Aminoacylase-1 is a cytosolic, homodimeric, zinc-binding enzyme that catalyzes the hydrolysis of acylated L-amino acids to L-amino acids and acyl group, and has been postulated to function in the catabolism and salvage of acylated amino acids. ACY1 has been assigned to 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 ACY1 is the first member of a new family of zinc-binding enzymes.
ACY1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 428 amino acids (1-408 a.a.) and having a molecular mass of 48kDa. The ACY1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
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