Recombinant Human ACY-1 protein is a Human Full Length protein, in the 1 to 408 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application MS | Reactivity Reacts | Dilution info - | Notes - |
Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids.
Aminoacylase-1, ACY-1, N-acyl-L-amino-acid amidohydrolase, ACY1
Recombinant Human ACY-1 protein is a Human Full Length protein, in the 1 to 408 aa range, expressed in Escherichia coli, with >90% purity and suitable for SDS-PAGE, MS.
pH: 7.4
Constituents: PBS, 10% Glycerol (glycerin, glycerine)
ab99247 is purified using conventional chromatography techniques.
Catalyzes the hydrolysis of N-acetylated amino acids to acetate and free amino acids.
Belongs to the peptidase M20A family.
The protein ACY-1 also known as aminoacylase 1 or ACY plays a significant role in the deacetylation process of N-acyl amino acids. ACY-1 is a zinc-binding enzyme and has a molecular weight of approximately 45 kDa. This enzyme is expressed in various tissues including the liver and kidney. ACY-1 is essential for amino acid metabolism by catalyzing the hydrolysis of N-acyl-L-amino acids into L-amino acids and free fatty acids.
The aminoacylase 1 enzyme functions in detoxification and metabolic regulation. It is not typically part of large protein complexes but acts independently to regulate amino acid and acetyl-CoA pathways. The activity facilitates the recycling of acyl groups and amino acids which is important for maintaining cellular homeostasis.
Aminoacylase 1 is involved in amino acid catabolism and lipid metabolism pathways. In these processes ACY-1 interacts with proteins such as acetyl-CoA synthetase in the conversion of excess acyl-CoAs into free fatty acids and CoA preventing the build-up of toxic metabolites. It also has an indirect relationship with the urea cycle by ensuring the availability of free amino acids for further metabolism.
Alterations in ACY-1 function relate to neurological disorders and metabolic syndromes. For instance defects in ACY-1 have been associated with Canavan disease a condition affecting the brain. The protein's activity imbalance might also link to metabolic disorders where its interaction with proteins like aspartoacylase comes into play further affecting the acetylation status and metabolic regulation.
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15% SDS-PAGE using ab99247 (3μg).
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