ASAHL, Recombinant, Human (N-Acylsphingosine Amidohydrolase-like)

The human ASAHL gene encodes N-acylethanolamine-hydrolyzing acid amidase (NAAA), a fatty acid amidase with maximal activity at acidic pH (1). NAAA hydrolyzes a number of N-acyl ethanolamines, including N-myristoyl-, N-stearoyl, N-oleoyl, and N-arachidonoyl, but is most active against N-palmitoylethanolamine (2). NAAA is a member of the cholylglycine hydrolase family of enzymes, and is structurally similar to acid ceramidase (3). NAAA is both a lysosomal and a secreted enzyme, and like acid ceramidase, has been observed to be proteolytically processed during maturation (3). NAAA can be distinguished from anandamide amidohydrolase by its lack of inhibition by methyl arachidonyl fluorophosphonate (2).\n\nRecombinant human N-acylethanolamine-hydrolyzing acid amidase (NAAA) encoded by the ASAHL gene (rhASAHL; amino acid residues 1-359; Accession # Q02083; variant V151I) was expressed with a C-terminal 10X His tag in a Chinese Hamster Ovary cell line.\n\nCalculated molecular mass of 39kD and migrates as a 50kD band in SDS-PAGE under reducing conditions. Fragments of 33 and 2 kD, resulting from proteolytic processing during maturation, are also present.\n\nActivity: Measured by its ability to hydrolyze the substrate N-palmitoylethanolamide into palmitate and ethanolamine. \n\nStorage and Stability:\nMay be stored at 4 degrees C for short-term only. For long-term storage, store at -20 degrees C. Aliquots are stable for at least 6 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

A3597-42H

Size

10ug

Form

Supplied as a liquid in 25mM MES, 0.5M sodium chloride, pH 6.5.

Purity

(same/more than) 95%, as determined by SDS-PAGE and visualized by silver stain.\nEndotoxin: (same/less than) 1.0 EU/1 ug.

References

1. Hong, S.B.. et al., 1999, Genomics 62:232 - 241.\n2. Ueda, N.. et al., 2001, J. Biol. Chem. 276:35552 - 35557.\n3. Tsuboi, K.. et al., 2005, J. Biol. Chem. 280:11082 - 11092.