Mouse ASAHL/N-acylethanolamine-hydrolyzing Acid A Antibody Summary
Val33-Ser362
Accession # AAH04572
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data

Detection of Mouse N-acylethanolamine-hydrolyzing Acid Amidase/ASAHL by Western Blot. Western blot shows lysates of mouse lung tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Mouse N-acylethanolamine-hydrolyzing Acid Amidase/ASAHL Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4886) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for N-acylethanolamine-hydrolyzing Acid Amidase/ASAHL at approximately 30 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.
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Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: ASAHL/N-acylethanolamine-hydrolyzing Acid Amidase
The mouse 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 choloylglycine hydrolase family of enzymes, and is structurally similar to acid ceramidase (1). NAAA is both a lysosomal and a secreted enzyme, and like acid ceramidase, has been observed to be proteolytically processed during maturation (1). Through its amidase activity, ASAHL may play a role in the termination of the actions of a variety of N-acylethanolamides (3). NAAA can be distinguished from anandamide amidohydrolase by its lack of inhibition by methyl arachidonoyl fluorophosphonate (2).
- Tsuboi, K. et al. (2005) J. Biol. Chem. 280:11082.
- Ueda, N. et al. (2001) J. Biol. Chem. 276:35552.
- Sun, Y. X. et al. (2005) Biochim. Biophys. Acta 1736:211.
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