To block protein-antibody complex formation during immunochemical analysis of NAPE-PLD
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NAPE-PLD Blocking Peptide (aa 159-172)

Item No. 10303

Technical Information
200 µg of peptide lyophilized from from 200 µl water
Shipping & Storage Information
Storage
-20°C
Shipping
Wet ice in continental US; may vary elsewhere
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    Product Description

    To be used in conjunction with Cayman’s NAPE-PLD (Internal) Polyclonal Antibody (Item No. 10305) to block protein-antibody complex formation during analysis of NAPE-PLD. N-Acylethanolamines (NAEs) are involved in diverse biological processes such as inflammatory regulation, apoptosis, and tissue degeneration.1 In animals, NAEs are mainly biosynthesized via a membrane phospholipid-dependent pathway, which is the enzymatic hydrolysis of N-acyl-phosphatidylethanolamine (NAPE). The enzyme catalyzing this reaction is a phospholipase D (PLD) subtype selective for NAPE named N-acylphosphatidylethanolamine-hydrolysing PLD (NAPE-PLD). It has been cloned from mouse, rat, and human and is 393-396 amino acids in length, with an estimated molecular weight of 46 kDa. Both NAPE-PLD mRNA and protein activity have been detected in a wide range of tissues with the highest levels in brain, kidney, and testis.2 In rat, NAPE-PLD activity in the brain is low in neonates and is 15-fold higher in adults, whereas the activity remains constant in the heart during development.3

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Hansen, H.S., Moesgaard, B., Petersen, G., et alPutative neuroprotective actions of N-acyl-ethanolamines. Pharmacol. Ther. 95(2), 119-126 (2002).

    2. Okamoto, Y., Morishita, J., Tsuboi, K., et alMolecular characterization of a phospholipase D generating anandamide and its congeners. The Journal of Biological Chemisty 279(7), 5298-5305 (2004).

    3. Moesgaard, B., Petersen, G., Jaroszewski, J.W., et alAge dependent accumulation of N-acyl-ethanolamine phospholipids in ischemic rat brain: A 31P NMR and enzyme activity study. J. Lipid Res. 41(6), 985-990 (2000).