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anti-Human MTAP Anticorps:
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Human Polyclonal MTAP Primary Antibody pour WB - ABIN1881557
Newton-Bishop, Chang, Iles, Taylor, Bakker, Chan, Leake, Karpavicius, Haynes, Fitzgibbon, Elliott, Kanetsky, Harland, Barrett, Bishop: Melanocytic nevi, nevus genes, and melanoma risk in a large case-control study in the United Kingdom. dans Cancer epidemiology, biomarkers & prevention : a publication of the American Association for Cancer Research, cosponsored by the American Society of Preventive Oncology 2010
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Human Monoclonal MTAP Primary Antibody pour IF, ELISA - ABIN561859
Rose, Poliseno, Wang, Clark, Pearlman, Wang, Vega Y Saenz de Miera, Medicherla, Christos, Shapiro, Pavlick, Darvishian, Zavadil, Polsky, Hernando, Ostrer, Osman: Integrative genomics identifies molecular alterations that challenge the linear model of melanoma progression. dans Cancer research 2011
The SNP rs7023954 of methylthioadenosine phosphorylase co-dominantly expressed alleles revealed no difference in the conversion rate of 5'-methylthioadenosine to adenine and 5-methylthioribose-1-phosphate, indicating that this known enzymatic activity does not modulate the tumor suppressive function of methylthioadenosine phosphorylase.
Data demonstrate that MTAP deficiency leads to accumulation of MTA (Montrer DNMT1 Anticorps) inducing deregulation of central cellular pathways that control cell fate and contributes to the onset of a proliferative and antiapoptotic phenotype in the liver.
methionine adenosyltransferase II alpha (MAT2A (Montrer MAT2A Anticorps)), and the arginine methyltransferase, PRMT5 (Montrer PRMT5 Anticorps), as vulnerable enzymes in cells with MTAP deletion.
MTAP expression was significantly higher in Luminal-A breast tumors than in triple negative breast neoplasms, suggesting the lack of expression in more aggressive breast tumors.
study to describe MTAP expression in a series of Pilocytic astrocytomas and relate it to the clinicopathological features of the patients; found MTAP expression is retained in Pilocytic astrocytomas and is not an outcome predictor for these tumors
MTAP deficiency was predictive of worse disease-specific survival and distant metastasis-free survival, suggesting its role in disease progression and as an independent prognostic biomarker of nasopharyngeal carcinoma
In the MTAP-deficient cases, the homozygous deletion of MTAP predicted adverse outcome. In MTAP-deficient cells, MTAP reexpression inhibited cell migration and invasion, proliferation and anchorage-independent colony formation and downregulated cyclin D1 (Montrer CCND1 Anticorps).
MTAP expression is an independent prognostic factor and has greater prognostic significance than p16 (Montrer CDKN2A Anticorps) expression in non-small cell lung cancer and concordant loss of MTAP and p16 (Montrer CDKN2A Anticorps) expression indicates poor outcomes in lung cancer patients.
MTAP-mediated regulation of methylthioadenosine links polyamine metabolism with NF-kappaB (Montrer NFKB1 Anticorps) activation and apoptosis in hepatic stellate cells.
SNP rs10118757 was associated with CAD (Montrer CAD Anticorps) risk in a Chinese Han population, indicating that MTAP gene may play a potential role in the pathophysiological process of CAD (Montrer CAD Anticorps).
Germline Mutations in Mtap is associated with lymphomagenesis.
Regulation of MTAP by reactive oxygen species might participate in the redox regulation of the methionine catabolic pathway in the liver
Studies show that Mtap is a tumor suppressor gene independent of CDKN2A (Montrer CDKN2A Anticorps) and ARF (Montrer CDKN2A Anticorps).
This gene encodes an enzyme that plays a major role in polyamine metabolism and is important for the salvage of both adenine and methionine. The encoded enzyme is deficient in many cancers because this gene and the tumor suppressor p16 gene are co-deleted. Multiple alternatively spliced transcript variants have been described for this gene, but their full-length natures remain unknown.
, 5'-methylthioadenosine phosphorylase
, MTA phosphorylase
, MeSAdo phosphorylase
, S-methyl-5'-thioadenosine phosphorylase