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anti-Mouse (Murine) ADAM12 Antibodies:
anti-Human ADAM12 Antibodies:
anti-Rat (Rattus) ADAM12 Antibodies:
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Human Polyclonal ADAM12 Primary Antibody for IHC (p), IHC - ABIN268655
Isozaki, Rabquer, Ruth, Haines, Koch: ADAM-10 is overexpressed in rheumatoid arthritis synovial tissue and mediates angiogenesis. in Arthritis and rheumatism 2013
Show all 2 Pubmed References
Human Monoclonal ADAM12 Primary Antibody for ELISA, WB - ABIN563531
Zhou, Ran, Hu, Pan, Li, Chen, Sun, Peng, Zhao, Yu, Sun, Yang: TM4SF3 promotes esophageal carcinoma metastasis via upregulating ADAM12m expression. in Clinical & experimental metastasis 2008
Human Monoclonal ADAM12 Primary Antibody for ELISA, WB - ABIN393268
Wang, Lu, Zhu, Li: ADAM12 is an effective marker in the second trimester of pregnancy for prenatal screening of Down syndrome. in Prenatal diagnosis 2010
Show all 6 Pubmed References
Human Polyclonal ADAM12 Primary Antibody for ICC, IF - ABIN4278207
Qundos, Hong, Tybring, Divers, Odeberg, Uhlen, Nilsson, Schwenk: Profiling post-centrifugation delay of serum and plasma with antibody bead arrays. in Journal of proteomics 2013
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 (show TNF Antibodies)-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 (show ADAM17 Antibodies) 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 (show IGF1 Antibodies) on ADAM12 expression during the course of myogenesis is reported.
Nitric oxide synthase (show NOS Antibodies) deficiency has differential effects on ADAM12 expression in growing mouse brain.
Inhibition of Erbb2 (show ERBB2 Antibodies) suppressed the increase in metalloproteinase ADAM12 expression in skin tumors.
TGF-beta (show TGFB1 Antibodies) stimulation of renal cells results in a significant up-regulation of Adams 10, 17, 12, and 19
ADAM12 enhanced ephrin-A1 (show EFNA1 Antibodies) cleavage in response to transforming growth factor-betra1 in primary tumors.
The endogenous SnoN (show SKIL Antibodies) plays a role in regulating ADAM12 expression in response to TGFbeta1 (show TGFB1 Antibodies).
our study provide crucial evidence that ADAM12 induces epithelial to mesenchymal transition and promotes cell migration, invasion and proliferation in pituitary adenomas via EGFR (show EGFR Antibodies)/ERK (show EPHB2 Antibodies) 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 (show VEGFA Antibodies) and MMP-9 (show MMP9 Antibodies) but negatively associated with TSP1 (show THBS1 Antibodies). These findings suggest that ADAM12 regulates endothelial cell function and facilitates a proangiogenic microenvironment in a STAT3 (show STAT3 Antibodies)-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 (show TWIST1 Antibodies) 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).
Tetraspanin-8 (show TSPAN8 Antibodies) has a role in promoting hepatocellular carcinoma metastasis by increasing ADAM12m expression
A novel regulator, myoferlin (show MYOF Antibodies), 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 (show CDH1 Antibodies), which plays important roles in the regulation of cell adhesion and tumor metastasis.
Our data support a role for ADAM12 in NHL (show RTEL1 Antibodies) cell proliferation, adhesion, and drug resistance, and it may pave the way for a novel therapeutic approach for CAM-DR in NHL (show RTEL1 Antibodies).
The rs3740199 polymorphism in the ADAM12 gene was associated with knee osteoarthritis genetic susceptibility.
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)