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Merck
CN

P3644

Sigma-Aldrich

L-α-磷脂酰胆碱

from soybean, Type IV-S, ≥30% (enzymatic)

别名:

1,2-二酰基-sn-甘油-3-胆碱磷酸, 3-sn-磷脂酰胆碱, L-α-卵磷脂, Azolectin, PC

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About This Item

CAS号:
Beilstein:
5209585
EC 号:
UNSPSC代码:
51321705
NACRES:
NA.25

生物来源

soybean

质量水平

类型

Type IV-S

表单

solid

浓度

≥30% (enzymatic)

溶解性

chloroform: soluble 100 mg/mL, clear to slightly hazy, yellow to orange

官能团

phospholipid

脂质类型

phosphoglycerides

运输

ambient

储存温度

−20°C

SMILES字符串

[P](=O)([O-])(OC[C@H](OC(=O)CCCCCCC\C=C/C\C=C/CCCCC)COC(=O)CCCCCCCCCCCCCCC)OCC[N+](C)(C)C

InChI

1S/C42H80NO8P/c1-6-8-10-12-14-16-18-20-21-23-25-27-29-31-33-35-42(45)51-40(39-50-52(46,47)49-37-36-43(3,4)5)38-48-41(44)34-32-30-28-26-24-22-19-17-15-13-11-9-7-2/h14,16,20-21,40H,6-13,15,17-19,22-39H2,1-5H3/b16-14-,21-20-/t40-/m1/s1

InChI key

JLPULHDHAOZNQI-ZTIMHPMXSA-N

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应用

L-α-磷脂酰胆碱适用于:
  • 作为人类红细胞大量扩增培养(HEMAdef)培养基的组份,用于人成红细胞的临床扩增
  • 氯离子流出试验,检测可溶性 CLIC1 引起的脂质囊泡的氯离子渗透性
  • 测定溶解的蜡合酶活性的试验
  • 作为缓冲液 A 的组分,用于重悬腺苷酸环化酶的胆酸盐溶解催化单元
  • 作为冷冻反刍动物精子的冷冻保护剂
  • 作为评估磷脂酶活性的底物
  • 制备脂质体,评估其 ARF(ADP 核糖基化因子)和 AP-1(衔接蛋白)的募集效率
  • 制备可溶性腺苷酸环化酶的分离催化单元

生化/生理作用

磷脂酰胆碱是真核细胞中的主要膜磷脂,形成这些膜的结构组分。它还用作几种脂质信使的储库和几种生物活性脂质的来源,例如溶血磷脂酰胆碱、磷脂酸、二酰基甘油、溶血磷脂酰胆碱、血小板活化因子和花生四烯酸。
脑磷脂脑中的主要结构磷脂,包含脂肪总量的约15%;主要局限于灰质。

制备说明

纯化自产品 P 5638

储存分类代码

11 - Combustible Solids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, type N95 (US)


历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Hossein Salmani et al.
Cryobiology, 68(2), 276-280 (2014-02-20)
Soybean lecithin is a suitable plant-based cryoprotectant for freezing ruminant sperm. Optimum level of lecithin was not clear for goat semen cryopreservation. The objective of this study was to investigate the effects of different levels of soybean lecithin in semen
K D Lardizabal et al.
Plant physiology, 122(3), 645-655 (2000-03-11)
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R S Salter et al.
The Journal of biological chemistry, 256(19), 9830-9833 (1981-10-10)
The catalytic and guanine nucleotide regulatory (G/F) units of solubilized bovine brain adenylate cyclase were separated by gel filtration as described by Strittmatter, S., and Neer, E. J. ((1980) Proc. Natl. Acad. Sci. U. S. A. 77, 6344-6348). The isolated
Anna Kloda et al.
Proceedings of the National Academy of Sciences of the United States of America, 104(5), 1540-1545 (2007-01-24)
In this study, the heteromeric N-methyl-D-aspartate (NMDA) receptor channels composed of NR1a and NR2A subunits were expressed, purified, reconstituted into liposomes, and characterized by using the patch clamp technique. The protein exhibited the expected electrophysiological profile of activation by glutamate
Masayuki Iwamoto et al.
ACS synthetic biology, 7(4), 1004-1011 (2018-03-24)
Processes involved in the functional formation of prokaryotic membrane proteins have remained elusive. Here, we developed a new in vitro membrane protein expression system to detect nascent activities of the KcsA potassium channel in lipid bilayers under an applied membrane

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