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Expression, purification and crystallization of fully active, glycosylated human interleukin-5
Y Guisez1, C Oefner, F K Winkler
1Roche Research Gent, Belgium.
FEBS Letters
|September 27, 1993
Abstract:
Recombinant human interleukin-5 (hIL-5) has been expressed at high levels and produced in large quantities in baculovirus infected Sf9 insect cells. The glycosylated protein was purified using immuno-affinity chromatography and gel filtration. Purified hIL-5 has been crystallized using standard vapour diffusion techniques with PEG as a coprecipitant. The crystals belong to the C2 space group and diffract to 2 A.