P4912
Phospholipase D from Streptomyces sp.
Type VII, lyophilized powder, ≥150 units/mg solid
Synonym(e):
Lecithinase D, Phosphatidylcholine phosphatidohydrolase
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About This Item
Empfohlene Produkte
Biologische Quelle
Streptomyces sp.
Qualitätsniveau
Typ
Type VII
Form
lyophilized powder
Spezifische Aktivität
≥150 units/mg solid
Lagertemp.
−20°C
Anwendung
Phospholipase D (PLD) has been used to hydrolyze the phosphate bonds of phospholipids and sphingomyelin to yield the corresponding phosphatidic acid. It has also been used to study metabolic labeling and direct imaging of choline phospholipids in vivo by measuring propargyl-Cho incorporation. Furthermore, PLD has been used in purification and kinetic studies.
The enzyme from Sigma has been used in the translocation of sphingosine kinase 1 (SK1) to membrane fractions under in vitro conditions. It has also been used to produce phosphatidic acid (PA) from phosphatidylcholine (PC) in HL60 permeabilized cells.
Biochem./physiol. Wirkung
Phospholipase D is glycerophospholipid-specific. It is markedly less active on sphingomyelins and lysophospholipids. Phospholipase D hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Hydrolyzes the phosphate bonds of phospholipids and sphingomyelin to give the corresponding phosphatidic acid.
Verpackung
Bottomless glass bottle. Contents are inside inserted fused cone.
Einheitendefinition
One unit will liberate 1.0 μmole of choline from 1,2-Dioleoyl-sn-glycero-3-phosphocholine per hour at pH 8.0 at 37 °C.
Hinweis zur Analyse
Protein by biuret
Inhibitor
Produkt-Nr.
Beschreibung
Preisangaben
Signalwort
Danger
H-Sätze
P-Sätze
Gefahreneinstufungen
Resp. Sens. 1
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Analysenzertifikate (COA)
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Mohamed H Yaghmour et al.
Journal of lipid research, 62, 100022-100022 (2021-01-17)
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The Journal of biological chemistry, 287(38), 32263-32276 (2012-07-24)
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Christine Delon et al.
The Journal of biological chemistry, 279(43), 44763-44774 (2004-08-18)
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