L3295
Phospholipase A1 from Aspergillus oryzae
Synonyme(s) :
Lecitase™ Ultra, PLA1
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About This Item
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54
Produits recommandés
Produit recombinant
expressed in Aspergillus oryzae
Niveau de qualité
Forme
liquid
Activité spécifique
≥10 KLU/g
Température de stockage
2-8°C
Description générale
Phospholipase A1 (PLA1) catalyzes the hydrolysis of acyl group from position 1 of lecithin to yield lysolecithin. It is expressed in a wide range of organisms such as rat platelets, bovine brain and testis, hornet venom, bonito muscle and fungi. Gene coding for PLA1 consists of four exons and three short introns spanning 1,056bp of genomic DNA. Mature protein contains 269 aminoacids and two possible N-glycosylation sites (Asn27 and Asn55).
Application
Phospholipase A1 from Aspergillus oryzae has been used:
- in the preparation of sn-1 and sn-2 C18:1- lysophosphatidylcholine (LPC) regioisomer standards
- as a catalyst for the synthesis 6-O-glucosyl-poly(3-hydroxyalkanoates) in a micro-aqueous system
- to catalyze the synthesis of methyl butanoate and methyl benzoate flavor esters in continuous flow microreactor
- to hydrolyze 17:0 phosphocholine (PC)
Remarque sur l'analyse
minimum activity 10 KLU/G liquid
Informations légales
Lecitase is a trademark of Novozymes Corp.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
C Preston Moon et al.
Proceedings of the National Academy of Sciences of the United States of America, 108(25), 10174-10177 (2011-05-25)
The transfer free energies of the twenty natural amino acid side chains from water to phospholipid bilayers make a major contribution to the assembly and function of membrane proteins. Measurements of those transfer free energies will facilitate the identification of
Structure and function of phosphatidylserine-specific phospholipase A1
Aoki J, et al.
Biochimica et Biophysica Acta, 1582(1-3), 26-32 (2002)
Yuh-Ren Chen et al.
Archives of microbiology, 193(6), 419-428 (2011-03-10)
The lysis protein of the colicinogenic operon is essential for colicin release and its main function is to activate the outer membrane phospholipase A (OMPLA) for the traverse of colicin across the cell envelope. However, little is known about the
Enzymatic synthesis of 6-O-glucosyl-poly (3-hydroxyalkanoate) in organic solvents and their binary mixture
Gumel AM, et al.
International Journal of Biological Macromolecules (2013)
Nicole A Housley et al.
Journal of bacteriology, 193(18), 4634-4642 (2011-07-19)
Here we have characterized the Rickettsia prowazekii RP534 protein, a homologue of the Pseudomonas aeruginosa ExoU phospholipase A (PLA) secreted cytotoxin. Our studies showed that purified recombinant RP534 PLA possessed the predicted PLA(2) and lyso-PLA(2) activities based on what has
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