InChI
1S/C41H80O16P2.H3N/c1-3-5-7-9-11-13-15-17-19-21-23-25-27-29-34(42)53-31-33(55-35(43)30-28-26-24-22-20-18-16-14-12-10-8-6-4-2)32-54-59(51,52)57-41-38(46)36(44)40(37(45)39(41)47)56-58(48,49)50;/h33,36-41,44-47H,3-32H2,1-2H3,(H,51,52)(H2,48,49,50);1H3/t33-,36-,37+,38-,39-,40+,41+;/m1./s1
SMILES string
N.CCCCCCCCCCCCCCCC(=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](O)[C@H]1O)OC(=O)CCCCCCCCCCCCCCC
InChI key
LVICQWVAYMJTST-LCJGNHTMSA-N
form
solid
solubility
DMSO: soluble, chloroform: soluble, ethanol: soluble
storage temp.
−20°C
Quality Level
General description
Component of lipid signaling pathway; substrate for phosphatidylinositol 3-kinase and phosphatidylinositol-4-phosphate 5-kinase; shown to promote β-adrenergic receptor kinase phosphorylation of the β2-adrenergic receptor.
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Yu Mei et al.
Cell research, 22(3), 581-597 (2011-09-07)
Phosphatidylinositol monophosphate 5-kinase (PIP5K) catalyzes the synthesis of PI-4,5-bisphosphate (PtdIns(4,5)P(2)) by phosphorylation of PI-4-phosphate at the 5 position of the inositol ring, and is involved in regulating multiple developmental processes and stress responses. We here report on the functional characterization
Hui Ma et al.
Cell research, 16(5), 466-478 (2006-05-16)
Multiple repeats of membrane occupation and recognition nexus (MORN) motifs were detected in plant phosphatidylinositl monophosphate kinase (PIPK), a key enzyme in PI-signaling pathway. Structural analysis indicates that all the MORN motifs (with varied numbers at ranges of 7-9), which
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
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
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
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