High-Purity Maltoside Detergents
High-Purity Maltoside Detergents
Thermo Scientific™

High-Purity Maltoside Detergents

Thermo Scientific n-Dodecyl-β-D-Maltosideは、タンパク質活性を維持したまま膜タンパク質を可溶化するのに特に有用です。この水溶性の非イオン性界面活性剤は、疎水性膜タンパク質の分離にもっともよく使用されます。n-Dodecyl-β-D-maltosideは、NP-40、CHAPS、オクチル-β-グルコシドなどの一般的に使用される多くの界面活性剤よりも良好にタンパク質活性を維持できる詳細を見る
製品番号(カタログ番号)数量試薬タイプ
899021 g界面活性剤(純粋)
899035 g界面活性剤(純粋)
A655091 gUDM
A509401 gLMNG
A655105 gUDM
A5094110 x 1 mLLMNG/CHS Solution (10:1)
A655111 gOM
A655125 gOM
A655131 gn-Nonyl-Beta-Maltoside
A655145 gn-Nonyl-Beta-Maltoside
製品番号(カタログ番号) 89902
価格(JPY)
22,200
キャンペーン価格
Ends: 27-Mar-2026
37,000
割引額 14,800 (40%)
Each
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数量:
1 g
試薬タイプ:
界面活性剤(純粋)
一括またはカスタム形式をリクエストする
Thermo Scientific n-Dodecyl-β-D-Maltosideは、タンパク質活性を維持したまま膜タンパク質を可溶化するのに特に有用です。

この水溶性の非イオン性界面活性剤は、疎水性膜タンパク質の分離にもっともよく使用されます。n-Dodecyl-β-D-maltosideは、NP-40、CHAPS、オクチル-β-グルコシドなどの一般的に使用される多くの界面活性剤よりも良好にタンパク質活性を維持できる、穏やかな界面活性剤であることが複数の実験で実証されています。

n-Dodecyl-β-D-Maltosideの特長:

•脂質様非イオン性界面活性剤
• 疎水性膜タンパク質の分離および可溶化に特に有用
• 他のほとんどの界面活性剤よりも良好に膜タンパク質の活性を維持
• 低UV吸収性の高純度化合物

n-Dodecyl-β-D-maltosideはほとんどの界面活性剤と同様に、疎水性/親水性の両特性を有しており、脂肪置換を促進し、膜タンパク質に脂質様環境を提供します。これらの界面活性剤が膜タンパク質構造を維持する能力は、部分的には、脂質とタンパク質の相互作用に対する阻害が低く、天然の脂質集合の一部が維持されることによることが研究で示唆されています。膜タンパク質のあらゆる研究に最適な界面活性剤または条件設定は存在しませんが、n-Dodecyl-β-D-maltosideは、特定のタンパク質手法で特に有益な独自の特性を有しています。

n-Dodecyl-β-D-Maltosideの特性:
• 化学名:n-Dodecyl-beta-D-maltoside
• 分子量:510.6g
• 界面活性剤分類:非イオン性
• 凝集数:98(平均)、70~140の範囲
• ミセル分子量:50000g
• 臨界ミセル濃度(CMC):水で0.17 mM(0.009%、w/v)、0.2M NaClで0.12 mM(0.006%、w/v)
• 雲り点:不明
• 透析:不可

n-Dodecyl-beta-maltoside仕様(製品番号89902、89903):
• 化学式:C24H46O11
• 分子量:510.6g
• 純度(HPLCで測定):≥99%
• 吸光度(1%界面活性剤溶液):340 nmで<0.02、280 nmで<0.04、260 nmで<0.06、225 nmで<0.1
• pH(1%溶液):5~8
• 溶解度(0~5℃の水中):≥20%
• 導電率(10%溶液):<40 mS

関連製品
Surfact-Amps™ Detergent Sampler
研究用にのみ使用できます。

n-Dodecyl-β-D-maltosideはほとんどの界面活性剤と同様に、疎水性/親水性の両特性を有しており、脂肪置換を促進し、膜タンパク質に脂質様環境を提供します。これらの界面活性剤が膜タンパク質構造を維持する能力は、部分的には、脂質とタンパク質の相互作用に対する阻害が低く、天然の脂質集合の一部が維持されることによることが研究で示唆されています。膜タンパク質のあらゆる研究に最適な界面活性剤または条件設定は存在しませんが、n-Dodecyl-β-D-maltosideは特定のタンパク質手法で特に有益な独自の特性を有しています。

