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Dog (Canine) Polyclonal AGXT Primary Antibody für ELISA - ABIN451791
Hoshino, Kühne, Filjak, Kröger: Regulation and characterization of L-serine: pyruvate aminotransferase in rat liver cytosol and mitochondria. in Zeitschrift fur Naturforschung. Section C, Biosciences 1977
Human Polyclonal AGXT Primary Antibody für IHC, IHC (p) - ABIN4278741
Castello, Borzone, DAria, Annunziata, Piccolo, Brunetti-Pierri: Helper-dependent adenoviral vectors for liver-directed gene therapy of primary hyperoxaluria type 1. in Gene therapy 2016
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 (zeige PLP1 Antikörper)) but does not display catalytic activity.
Letter/Case Report: novel missense AGXT gene mutation in a Sri (zeige SRI Antikörper) 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
The pathogenic mutation G47R causes misfolding of alanine:glyoxylate aminotransferase.
A review of the current knowledge of the biochemical properties of liver peroxisomal alanine:glyoxylate aminotransferase and of the molecular defects caused by single point mutations associated with Primary Hyperoxaluria Type 1.
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 1
, serine--pyruvate aminotransferase, mitochondrial
, serine--pyruvate aminotransferase, peroxisomal
, angiotensin receptor 2
, serine:pyruvate aminotransferase SPT
, serine:pyruvate/alanine:glyoxylate aminotransferase
, alanine:glyoxylate aminotransferase