L3295
Phospholipase A1 from Aspergillus oryzae
Synonym(e):
Lecitase™ Ultra, PLA1
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About This Item
Empfohlene Produkte
Rekombinant
expressed in Aspergillus oryzae
Qualitätsniveau
Form
liquid
Spezifische Aktivität
≥10 KLU/g
Lagertemp.
2-8°C
Allgemeine Beschreibung
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).
Anwendung
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)
Hinweis zur Analyse
minimum activity 10 KLU/G liquid
Rechtliche Hinweise
Lecitase is a trademark of Novozymes Corp.
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 1
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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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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Specific enrichment of 2-arachidonoyl-lysophosphatidylcholine in carotid atheroma plaque from type 2 diabetic patients
Menegaut L, et al.
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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)
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