Application
Reactive Yellow 3-agarose is used in affinity chromatography, protein chromatography and dye resins. Reactive Yellow 3-agarose has been used in immunohistochemical localization studies to show where tyramine N-(hydroxycinnamoyl)transferase (THT) polypeptides occur in opium poppy. Reactive Yellow-agarose has also been used to purify human cholesteryl ester transfer protein.
Physical form
Suspension in 0.5 M NaCl containing preservative
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Purification of hydroxycinnamoyl-CoA:tyramine hydroxycinnamoyltransferase from cell-suspension cultures of <I>Solanum tuberosum</I> L. cv. Datura.
Hohlfeld, H., et al.
Planta, 199(1), 166-168 (1996)
J M Stoop et al.
Archives of biochemistry and biophysics, 298(2), 612-619 (1992-11-01)
A mannitol:mannose 1-oxidoreductase was isolated from celeriac (Apium graveolens var. rapaceum) root tips by fractionation with (NH4)2SO4, followed by chromatography on a Fractogel DEAE column and then concentration with (NH4)2SO4. This newly discovered mannitol dehydrogenase catalyzes the NAD-dependent oxidation of
M L Fonda
The Journal of biological chemistry, 267(22), 15978-15983 (1992-08-05)
Human erythrocytes rapidly convert vitamin B6 to pyridoxal-P and contain soluble phosphatase activity which dephosphorylates pyridoxal-P at a pH optimum of 6-6.5. This phosphatase was purified 51,000-fold with a yield of 39% by ammonium sulfate precipitation and chromatography on DEAE-Sepharose
J M Green et al.
The Journal of biological chemistry, 266(20), 12971-12975 (1991-07-15)
p-Aminobenzoate, a component of the vitamin folate, is one of seven compounds derived from the aromatic precursor chorismate in Escherichia coli. Historically the gene products of pabA and pabB were assumed to be sufficient for de novo p-aminobenzoate biosynthesis. Recent
T Vogt et al.
Planta, 203(3), 349-361 (1997-01-01)
Uridine 5'-diphosphoglucose:betanidin 5-O- and 6-O-glucosyltransferases (5-GT and 6-GT; EC 2.4.1) catalyze the regiospecific formation of betanin (betanidin 5-O-beta-glucoside) and gomphrenin I (betanidin 6-O-beta-glucoside), respectively. Both enzymes were purified to near homogeneity from cell-suspension cultures of Dorotheanthus bellidiformis, the 5-GT by
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