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Citations & References (6)
Invitrogen™
Oregon Green™ 488-X, Succinimidyl Ester, 6-isomer
The amine-reactive Oregon Green™ 488-X, succinimidyl ester can be used to can be used to create green fluorescent bioconjugates withRead more
| Catalog Number | Quantity |
|---|---|
| O6185 also known as O-6185 | 5 mg |
Catalog number O6185
also known as O-6185
Price (MXN)
-
Quantity:
5 mg
The amine-reactive Oregon Green™ 488-X, succinimidyl ester can be used to can be used to create green fluorescent bioconjugates with excitation/emission maxima ∼496/524 nm. This fluorinated analog of fluorescein overcomes some of the key limitations of fluorescein, including greater photostability and a lower pKa (pKa ∼ 4.7 versus 6.4 for fluorescein), making its fluorescence essentially pH insensitive in the physiological pH range. This reactive dye contains an additional seven-atom aminohexanoyl spacer ('X') between the fluorophore and the succinimidyl ester group. This spacer helps to separate the fluorophore from its point of attachment, potentially reducing the interaction of the fluorophore with the biomolecule to which it is conjugated.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical ReactivityAmine
Emission524
Excitation496
Label or DyeOregon Green™ 488
Product TypeSuccinimidyl Ester
Quantity5 mg
Reactive MoietyActive Ester, Succinimidyl Ester
Shipping ConditionRoom Temperature
Label TypeClassic Dyes
Product LineOregon Green
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (6)
Citations & References
Abstract
Evolution of peptides that modulate the spectral qualities of bound, small-molecule fluorophores.
Journal:Chem Biol
PubMed ID:9862799
'BACKGROUND: Fluorophore dyes are used extensively in biomedical research to sensitively assay cellular constituents and physiology. We have created, as proof of principle, fluorophore dye binding peptides that could have applications in fluorescent dye-based approaches in vitro and in vivo. RESULTS: A panel of Texas red, Rhodamine red, Oregon green
Incorporation of reporter molecule-labeled nucleotides by DNA polymerases. I. Chemical synthesis of various reporter group-labeled 2'-deoxyribonucleoside-5'-triphosphates.
Journal:Nucleic Acids Res
PubMed ID:12736313
Fluorescent-labeled DNA is generated through enzymatic incorporation of fluorophore-linked 2'-deoxyribonucleoside-5'-triphosphates (dNTPs) by DNA polymerases. We describe the synthesis of a variety of dye-labeled dNTPs. Amino-linker-modified 5'-triphosphates of all four naturally occurring nucleobases were used as precursors. Commercially available dyes were coupled to the amino function of the side chain. In
Cystic fibrosis transmembrane conductance regulator-independent phagosomal acidification in macrophages.
Journal:J Biol Chem
PubMed ID:17724021
It was reported recently that the cystic fibrosis transmembrane conductance regulator (CFTR) is required for acidification of phagosomes in alveolar macrophages (Di, A., Brown, M. E., Deriy, L. V., Li, C., Szeto, F. L., Chen, Y., Huang, P., Tong, J., Naren, A. P., Bindokas, V., Palfrey, H. C., and Nelson,
Noninvasive imaging of cell death using an Hsp90 ligand.
Journal:J Am Chem Soc
PubMed ID:21322555
Cell death plays a central role in normal physiology and in disease. Common to apoptotic and necrotic cell death is the eventual loss of plasma membrane integrity. We have produced a small organoarsenical compound, 4-(N-(S-glutathionylacetyl)amino)phenylarsonous acid, that rapidly accumulates in the cytosol of dying cells coincident with loss of plasma
Essential role of histidine 20 in the catalytic mechanism of Escherichia coli peptidyl-tRNA hydrolase.
Journal:Biochemistry
PubMed ID:15078105
The peptidyl-tRNA hydrolase (Pth) enzyme plays an essential role in recycling tRNA from peptidyl-tRNA that has prematurely dissociated from the ribosome. In this study of Escherichia coli Pth, the critical role of histidine 20 was investigated by site-directed mutagenesis, stopped-flow kinetic measurements, and chemical modification. The histidine residue at position