ADAM-10 is overexpressed in rheumatoid arthritis synovial tissue and mediates angiogenesis. dans Arthritis and rheumatism 2013
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Human Polyclonal ADAM12 Primary Antibody pour ELISA, WB - ABIN547357
Galliano, Huet, Frygelius, Polgren, Wewer, Engvall: Binding of ADAM12, a marker of skeletal muscle regeneration, to the muscle-specific actin-binding protein, alpha -actinin-2, is required for myoblast fusion. dans The Journal of biological chemistry 2000
Human Polyclonal ADAM12 Primary Antibody pour ICC, IF - ABIN4278207
Qundos, Hong, Tybring, Divers, Odeberg, Uhlen, Nilsson, Schwenk: Profiling post-centrifugation delay of serum and plasma with antibody bead arrays. dans Journal of proteomics 2013
Human Monoclonal ADAM12 Primary Antibody pour ELISA, WB - ABIN393268
Wang, Lu, Zhu, Li: ADAM12 is an effective marker in the second trimester of pregnancy for prenatal screening of Down syndrome. dans Prenatal diagnosis 2010
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Human Monoclonal ADAM12 Primary Antibody pour ELISA, WB - ABIN563531
Zhou, Ran, Hu, Pan, Li, Chen, Sun, Peng, Zhao, Yu, Sun, Yang: TM4SF3 promotes esophageal carcinoma metastasis via upregulating ADAM12m expression. dans Clinical & experimental metastasis 2008
results suggest that adam12 plays a significant role in the regulation of body growth during juvenile stage in zebrafish, although the precise molecular mechanisms await further study.
In conclusion, MiR29a regulates endothelial cell ADAM12 upregulation in ischemia and this is impaired in hyperglycemia.
It was concluded that TNF-alpha-induced changes in extracellular matix components increased expression of ADAM12 among other changes that were temporally related with the onset of myocyte function.
ADAM12 and ADAM17 are essential molecules for the impairment of barrier function of retinal vasculature under hypoxia.
Augmentation of ADAM12 expression in vivo improved outcomes in Balb/c mice, whereas knockdown of ADAM12 made outcomes worse in C57Bl/6 mice. In vitro, ADAM12 expression modulates endothelial cell proliferation, survival, and angiogenesis.
The effect of insulin-like growth factor-I on ADAM12 expression during the course of myogenesis is reported.
Nitric oxide synthase deficiency has differential effects on ADAM12 expression in growing mouse brain.
Inhibition of Erbb2 suppressed the increase in metalloproteinase ADAM12 expression in skin tumors.
TGF-beta stimulation of renal cells results in a significant up-regulation of Adams 10, 17, 12, and 19
ADAM12 enhanced ephrin-A1 cleavage in response to transforming growth factor-betra1 in primary tumors.
The endogenous SnoN plays a role in regulating ADAM12 expression in response to TGFbeta1.
Adam12 is spatiotemporally expressed in decidualizing stromal cells in intact pregnant females and in pseudopregnant mice undergoing artificially induced decidualization.
properly folded mouse ADAM12, after passing a rate-limiting step of exit from the ER, is processed in the secretory pathway and reaches the cell surface, where it can mediate adhesion-mediated signaling
These observations suggest Meltrin alpha may be involved in regulating adipogenesis and myogenesis through a linked developmental pathway.We also report here the chromosomal locations of Meltrin alpha in the mouse
Adam12 overexpression in skeletal muscle results in compenstaion for dystrophin- deficiency by increasing alpha7 integrin, utrophin and associated glycoproteins.
Role of metalloproteinase disintegrin ADAM12 in determination of quiescent reserve cells during myogenic differentiation in vitro was studied.
involvement of meltrin alpha in the development of obesity and in adipogenic cell proliferation.
novel protein-protein interaction reported here involving the extracellular domain of ADAM12 may have important biological consequences during myoblast differentiation
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
ADAM12 is a potential target for design of drugs that prevent carcinoma growth and is essential for tumor development and progression in the W10 mouse model for prostate cancer.
endogenous ADAM9 and/or ADAM12 present in wild type mouse embryonic fibroblasts contribute to Dll1 processing
our study provide crucial evidence that ADAM12 induces epithelial to mesenchymal transition and promotes cell migration, invasion and proliferation in pituitary adenomas via EGFR/ERK signaling pathway
This meta-analysis suggests that the ADAM 12 genetic polymorphisms rs1871054 and rs1044122 might be associated with risk of knee osteoarthritis; rs3740199 might be associated with risk of knee osteoarthritis in men.
