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アッセイ
>99% (TLC)
フォーム
powder
包装
pkg of 1 × 1 g (850334P-1g)
メーカー／製品名
Avanti Research™ - A Croda Brand 850334P
輸送温度
dry ice
保管温度
−20°C
SMILES記法
[P](=O)([O-])(OCC[N+](C)(C)C)OCCCCCCCCCC
InChI
1S/C15H34NO4P/c1-5-6-7-8-9-10-11-12-14-19-21(17,18)20-15-13-16(2,3)4/h5-15H2,1-4H3
InChI Key
VVVDGSCGBGBGFN-UHFFFAOYSA-N
詳細
MAPCHO™-10/n-decylphosphocholine (DPC) is a short-chain lipid like, zwitterionic detergent.[1]
N-decylphosphocholine is a structural analog of decanoyl lysophosphatidylcholine that is more stable to hydrolytic degradation. The lipid maybe used as a detergent for membrane protein solubilization and purification.
生物化学的／生理学的作用
Dodecylphosphocholine (DPC) is mainly used to isolate and purify membrane proteins and it also acts as a membrane-mimetic micellar environment for liquid-state nuclear magnetic resonance (NMR) studies of membrane proteins.[1]
包装
30 mL Amber Wide Mouth Bottle with Screw Cap (850334P-1g)
法的情報
Avanti Research is a trademark of Avanti Polar Lipids, LLC
MAPCHO is a trademark of Avanti Polar Lipids, LLC
保管分類コード
11 - Combustible Solids
WGK
WGK 3
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
850334P-1G:
850334P-BULK:
850334P-VAR:
最新バージョンのいずれかを選択してください：
Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis
Nolandt OV, et al.
Biochimica et Biophysica Acta (2012)
Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis
Nolandt OV, et al.
Biochimica et Biophysica Acta, 1818(5), 1142-1147 (2012)
Sheeja V Vasudevan et al.
Proceedings of the National Academy of Sciences of the United States of America, 107(15), 6847-6851 (2010-03-31)
Repair of damage to the central nervous system (CNS) is inhibited by the presence of myelin proteins that prevent axonal regrowth. Consequently, growth inhibitors and their common receptor have been identified as targets in the treatment of injury to the
Binyong Liang et al.
Proceedings of the National Academy of Sciences of the United States of America, 104(41), 16140-16145 (2007-10-04)
The bacterial outer membrane protein G (OmpG), a monomeric pH-gated porin, was overexpressed in Escherichia coli and refolded in beta-octyl glucoside micelles. After transfer into dodecylphosphocholine micelles, the solution structure of OmpG was determined by solution NMR spectroscopy at pH
Roman Brunecky et al.
Biochemistry, 44(49), 16064-16071 (2005-12-08)
A growing number of modules including FYVE domains target key signaling proteins to membranes through specific recognition of lipid headgroups and hydrophobic insertion into bilayers. Despite the critical role of membrane insertion in the function of these modules, the structural
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