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S9514

Sigma-Aldrich

Superose® 12 Prep Grade

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
23151817
NACRES:
NA.56

Pricing and availability is not currently available.

form

suspension

Quality Level

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

Pictograms

Flame

Signal Word

Warning

Hazard 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


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    Customers Also Viewed

    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
    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
    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)
    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
    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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