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Key Documents

S9514

Sigma-Aldrich

Superose® 12 Prep Grade

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About This Item

Numéro CAS:
Numéro MDL:
Code UNSPSC :
23151817
Nomenclature NACRES :
NA.56

Forme

suspension

Niveau de qualité

Taille des particules

20-40 μm (wet)

Dimension de pores

1,000-300,000 Da fractionation range (globular proteins)

Température de stockage

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.

Autres remarques

Highly cross-linked beaded agarose

Forme physique

Suspension in 20% ethanol
aqueous ethanol suspension

Informations légales

Superose is a registered trademark of Cytiva

Pictogrammes

Flame

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Flam. Liq. 3

Code de la classe de stockage

3 - Flammable liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

100.4 - 109.4 °F

Point d'éclair (°C)

38 - 43 °C


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Les clients ont également consulté

G A Ameer et al.
Kidney international, 59(4), 1544-1550 (2001-03-22)
High plasma levels of beta2-microglobulin (beta2m) have been implicated in the formation of the severely destructive and potentially fatal amyloid deposits that are characteristic of dialysis-related amyloidosis (DRA). Conventional renal replacement technologies remove insufficient quantities of beta2m to normalize plasma
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

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