|Application ||WB, E|
|Calculated MW||40066 Da|
|Antigen Region||331-359 aa|
|Other Names||N-acylethanolamine-hydrolyzing acid amidase, 351-, Acid ceramidase-like protein, N-acylsphingosine amidohydrolase-like, ASAH-like protein, N-acylethanolamine-hydrolyzing acid amidase subunit alpha, N-acylethanolamine-hydrolyzing acid amidase subunit beta, NAAA, ASAHL, PLT|
|Target/Specificity||This NAAA antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 331-359 amino acids from the C-terminal region of human NAAA.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||NAAA Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Degrades bioactive fatty acid amides to their corresponding acids, with the following preference: N- palmitoylethanolamine > N-myristoylethanolamine > N- lauroylethanolamine = N-stearoylethanolamine > N- arachidonoylethanolamine > N-oleoylethanolamine. Also exhibits weak hydrolytic activity against the ceramides N- lauroylsphingosine and N-palmitoylsphingosine.|
|Tissue Location||Expressed in numerous tissues, with highest levels in liver and kidney, followed by pancreas|
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Provided below are standard protocols that you may find useful for product applications.
This gene encodes an N-acylethanolamine-hydrolyzing enzyme which is highly similar to acid ceramidase. Multiple transcript variants encoding different isoforms have been found for this gene.
Wang, J., et al. J. Biochem. 144(5):685-690(2008)
Muller, T.D., et al. Child Adolesc Psychiatry Ment Health 2 (1), 33 (2008) :
Schulze, H., et al. Biol. Chem. 388(12):1333-1343(2007)
Zhao, L.Y., et al. Biochim. Biophys. Acta 1771(11):1397-1405(2007)
Oh, J.H., et al. Mamm. Genome 16(12):942-954(2005)
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