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AGXT is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Additionally we are shipping Alanine Glyoxylate Aminotransferase Proteins (8) and Alanine Glyoxylate Aminotransferase Kits (5) and many more products for this protein.
Showing 10 out of 84 products:
Human Monoclonal AGXT Primary Antibody for EIA, IF - ABIN452656
Donini, Ferrari, Fedeli, Faini, Lamberto, Marletta, Mellini, Panini, Percudani, Pollegioni, Caldinelli, Petrucco, Peracchi: Recombinant production of eight human cytosolic aminotransferases and assessment of their potential involvement in glyoxylate metabolism. in The Biochemical journal 2009
Show all 3 references for ABIN452656
Human Polyclonal AGXT Primary Antibody for FACS, IHC (p) - ABIN390393
Cellini, Montioli, Paiardini, Lorenzetto, Voltattorni: Molecular Insight into the Synergism between the Minor Allele of Human Liver Peroxisomal Alanine:Glyoxylate Aminotransferase and the F152I Mutation. in The Journal of biological chemistry 2009
Show all 2 references for ABIN390393
Human Polyclonal AGXT Primary Antibody for EIA, WB - ABIN452724
Bertoldi, Cellini, Paiardini, Montioli, Borri Voltattorni: Reactions of human liver peroxisomal alanine:glyoxylate aminotransferase with beta-chloro-L-alanine and L-cysteine: spectroscopic and kinetic analysis. in Biochimica et biophysica acta 2008
Show all 2 references for ABIN452724
Human Polyclonal AGXT Primary Antibody for 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
Letter/Case Report: novel missense AGXT gene mutation in a Sri (show SRI Antibodies) 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.
S81L and G170R mutations of AGT is associated with Primary Hyperoxaluria type I in homozygosis and heterozygosis.
AGT missense mutations associated with Primary Hyperoxaluria Type 1, were characterized.
Data suggest that dequalinium chloride (DECA) may be a pharmacologic strategy to treat primary hyperoxaluria 1 (PH1) patients with mutations in alanine:glyoxylate aminotransferase (AGT).
These are the first cases of primary hyperoxaluria type 1 to be diagnosed by clinical manifestations and AGXT gene mutations in mainland China.
data imply that the AGT Pro11Leu polymorphism is not directly responsible for the low incidence of stone formation in black South Africans.
Modeling of the mutations on a 1.9 A crystal structure suggests that Primary hyperoxaluria type I causing mutants perturb locally the native structure of AGT.
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