P3584

L-α-Phosphatidyl-D-myo-inositol 4,5-diphosphate, dioctanoyl

Name: <SC>L</SC>-α-Phosphatidyl-<SC>D</SC>-<I>myo</I>-inositol 4,5-diphosphate, dioctanoyl
Brand: SIGMA

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Über diesen Artikel

Empirische Formel (Hill-System):

C₂₅H₄₉O₁₉P₃

CAS-Nummer:

204858-53-7

Molekulargewicht:

746.57

NACRES:

NA.77

PubChem Substance ID:

24898428

UNSPSC Code:

12352207

MDL number:

MFCD02259161

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InChI

1S/C25H49O19P3/c1-3-5-7-9-11-13-18(26)39-15-17(41-19(27)14-12-10-8-6-4-2)16-40-47(37,38)44-23-20(28)21(29)24(42-45(31,32)33)25(22(23)30)43-46(34,35)36/h17,20-25,28-30H,3-16H2,1-2H3,(H,37,38)(H2,31,32,33)(H2,34,35,36)/t17-,20-,21+,22+,23-,24-,25-/m1/s1

SMILES string

CCCCCCCC(=O)OC[C@H](COP(O)(=O)O[C@@H]1[C@H](O)[C@H](O)[C@@H](OP(O)(O)=O)[C@H](OP(O)(O)=O)[C@H]1O)OC(=O)CCCCCCC

InChI key

XLNCEHRXXWQMPK-MJUMVPIBSA-N

form

powder

solubility

H₂O: soluble

storage temp.

−20°C

Quality Level

100

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Dieser Artikel	I9766	P7686	P3953
Sigma-Aldrich P3584 L-α-Phosphatidyl-D-myo-inositol 4,5-diphosphate, dioctanoyl	Sigma-Aldrich I9766 D-myo-Inositol 1,4,5-tris-phosphate trisodium salt	Sigma-Aldrich P7686 L-α-Phosphatidyl-D-myo-inositol 4-monophosphate, dipalmitoyl ammonium salt	Sigma-Aldrich P3953 L-α-Phosphatidyl-D-myo-inositol 3-monophosphate, dipalmitoyl
solubility H₂O: soluble	solubility H₂O: soluble	solubility DMSO: soluble, chloroform: soluble, ethanol: soluble	solubility DMSO: soluble, chloroform: soluble, ethanol: soluble
form powder	form powder	form solid	form -
storage temp. −20°C	storage temp. −20°C	storage temp. −20°C	storage temp. −20°C
Quality Level 100	Quality Level 300	Quality Level 200	Quality Level -

General description

Signaling lipid which apparently acts by binding to pleckstrin homology domains; direct activator of inward rectifier potassium channels; phospholipase C and PI3-kinase substrate; activates phospholipase D.

Features and Benefits

This compound is featured on the Potassium Channels page of the Handbook of Receptor Classification and Signal Transduction. To browse other handbook pages, click here.

Lagerklasse

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Glycoprotein D of HSV-1 is dependent on tegument protein UL16 for packaging and contains a motif that is differentially required for syncytia formation.

Jillian C Carmichael et al.

Virology, 527, 64-76 (2018-11-23)

Glycoprotein D (gD) of herpes simplex virus type 1 (HSV-1) plays a key role in multiple events during infection including virus entry, cell-to-cell spread, and virus-induced syncytia formation. Here, we provide evidence that an arginine/lysine cluster located at the transmembrane-cytoplasm

Direct activation of inward rectifier potassium channels by PIP2 and its stabilization by Gbetagamma.

C L Huang et al.

Nature, 391(6669), 803-806 (1998-03-05)

Inward rectifier K+ channels, which modulate electrical activity in many cell types, are regulated by protein kinases, guanine-nucleotide-binding proteins (G proteins) and probably actin cytoskeleton. Generation of phosphatidylinositol 4,5-bisphosphate (PIP2) by ATP-dependent lipid kinases is known to activate inward rectifier

Pleckstrin homology domain-mediated membrane association and activation of the beta-adrenergic receptor kinase requires coordinate interaction with G beta gamma subunits and lipid.

J A Pitcher et al.

The Journal of biological chemistry, 270(20), 11707-11710 (1995-05-19)

The pleckstrin homology (PH) domain is an approximately 100-amino-acid region of sequence homology present in numerous proteins of diverse functions, which forms a discrete structural module. Several ligands capable of binding to PH domain-containing proteins have been identified including phosphatidylinositol

Structural characterization of the interaction between a pleckstrin homology domain and phosphatidylinositol 4,5-bisphosphate.

J E Harlan et al.

Biochemistry, 34(31), 9859-9864 (1995-08-08)

The pleckstrin homology (PH) domain is a protein module of approximately 100 amino acids that is found in several proteins involved in signal transduction [for a recent review, see Gibson et al. (1994) Trends Biochem. Sci. 19, 349-353]. Although the

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