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two novel AGXT missense mutations (p.M49L and p.N72I), which will enrich the AGXT mutation database and provide a better comprehension of PH1 pathogenesis, were identified in a big Chinese PH1 family. Significant morphological and structural difference of kidney stones from two siblings with the same genotype observed in this study displays the heterogeneity of genotype-phenotype correlation
AGXT mutational analysis was performed to confirm the diagnosis of PH1.
this study identifies a novel AGXT gene mutation in primary hyperoxaluria after kidney transplantation failure in Tunisian patient
AGXT gene sequencing is now the choice of diagnosis of Primary hyperoxaluria type 1 (PH1)due to its non-invasive nature compared to liver enzyme assay. Early diagnosis and accurate treatment in PH1 is important for better patient outcomes.
Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1.
Novel AGXT mutations in a Tunisian population with primary hyperoxaluria type 1.
The novel p.Gln137Hisfs*19 AGXT mutation detected in this study extends the spectrum of known primary hyperoxaluria type I AGXT gene mutations in Tunisia.
Data show that onomeric minor allele of human alanine glyoxylate aminotransferase (AGT-Mi) binds pyridoxal 5-phosphate (PLP (show PLP1 Proteins)) but does not display catalytic activity.
Letter/Case Report: novel missense AGXT gene mutation in a Sri (show SRI Proteins) Lankan family with primary hyperoxaluria type 1.
Primary hyperoxaluria type 1 (PH1) is due to a defect in the AGXT gene. The aim of our study was to analyze the mutations causing PH1 in the Moroccan population
AGT-deficient mice showed decreased vascular permeability, a readout of in vivo histamine activity.
expressed wild-type human AGT1 was predominantly localized in mouse hepatocellular peroxisomes, whereas the most common mutant form of AGT1 (G170R) was localized predominantly in the mitochondria
This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria.
L-alanine: glyoxylate aminotransferase 1
, alanine--glyoxylate aminotransferase
, hepatic peroxisomal alanine:glyoxylate aminotransferase
, serine--pyruvate aminotransferase
, serine-pyruvate aminotransferase
, serine:pyruvate aminotransferase
, alanine:glyoxylate aminotransferase
, angiotensin receptor 2
, serine--pyruvate aminotransferase, mitochondrial
, serine--pyruvate aminotransferase, peroxisomal
, serine:pyruvate aminotransferase SPT
, serine:pyruvate/alanine:glyoxylate aminotransferase
, alanine-glyoxylate aminotransferase 1
, LOW QUALITY PROTEIN: serine--pyruvate aminotransferase, mitochondrial
, alanine-glyoxylate aminotransferase
, putative alanine:glyoxylate aminotransferase
, alanine-glyoxylate aminotransferase b