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인용 및 참조 문헌 (315)
Invitrogen™
Lissamine™ Rhodamine B 1,2-Dihexadecanoyl-sn-Glycero-3-Phosphoethanolamine, Triethylammonium Salt (rhodamine DHPE)
The phospholipid, rhodamine DHPE is labeled on the head group with the red-fluorescent rhodamine B fluorophore with excitation/emission maxima ∼560/580자세히 알아보기
| 카탈로그 번호 | 수량 |
|---|---|
| L1392 | 5 mg |
카탈로그 번호 L1392
제품 가격(KRW)
342,000
온라인 행사
Ends: 31-Dec-2025
379,000할인액 37,000 (10%)
Each
수량:
5 mg
제품 가격(KRW)
342,000
온라인 행사
Ends: 31-Dec-2025
379,000할인액 37,000 (10%)
Each
The phospholipid, rhodamine DHPE is labeled on the head group with the red-fluorescent rhodamine B fluorophore with excitation/emission maxima ∼560/580 nm.
For Research Use Only. Not for use in diagnostic procedures.
사양
권장 스토리지Store in freezer (-5 to -30°C) and protect from light.
물리적 형태Solid
제품라인Invitrogen
수량5 mg
Unit SizeEach
인용 및 참조 문헌 (315)
인용 및 참조 문헌
Abstract
Journal:
PubMed ID:18198177
Poly(aspartic acid)-dependent fusion of liposomes bearing the quaternary ammonium detergent [[[(1,1,3,3-tetramethylbutyl)cresoxy]ethoxy]ethyl] dimethylbenzylammonium hydroxide.
Journal:Biochemistry
PubMed ID:3349055
Addition of the quaternary ammonium detergent [[[(1,1,3,3-tetramethylbutyl)cresoxy]ethoxy]ethyl] dimethylbenzylammonium hydroxide (DEBDA[OH]) and the fluorescent probes N-(7-nitro-2-1,3-benzoxadiazol-4-yl)phosphatidylethanolamine and N-(lissamine rhodamine B sulfonyl)phosphatidylethanolamine (N-NBD-PE and N-Rh-PE, respectively) to liposomes composed of phosphatidylcholine (PC) and cholesterol (chol) resulted in the formation of fluorescently labeled liposomes bearing DEBDA[OH]. Incubation of the anionic polymer poly(aspartic acid)
Use of resonance energy transfer to study the kinetics of amphiphile transfer between vesicles.
Journal:Biochemistry
PubMed ID:7082641
Topography of the hydrophilic helices of membrane-inserted diphtheria toxin T domain: TH1-TH3 as a hydrophilic tether.
Journal:Biochemistry
PubMed ID:16800637
'After low pH-triggered membrane insertion, the T domain of diphtheria toxin helps translocate the catalytic domain of the toxin across membranes. In this study, the hydrophilic N-terminal helices of the T domain (TH1-TH3) were studied. The conformation triggered by exposure to low pH and changes in topography upon membrane insertion
Immunochemical analysis shows all three domains of diphtheria toxin penetrate across model membranes.
Journal:J Biol Chem
PubMed ID:7499201
'Diphtheria toxin undergoes membrane insertion and translocation across membranes when exposed to low pH. In this study, the translocation of the toxin has been investigated by the binding of antibodies to two preparations of model membrane-inserted toxin. In one preparation, toxin was added externally to model membrane vesicles and then