ACY1D, ACYLASE, ACY1

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

Baculovirus-Insect Cells

> 95 % as determined by SDS-PAGE

Lyophilized from sterile 50mM Tris, 100mM NaCl, pH 8.0, 10% glycerol

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 full length of human ACY1 (NP_000657.1) (Met 1-Ser 408) was expressed with a polyhistidine tag at the C-terminus.

The recombinant human ACY1 consists of 419 amino acids and predicts a molecular mass of 47.3 kDa. It migrates as an approximately 44 kDa protein in SDS-PAGE under reducing conditions.

42,195 Da

aminoacylase 1

aminoacylase-1

Aminoacylase-1

ACY-1??[Similar Products]

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. [provided by RefSeq, Nov 2010]

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: 3p21.2

Cellular Component: cytosol

Molecular Function: aminoacylase activity; identical protein binding; protein binding; zinc ion binding

Biological Process: peptide catabolic process; xenobiotic metabolic process

Disease: Aminoacylase 1 Deficiency

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