仕様:

  • 化学式:C24H46O11
  • 分子量:510.6
  • 純度(HPLCで測定):≥ 99%
  • 吸光度(1%界面活性剤溶液):340 nmで*< 0.02;280 nmで< 0.04;260 nmで< 0.06;225 nmで< 0.1
  • pH(1%溶液):5∼8
  • 溶解度(0∼5°C水中):≥ 20%
  • 導電率(10%溶液):< 40 mS

引用文献:

  1. Casey, J. R.., et al.(1993).Biochemistry, 32, 1172-1179.
  2. Engel, C.K., et. al.(2002).Biochimica et Biophysica Acta, 1564, 47-56.
  3. Boulter, J. M., Wang, D. N., (2001).Protein Expression and Purification, 22, 337-348.
  4. le Maire, M., et. al.(2000).Biochimica et Biophysica Acta, 1508, 86-111.
  5. Banerjee, P., et. al.(1995). Chemistry and Physics of Lipids, 77, 65-78.
  6. Wang, D. N., et. al.(2003). Biochimica et Biophysica Acta, 1610, 23-36.
  7. Berger,B.W., et. al.(2005). Biophysical Journal, 89, 452-464.
  8. Auer, M. et. al.(2001).Biochemistry, 40, 6628-6635.
仕様
分子量510.6 g/mol
数量1 g
試薬タイプ界面活性剤(純粋)
形状粉末
製品タイプDetergent
Unit SizeEach
組成および保存条件
-20℃以下で保存

よくあるご質問(FAQ)

Are detergents denaturing or non-denaturing with respect to protein structure?

Ionic detergents, or those that carry a charge, are the most likely to be denaturing to proteins. Denaturing detergents can be anionic such as sodium dodecyl sulfate (SDS) or cationic such as ethyl trimethyl ammonium bromide. These detergents totally disrupt membranes and denature proteins by breaking protein-protein interactions through changes in the three-dimensional structure of the proteins. Nondenaturing detergents can be divided into nonionic detergents (i.e., Triton X-100), bile salts (i.e., cholate), and zwitterionic detergents (i.e., CHAPS).



Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

What are detergents?

Detergents are amphipathic molecules containing both a nonpolar “tail” having aliphatic or aromatic character, and a polar “head”. The ionic character of the polar head group forms the basis for broad classification of detergents as ionic, nonionic, or zwitterionic.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

How does detergent-based cell lysis work?

Detergents are amphipathic molecules, meaning they contain both a nonpolar “tail” having aliphatic or aromatic character and a polar “head”. Like the components of biological membranes, detergents have hydrophobic-associating properties as a result of their nonpolar tail groups. Nevertheless, detergents are themselves water soluble.

Consequently, detergent molecules allow the dispersion (miscibility) of water-insoluble, hydrophobic compounds into aqueous media, including the extraction and solubilization of membrane proteins. Detergent monomers solubilize membrane proteins by partitioning into the membrane bilayer. With increasing amounts of detergents, membranes undergo various stages of solubilization.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

What types of detergents are available for cell lysis?

Detergents can be denaturing or non-denaturing with respect to protein structure. Denaturing detergents can be anionic such as sodium dodecyl sulfate (SDS) or cationic such as ethyl trimethyl ammonium bromide. These detergents totally disrupt membranes and denature proteins by breaking proteinprotein interaction. These detergents are considered harsh. Non-denaturing detergents can be divided into nonionic detergents (i.e., Triton X-100), bile salts (i.e., cholate), and zwitterionic detergents (i.e., CHAPS). These detergents do not denature proteins and do not break protein-protein interactions. These detergents are considered mild.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Why does the method of cell lysis matter?

Cell lysis is the first step in cell fractionation, organelle isolation, and protein extraction and purification. As such, cell lysis opens the door to a myriad of proteomics research methods. Many techniques have been developed and used to obtain the best possible yield and purity for different species of organisms, sample types (cells or tissue), and target molecule or subcellular structure. Subcellular fractionation and protein enrichment are important methods in the rapidly growing field of proteomics. Isolation of subcellular fractions and concentration of proteins in low abundance allow for more efficient identification and study of proteins of interest. Examples are the isolation of integral membrane proteins and nuclear proteins.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.