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Cow (Bovine) Polyclonal AGXT2 Primary Antibody for WB - ABIN2783579
Baker, Cramer, Kennedy, Assimos, Holmes: Glycolate and glyoxylate metabolism in HepG2 cells. in American journal of physiology. Cell physiology 2004
Human Polyclonal AGXT2 Primary Antibody for ICC, IF - ABIN4278743
Kittel, Müller, König, Mieth, Sticht, Zolk, Kralj, Heinrich, Fromm, Maas: Alanine-glyoxylate aminotransferase 2 (AGXT2) polymorphisms have considerable impact on methylarginine and β-aminoisobutyrate metabolism in healthy volunteers. in PLoS ONE 2014
We purified human AGXT2 from tissues of AGXT2 transgenic mice and demonstrated its ability to metabolize homoarginine to 6-guanidino-2-oxocaproic acid (GOCA). After incubation of HepG2 cells overexpressing AGXT2 with isotope-labeled homoarginine-d4 we were able to detect labeled GOCA in the medium
study in a well-characterized rheumatoid arthritis population did not show an association between serum concentrations of dimethylarginines and genetic variants of the AGXT2 gene.
AGXT2 rs37369 polymorphism is associated with increased risk for chronic heart failure, which may due to distinct disparities of alleles in asymmetric dimethylarginine degradation
Single nucleotide polymorphism in AGXT2 gene is associated with renal dysfunction in patients with chronic heart failure.
The Alanine-glyoxylate aminotransferase 2 p.V498L polymorphism is associated with both paroxysmal and chronic forms of atrial fibrillation in coronary angiographic patients without structural heart disease in ultrasound, and earlier age at onset of ischemic stroke in patients undergoing exercise stress testing.
AGXT2 rs37369 polymorphism is associated with increased risk for CHD in smokers and in diabetes mellitus patients
The AGXT2 genotype may be an important factor underlying atherosclerosis.
The results of this study that the AGXT2 gene is not associated with schizophrenia in Japanese subjects.
SNPs of AGXT2 affect plasma as well as urinary BAIB.
AGXT2 has an important role in SDMA metabolism in humans and may additionally have an unanticipated role in the autonomic nervous system regulation of cardiac function.
Alanine-glyoxylate aminotransferase-2 metabolizes endogenous methylarginines, regulates NO, and controls blood pressure.
mitochondrially localized human AGXT2 is able to effectively metabolize ADMA in vivo resulting in decreased ADMA levels and improved endothelial NO production.
Discusses the cloning of the rat gene.
this study shows that diabetes-linked transcription factor HNF4alpha regulates maminotransferase 2etabolism of endogenous methylarginines and beta-aminoisobutyric acid by controlling expression of alanine-glyoxylate
we experimentally proved the presence of a new pathway of homoarginine catabolism - its transamination by AGXT2 with formation of GOCA and demonstrated that endogenous AGXT2 is required for maintenance of homoarginine levels in mice.
In this work, we describe an assay for the AGXT2 activity in mouse liver and kidney tissue. The overall production rates of DMGV-d(6) in mice were 195.37 pmol/min/mg total protein in liver and 85.21 pmol/min/mg total protein in kidney tissue.
The protein encoded by this gene is a class III pyridoxal-phosphate-dependent mitochondrial aminotransferase. It catalyzes the conversion of glyoxylate to glycine using L-alanine as the amino donor.
, alanine--glyoxylate aminotransferase 2, mitochondrial
, beta-ALAAT II
, beta-alanine-pyruvate aminotransferase
, AGT 2
, alanine-glyoxylate aminotransferase 2