产品名称
L-α-磷脂酰肌醇 钠盐 来源于大豆, ≥99%
SMILES string
O[C@H]1[C@H](O)[C@@H](O)[C@@H](O)[C@@H](OP(OC[C@H](OC([R])=O)COC([R])=O)(O[Na])=O)[C@@H]1O
biological source
soybean
assay
≥99%
form
powder
functional group
phospholipid
lipid type
phosphoglycerides
shipped in
ambient
storage temp.
−20°C
Quality Level
Biochem/physiol Actions
磷脂膜组分，磷酸肌醇的前体。
Other Notes
主要含亚油酸和棕榈酸。
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)
Michael Witting et al.
PloS one, 12(3), e0172311-e0172311 (2017-03-10)
Lipid identification is a major bottleneck in high-throughput lipidomics studies. However, tools for the analysis of lipid tandem MS spectra are rather limited. While the comparison against spectra in reference libraries is one of the preferred methods, these libraries are
Yongmin Xiong et al.
Journal of cellular physiology, 219(2), 402-414 (2009-01-01)
Previously, we showed that laminin-binding to the dystrophin glycoprotein complex (DGC) of skeletal muscle causes a heterotrimeric G-protein (Galphabetagamma) to bind, changing the activation state of the Gsalpha subunit. Others have shown that laminin-binding to the DGC also leads to
Delphine Cardi et al.
The Journal of biological chemistry, 285(34), 26406-26416 (2010-06-10)
The antimalarial drugs artemisinins have been described as inhibiting Ca(2+)-ATPase activity of PfATP6 (Plasmodium falciparum ATP6) after expression in Xenopus oocytes. Mutation of an amino acid residue in mammalian SERCA1 (Glu(255)) to the equivalent one predicted in PfATP6 (Leu) was
S D Tachado et al.
Proceedings of the National Academy of Sciences of the United States of America, 94(8), 4022-4027 (1997-04-15)
The perturbation of various glycosylphosphatidylinositol (GPI)-anchored surface proteins imparts profound regulatory signals to macrophages, lymphocytes and other cell types. The specific contribution of the GPI moieties to these events however is unclear. This study demonstrates that purified GPIs of Plasmodium
T I Lin et al.
Journal of virology, 75(8), 3647-3656 (2001-03-27)
The viral ion channel protein M2 supports the transit of influenza virus and its glycoproteins through acidic compartments of the cell. M2 conducts endosomal protons into the virion to initiate uncoating and, by equilibrating the pH at trans-Golgi membranes, preserves
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