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Human Polyclonal MAT1A Primary Antibody for IHC (p), WB - ABIN656632
Bing, Zhu, Yu, Li, Liu, Li, Wang, Qi, Guo, Yuan, He, Liu, Liu: Glucocorticoid-induced S-adenosylmethionine enhances the interferon signaling pathway by restoring STAT1 protein methylation in hepatitis B virus-infected cells. in The Journal of biological chemistry 2014
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Human Polyclonal MAT1A Primary Antibody for ICC, IF - ABIN4332790
Yang, Cho, Li, Peng, Ko, Mato, Lu: MicroRNAs regulate methionine adenosyltransferase 1A expression in hepatocellular carcinoma. in The Journal of clinical investigation 2013
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Cow (Bovine) Polyclonal MAT1A Primary Antibody for WB - ABIN2776786
Oh, Yang, Hahn, Kim, Byun, Jeon, Kim, Song, Noh, Kim, Yoo, Kim, Kim: Transcriptome analysis of human gastric cancer. in Mammalian genome : official journal of the International Mammalian Genome Society 2005
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Human Polyclonal MAT1A Primary Antibody for WB - ABIN5664106
Song, Li, Wang, Du, Yang: DMBA acts on cumulus cells to desynchronize nuclear and cytoplasmic maturation of pig oocytes. in Scientific reports 2018
Increased MAT1A expression is associated with recurrence in hepatocellular carcinoma.
interplay between MATalpha1, c-Myc, and Maf proteins, and their deregulation during chronic cholestasis may facilitate cholangiocarcinoma oncogenesis
Of the 22 single nucleotide polymorphisms studied, the rs8193 polymorphism lying in the micro-RNA binding site of 3'-UTR of CD44 was significantly (P=.0270) associated with RT-induced adverse skin reactions. Generalized multifactor dimensionality reduction analysis showed significant (P=.0107) gene-gene interactions between MAT1A and CD44.
A compound mutation of the methionine adenosyltransferase 1A (MAT1A) gene, c.345delA and c.529C>T, was identified in the patient, and His father and mother were found to be heterozygous for the c.345delA mutation and c.529C>T mutation, respectively.
S-adenosyl-L-methionine diminishes hepatitis C virus expression by altering MAT1A/2A signaling in hepatocytes.
5-Aza-CdR showed no effects on MAT2A methylation.
The mutations in the other 10 patients showed autosomal recessive inheritance and included eight novel MAT1A mutations.
Liver-specific isoenzyme MAT1A is genetically linked with an inborn metabolic disorder of hypermethioninemia, as well as a ubiquitously expressed isoenzyme MAT2A, whose enzymatic activity is regulated by an associated subunit MAT2B.
Methionine adenosyltransferase I/III deficiency is caused by mutations in the MAT1A gene. (Review)
upregulation of miR-664, miR-485-3p, and miR-495 contributes to lower MAT1A expression in HCC, and enhanced tumorigenesis may provide potential targets for HCC therapy.
Report SNPs that are highly associated with hepatic GNMT protein expression and the coordinate regulation of MAT1A levels.
we found for the first time a post-transcriptional regulation of MAT1A and MAT2A by AUF1 and HuR in hepatocellular carcinoma.
Human Dead-box protein 3 (DDX3X), a RNA helicase regulating RNA splicing, export, transcription and translation was down-regulated upon MAT1A expression.
genetic variant MAT1A 3U1510 displayed a significant interaction with dietary n-3:n-6 polyunsaturated fatty acids ratio in determining plasma homocysteine
Coexpression of MAT2A and MAT2B in COS-1 cells resulted in significantly increased MAT enzyme activity.
Methylation of the MAT1A coding region can inhibit gene transcription. This represents a key mechanism for decreased MAT1A expression in hepatocellular carcinoma.
Results show a rather high frequency of hypermethioninaemia due to MAT I/III deficiency (MAT1A dominant mutation) in the Galician neonatal population.
MAT and tripolyphosphatase (PPPase) activities of 18 MAT1A variants, six of them novel, and none of them previously assayed for activity. With the exception of G69S and Y92H, all recombinant proteins showed impairment (usually severe) of MAT activity.
expression of the MAT1A gene is mediated by C/EBP and is indirectly upregulated by T(3) in hepatoma cell lines
MAT1A variants were strongly associated with hypertension and stroke; improving folate and vitamin B-6 status may decrease cardiovascular disease risk of only a subset of the population, depending on genotype.
MAT1A is required for normal VLDL assembly and plasma lipid homeostasis in mice. Impaired VLDL synthesis, mainly due to SAMe deficiency, contributes to NAFLD development in MAT1A-KO mice.
DUSP1 mRNA and protein levels are lower in Mat1a knockout livers and fall rapidly in cultured hepatocytes.
Spontaneous oxidative stress and liver tumors in mice lacking methionine adenosyltransferase 1A
MAT1A knockout hepatocytes have more baseline DNA synthesis but no mitogenic response to hepatocyte growth factor. MAT1A-produced SAMe has a major role in ERK signaling & cyclin D1 regulation during liver regeneration & mitogenic signal response.
Mat1a(-/-) mice have expansion of liver stem cells as they age. These cells have increased expression of several oncogenes and are tumorigenic in vivo.
C/EBPbeta plays an important role in epigenetic regulation of the mature hepatic gene MAT1A
By 1 month of age, genomic instability increases in livers of Mat1a knockout mice, possibly due to reduced APEX1 levels
CD133(+)CD45(-) oval cells isolated from premalignant 16-month-old Mat1a(-/-) mice demonstrated significant resistance to transforming growth factor-beta-induced apoptosis compared to CD133(-) cells.
This gene catalyzes a two-step reaction that involves the transfer of the adenosyl moiety of ATP to methionine to form S-adenosylmethionine and tripolyphosphate, which is subsequently cleaved to PPi and Pi. S-adenosylmethionine is the source of methyl groups for most biological methylations. The encoded protein is found as a homotetramer (MAT I) or a homodimer (MAT III) whereas a third form, MAT II (gamma), is encoded by the MAT2A gene. Mutations in this gene are associated with methionine adenosyltransferase deficiency.
, S-adenosylmethionine synthase isoform type-1
, S-adenosylmethionine synthetase isoform type-1
, adoMet synthase 1
, adoMet synthetase 1
, methionine adenosyltransferase 1
, methionine adenosyltransferase I/III
, S - adenosylmethionine synthetase