Data report that ADAM12 is upregulated in the vessels of aggressive breast tumors and exerts key regulatory functions. Also, its expression is significantly positively correlated with pro-angiogenic factors including VEGF and MMP-9 but negatively associated with TSP1. These findings suggest that ADAM12 regulates endothelial cell function and facilitates a proangiogenic microenvironment in a STAT3-dependent manner.
Results suggest that ADAM12 gene is a susceptibility gene underlying both joint destruction and growth retardation of the Kashin-Beck disease (KBD).
ADAM12 is induced by Twist1 and plays a crucial role in tumor invasion and metastasis by regulating both invadopodia and focal adhesions
statistically significant association between rs1871054 and risk of Knee Osteoarthritis in Asian population; other polymorphisms (rs3740199, rs1044122, or rs1278279) in ADAM12 were not associated with Knee Osteoarthritis in any population (Meta-Analysis).
rs3740199 polymorphism does not contribute to the development of knee osteoarthritis [meta-analysis]
Tetraspanin-8 has a role in promoting hepatocellular carcinoma metastasis by increasing ADAM12m expression
A novel regulator, myoferlin, of ADAM12 is discovered in HeLa cells and this protein increases ADAM12 expression level, stability, and its enzymatic activity, leading to the reduction of its substrate, E-cadherin, which plays important roles in the regulation of cell adhesion and tumor metastasis.
Our data support a role for ADAM12 in NHL cell proliferation, adhesion, and drug resistance, and it may pave the way for a novel therapeutic approach for CAM-DR in NHL.
The rs3740199 polymorphism in the ADAM12 gene was associated with knee osteoarthritis genetic susceptibility.
These results indicate that ADAM12 actively supports the CSC phenotype in claudin-low breast cancer cells via modulation of the EGFR pathway.
We conclude that ADAM12 and MMP-14 are associated with cavernous sinus invasion in pituitary adenomas, which qualifies these proteins in diagnosis and therapy.
ADAM12 expression is significantly upregulated in human masticatory mucosa during wound healing
Stromal expression patterns for both ADAM12 and CDCP1.
The first trimester maternal ADAM12-s levels were statistically significantly higher in the entire ART group, IVF and ICSI groups, and normal cycle-frozen embryo transfer group when compared with those in the controls.
The level of ADAM12 was upregulated in tumor tissues of breast cancer compared to that of adjacent normal tissues. patients with higher level of ADAM12 exhibited shorter survival time compared to that of low level of ADAM12
The siRNA-directed loss of ADAM12 impedes spontaneous fusion of primary cytotrophoblasts, whereas overexpression of the secreted variant, ADAM12S, potentiates cell fusion in the Bewo trophoblast cell line.
the present findings support the conclusion that the E2F1 transcription factor regulates the expression of ADAM12 by binding differential cis-acting elements.
ADAM12L is associated with epithelial to mesenchymal transition (EMT) and contributes to TGF-beta-dependent EMT.
These findings suggest ADAM12 is upregulated in muscles with more slow-oxidative myofibres, such as the LM, and is linked to type I myofibers in cattle.
The 5'- and 3'-regions of bovive ADAM12 have been analysed and compared to the human gene, and the promoter region has been cloned and sequenced.
This gene encodes a member of the ADAM (a disintegrin and metalloprotease) protein 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. This gene has two alternatively spliced transcripts: a shorter secreted form and a longer membrane-bound form. The shorter form is found to stimulate myogenesis.
ADAM metallopeptidase domain 12
, ADAM metallopeptidase domain 12 (meltrin alpha)
, a disintegrin and metalloproteinase domain 12 (meltrin alpha)
, ADAM 12
, a disintegrin and metalloprotease domain 12
, disintegrin and metalloproteinase domain-containing protein 12
, meltrin alpha
, ADAM12 short isoform
, disintegrin and metalloprotease 12
, a disintegrin and metallopeptidase domain 12 (meltrin alpha)