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
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
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Flam. Liq. 3
Storage Class Code
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 Gasmi et al.
Toxicon : official journal of the International Society on Toxinology, 29(7), 827-836 (1991-01-01)
A fibrinogenase from Vipera lebetina venom was isolated by gel filtration in a Superose 12 column prep grade HR 16/50 and by ion-exchange in a Mono Q HR 5/5 column. The purified enzyme, which was obtained with a yield of
Isolation and characterization of an extracellular protease of Actinomyces pyogenes
Schaufuss, P., et al.
Zentralblatt fur Bakteriologie, Parasitenkunde, Infektionskrankheiten Und Hygiene. 1. Abt. Medizinisch-Hygienische Bakteriologie, Virusforschung und Parasitologie. Originale, 271, 452-459 (1989)
H Youn et al.
Biochimica et biophysica acta, 1388(2), 405-418 (1998-12-22)
Lipoamide dehydrogenase was purified around 22-fold relative to the crude extracts of Streptomyces seoulensis with an overall yield of 9. 5%. The enzyme was composed of two identical subunits with a molecular mass of 54 kDa and contained 1 mol
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
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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