Reactive Red 120-agarose is used in affinity chromatography, protein chromatography and dye resins. Reactive Red 120-agarose has been used to study wheat quality breeding as well as to provide strong evidence that purified human P-glycoprotein (Pgp) functions as an ATP-dependent drug transporter.
Physikalische Form
Suspension in 0.5 M NaCl, enthält 0.02% Thiomersal
Applied and environmental microbiology, 63(7), 2928-2931 (1997-07-01)
Two extracellular, heat-labile alkaline phosphatases were purified from a psychrophilic Arthrobacter isolate, D10. The enzymes were active over different pH ranges, used distinct substrates, and had different kinetic properties. Each enzyme reacted specifically to its own antibody during immunoblot analysis.
Mannitol-1-phosphate (M1P) dehydrogenase (M1PDH; EC 1.1.1.17), an enzyme catalyzing the reduction of Fru-6-phosphate (F6P) to M1P in algal mannitol biosynthesis, was purified to homogeneity from a cell homogenate of the eulittoral red alga Caloglossa continua (Okamura) King et Puttock. The
Removing trace fluorescent contaminants from GroEL preparations.
F Weber
Methods in molecular biology (Clifton, N.J.), 140, 63-64 (2001-08-04)
Protein science : a publication of the Protein Society, 5(6), 1093-1099 (1996-06-01)
The nucleotide-binding component of the high-affinity ribose transport system of Escherichia coli, RbsA, was overproduced from a T7-7 expression vector, and the protein was purified. Biochemical analyses of the purified protein indicated that the ATP analogues, 5'-FSBA and 8-azido ATP
The Journal of biological chemistry, 281(9), 5938-5946 (2005-12-16)
In this study, we addressed the presence and location of nucleotide-binding sites in the voltage-dependent anion channel (VDAC). VDAC bound to reactive red 120-agarose, from which it was eluted by ATP, less effectively by ADP and AMP, but not by
Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..
