추천 제품
설명
zwitterionic
분석
≥98% (TLC)
형태
solid
분자량
211.28 g/mol
기술
DNA extraction: suitable
색상
white
solubility
methanol: 5 mg/mL, clear, colorless
SMILES string
OCC[N+](C)(C)CCCS([O-])(=O)=O
InChI
1S/C7H17NO4S/c1-8(2,5-6-9)4-3-7-13(10,11)12/h9H,3-7H2,1-2H3
InChI key
CNXPCGBLGHKAIL-UHFFFAOYSA-N
일반 설명
Dimethyl-2-hydroxyethylammoniumpropane sulfonate, or NDSB 211, is a nondetergent-sulfobetain. It is zwitterionic over a wide pH range, easily removed by dialysis and shows no significant absorption in the near UV range.
애플리케이션
NDSB 211 has been used in a study to assess halophilic protein stabilization by the mild solubilizing agents nondetergent sulfobetaines. It has also been used in a study to investigate an alternative strategy for crystallizing macromolecules.
Non-detergent sulfobetaine is a compound used for non-denaturing protien purification. Increases the extraction yield of membrane, nuclear and cytoskeletal associated proteins. Zwitterionic over a wide pH range, easily removed by dialysis and no significant absorption in the near UV range. Specific applications include microsomal protein extraction, nuclear protein recovery, precipitation reduction in IEF, and membrane-bound protease purification.
기타 정보
This product is non-micelle forming.
신호어
Danger
유해 및 위험 성명서
예방조치 성명서
Hazard Classifications
Skin Corr. 1B
Storage Class Code
8A - Combustible corrosive hazardous materials
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
시험 성적서(COA)
제품의 로트/배치 번호를 입력하여 시험 성적서(COA)을 검색하십시오. 로트 및 배치 번호는 제품 라벨에 있는 ‘로트’ 또는 ‘배치’라는 용어 뒤에서 찾을 수 있습니다.
이미 열람한 고객
Analytical biochemistry, 230(2), 290-294 (1995-09-20)
In this work, experiments performed on pig heart and halophilic malate dehydrogenase as well as halophilic elongation factor Tu demonstrate a protein stabilization property from the recently described mild solubilizing agents nondetergent sulfobetaines. A practical application is given by the
Searching for silver bullets: An alternative strategy for crystallizing macromolecules
Journal of Structural Biology, 156, 3887-3406 (2006)
Proteomics, 5(2), 354-359 (2005-01-04)
Proteins of haloarchaea are remarkably unstable in low-ionic-strength solvents and tend to aggregate under standard two-dimensional (2-D) gel electrophoresis conditions, causing strong horizontal streaking. We have developed a new approach to generate 2-D maps of halophilic proteins which included washing
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