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인용 및 참조 문헌 (125)
Invitrogen™
Monochlorobimane (mBCI)
Monochloromobimane is essentially nonfluorescent until conjugated, readily reacts with several low molecular weight thiols, including glutathione, N-acetylcysteine, mercaptopurine, peptides and자세히 알아보기
| 카탈로그 번호 | 수량 |
|---|---|
| M1381MP | 25 mg |
카탈로그 번호 M1381MP
제품 가격(KRW)
403,000
線上優惠
Ends: 31-Mar-2026
473,000할인액 70,000 (15%)
Each
수량:
25 mg
제품 가격(KRW)
403,000
線上優惠
Ends: 31-Mar-2026
473,000할인액 70,000 (15%)
Each
Monochloromobimane is essentially nonfluorescent until conjugated, readily reacts with several low molecular weight thiols, including glutathione, N-acetylcysteine, mercaptopurine, peptides and plasma thiols. The glutathione conjugate of monochlorobimane has absorption/emission maxima ∼394/490 nm.
For Research Use Only. Not for use in diagnostic procedures.
사양
방출490
제품 유형Monochlorobimane
수량25 mg
배송 조건Room Temperature
Unit SizeEach
구성 및 보관
Store in freezer -5°C to -30°C and protect from light.
인용 및 참조 문헌 (125)
인용 및 참조 문헌
Abstract
SLCO/OATP-like transport of glutathione in FasL-induced apoptosis: glutathione efflux is coupled to an organic anion exchange and is necessary for the progression of the execution phase of apoptosis.
Journal:The Journal of biological chemistry
PubMed ID:16857677
A general strategy for site-specific double labeling of globular proteins for kinetic FRET studies.
Journal:Bioconjugate chemistry
PubMed ID:12236801
Site-directed mutagenesis provides a straightforward means of creating specific targets for chemical modifications of proteins. This capability enhanced the applications of spectroscopic methods adapted for addressing specific structural questions such as the characterization of partially folded and transient intermediate structures of globular proteins. Some applications such as the steady state
Membrane translocation of charged residues at the tips of hydrophobic helices in the T domain of diphtheria toxin.
Journal:Biochemistry
PubMed ID:9893993
'The low pH triggered membrane insertion of the T domain of diphtheria toxin is a critical step in the translocation of the C domain of the toxin across membranes in vivo. We previously established that the T domain can interact with membranes in two distinct conformations, one in which the
Topography of diphtheria toxin A chain inserted into lipid vesicles.
Journal:Biochemistry
PubMed ID:15697244
'The membrane-inserting T domain of diphtheria toxin aids the low-pH-triggered translocation of the catalytic A chain of the toxin across endosomal membranes. To evaluate the role of the isolated A chain in translocation, the topography of isolated A chain inserted into model membrane vesicles was investigated using a mixture either
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