P4912
Phospholipase D from Streptomyces sp.
Type VII, lyophilized powder, ≥150 units/mg solid
Sinônimo(s):
Lecithinase D, Phosphatidylcholine phosphatidohydrolase
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About This Item
Produtos recomendados
fonte biológica
Streptomyces sp.
Nível de qualidade
tipo
Type VII
forma
lyophilized powder
atividade específica
≥150 units/mg solid
temperatura de armazenamento
−20°C
Aplicação
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.
Ações bioquímicas/fisiológicas
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.
Embalagem
Bottomless glass bottle. Contents are inside inserted fused cone.
Definição da unidade
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.
Nota de análise
Protein by biuret
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Equipamento de proteção individual
Eyeshields, Gloves, type N95 (US)
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The Journal of biological chemistry, 279(43), 44763-44774 (2004-08-18)
Sphingosine kinase 1 (SK1) phosphorylates sphingosine to generate sphingosine 1-phosphate (S1P). Because both substrate and product of the enzyme are potentially important signaling molecules, the regulation of SK1 is of considerable interest. We report that SK1, which is ordinarily a
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