S9514
Superose® 12 Prep Grade
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suspension
particle size
20-40 μm (wet)
pore size
1,000-300,000 Da fractionation range (globular proteins)
storage temp.
2-8°C
Quality Level
Application
Superose® 12 prep grade is used for protein chromatography, gel filtration chromatography and gel filtration media. Superose® 12 prep grade has been used to purify and characterize a haemolysin of Actinomyces pyogenes as well as a fibrinogenase from Vipera lebetina (desert adder) venom. Superose® 12 prep grade has also been used for the isolation and characterization of an extracellular protease of Actinomyces pyogenes.
Physical form
Suspension in 20% ethanol
aqueous ethanol suspension
Other Notes
Highly cross-linked beaded agarose
Legal Information
Superose is a registered trademark of Cytiva
signalword
Warning
hcodes
Hazard Classifications
Flam. Liq. 3
Clase de almacenamiento
3 - Flammable liquids
wgk
WGK 3
flash_point_f
100.4 - 109.4 °F
flash_point_c
38 - 43 °C
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Shih-Chieh Lee et al.
Journal of agricultural and food chemistry, 52(16), 4948-4952 (2004-08-05)
Our research on several proteins indicates that accurate molecular weights cannot be determined by Superose 12 column chromatography. In support of this statement, we present data on molecular weights of purified red kidney bean alpha-amylase inhibitor (RKB alphaAI) and white
S M Duff et al.
Plant physiology, 90(2), 734-741 (1989-06-01)
Phosphoenolpyruvate phosphatase from Brassica nigra leaf petiole suspension cells has been purified 1700-fold to apparent homogeneity and a final specific activity of 380 micromole pyruvate produced per minute per milligram protein. Purification steps included: ammonium sulfate fractionation, S-Sepharose, chelating Sepharose
J Durner et al.
Plant physiology, 93(3), 1027-1031 (1990-07-01)
Acetolactate synthase (ALS, EC 4.1.3.18) has been extracted and partially purified from etiolated barley shoots (Hordeum vulgare L.). Multiple forms of this enzyme were separated by gel filtration and/or anion-exchange chromatography using fast protein liquid chromatography. It could be demonstrated
C Balestrieri et al.
European journal of biochemistry, 193(1), 183-187 (1990-10-05)
The finding of a powerful inhibitor of pectin methylesterase in ripe kiwi fruit is reported. The inhibitor was revealed to be a glycoprotein. It was purified to homogeneity and found to have a molecular mass of about 28 kDa, as
H Ding et al.
Zentralblatt fur Veterinarmedizin. Reihe B. Journal of veterinary medicine. Series B, 43(3), 179-188 (1996-05-01)
A haemolysin produced by Actinomyces pyogenes ATCC 8164 was purified from culture supernatant by ammonium sulphate and polyethylene glycol precipitation, ion-exchange chromatography on DEAE-Sephacel, and fast-protein-liquid-chromatography on Superose 12 prep grade. The purified haemolysin, designated as pyolysin, displayed a single
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