1110014J22Rik, Acy-1, Acy1

For Research Use Only. Not for use in diagnostic procedures.

Human Cells

> 95 % as determined by SDS-PAGE

Lyophilized from sterile PBS, pH 7.4

Samples are stable for up to twelve months from date of receipt at -70 degree C

Manufactured in an ISO 9001:2015 Certified Laboratory.

Small volumes of ACY1 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Background: Aminoacylase 1 (ACY1), a metalloenzyme that removes amide-linked ACY1 groups from amino acids and may play a role in regulating responses to oxidative stress. Both the C-terminal fragment found in the two-hybrid screen and full-length ACY1 co-immunoprecipitate with SphK1. Though both C-terminal and full-length proteins slightly reduce SphK1 activity measured in vitro, the C-terminal fragment inhibits while full-length ACY1 potentiates the effects of SphK1 on proliferation and apoptosis. It suggested that ACY1 physically interacts with SphK1 and may influence its physiological functions. As a homodimeric zinc-binding enzyme, Aminoacylase 1 catalyzes the hydrolysis of N alpha-acylated amino acids. Deficiency of Aminoacylase 1 due to mutations in the Aminoacylase 1 (ACY1) gene follows an autosomal-recessive trait of inheritance and is characterized by accumulation of N-acetyl amino acids in the urine.

Description: A DNA sequence encoding the mouse ACY1 (Q99JW2) (Met 1-Ser 408) was expressed with a C-terminal polyhistidine tag.

The recombinant mouse ACY1 consists of 402 amino acids and has a calculated molecular mass of 45 kDa as estimated by SDS-PAGE under reducing conditions.

45,781 Da

aminoacylase 1

aminoacylase-1

Aminoacylase-1

ACY-1??[Similar Products]

ACY1: Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate). Defects in ACY1 are the cause of aminoacylase-1 deficiency (ACY1D). ACY1D results in a metabolic disorder manifesting with encephalopathy, unspecific psychomotor delay, psychomotor delay with atrophy of the vermis and syringomyelia, marked muscular hypotonia or normal clinical features. Epileptic seizures are a frequent feature. All affected individuals exhibit markedly increased urinary excretion of several N-acetylated amino acids. Belongs to the peptidase M20A family.

Protein type: Amino Acid Metabolism - arginine and proline; EC 3.5.1.14; Hydrolase

Chromosomal Location of Human Ortholog: 9 F1|9 57.49 cM

Molecular Function: aminoacylase activity; zinc ion binding

Biological Process: peptide catabolic process; proteolysis

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