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ACY1 encodes a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and an acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. De plus, nous expédions Aminoacylase 1 Anticorps (109) et Aminoacylase 1 Protéines (16) et beaucoup plus de produits pour cette protéine.
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with the elevated level in the disease progression of Chronic hepatitis B (CHB), ACY1 autoantibody may be a valuable serum biomarker for discriminating HBVrelated liver cirrhosis from CHB.
Biochemical analysis showed absence of ACY1 enzyme activity in the patient's fibroblasts.
ACY1 acts as a tumor suppressor in hepatocellular carcinoma.
Report serum aminoacylase-1 as a novel biomarker with potential prognostic utility for long-term outcome in renal transplant recipients with delayed graft function.
Case Report: ACY1-deficient patient presenting with autistic features.
We concluded that ACY1 expression in colorectal cancer varies with stage and appears to play a role in cell proliferation and apoptosis
These data suggest that aminoacylase expression is dysregulated in neuroblastoma.
aminoacylase 1 proteins with the mutations p.Arg378Trp, p.Arg378Gln and p.Arg393His were also detected in Western blot analysis
by complementing different active site mutants of human aminoacylase-1, study shows that catalysis occurs at the dimer interface
first report of a patient with aminoacylase I deficiency
Genetic deficiency of ACY1 leads to functional ACY1 deficiency and excretion of N-acetylated amino acids.
Because hK1 amidase activity is significantly lower in urine of systolic HF patients, it can be supposed that activity of renal kallikrein-kinin system may be suppressed in this systolic heart failure.
T347S variant of human Acy1 exhibited markedly increased catalytic efficiency against N-benzoylamino acids
Apo-aminoacylase followed similar rules as Holo-enzyme, which suggested the zinc ion may play more important roles on activity other than structure
Based on site-directed mutagenesis, homology modeling and substrate docking studies, a revised catalytic mechanism for porcine metalloenzyme aminoacylase 1 has been proposed.
This gene encodes a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and an acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. This gene is located on chromosome 3p21.1, a region reduced to homozygosity in small-cell lung cancer (SCLC), and its expression has been reported to be reduced or undetectable in SCLC cell lines and tumors. The amino acid sequence of human aminoacylase-1 is highly homologous to the porcine counterpart, and this enzyme is the first member of a new family of zinc-binding enzymes. Mutations in this gene cause aminoacylase-1 deficiency, a metabolic disorder characterized by central nervous system defects and increased urinary excretion of N-acetylated amino acids. Alternative splicing of this gene results in multiple transcript variants. Read-through transcription also exists between this gene and the upstream ABHD14A (abhydrolase domain containing 14A) gene, as represented in GeneID:100526760. A related pseudogene has been identified on chromosome 18.
, aminoacylase 1
, N-acyl-L-amino-acid amidohydrolase
, ACY IA
, ACY IB
, N-acylamino acid aminohydrolase (Aminoacylase 1)