Recommended Products
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.
Other Notes
Highly cross-linked beaded agarose
Physical form
Suspension in 20% ethanol
aqueous ethanol suspension
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
Certificates of Analysis (COA)
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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
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
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
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
Articles
This page provides information about performing an isolation of recombinant protein complexes with different pull-down assays with products from Cytiva.
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