S9514
Superose® 12 Prep Grade
form
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
Storage Class
3 - Flammable liquids
wgk
WGK 3
flash_point_f
100.4 - 109.4 °F
flash_point_c
38 - 43 °C
Regulatory Information
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A Van Tol et al.
Journal of lipid research, 32(11), 1719-1728 (1991-11-01)
The present study demonstrates very high levels of plasma lipids and high density lipoprotein (HDL) apolipoproteins (apoA-I and apoE) in female Nagase analbuminemic rats (NAR) fed a semi-synthetic diet in order to further increase the hyperlipidemia present in this strain.
Tianwei Tan et al.
Biotechnology journal, 5(5), 505-510 (2010-05-05)
Following its market introduction in 1982, the cross-linked 12% agarose gel media Superose 12 has become widely known as a tool for size exclusion chromatography of proteins and other biological macromolecules. In this review it is shown that, when appropriate
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
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
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