Description
Protein purification at the IMBB is carried out using several different FPLC and gravity systems, each complete with fraction collectors, UV detectors, prepacked columns, etc and are distributed in 6 stations around the IMBB campus.

Equipment

Services
1. Large scale (mg to gram) protein purification using tags on proteins (e.g. metal chelate affinity chromatography using His-tag, glutathione-sepharose resins for GST-tags, amylose affinity purification for fusions with the maltose binding protein etc.), or affinity chromatography of nucleic-acid binding proteins (methylases, restriction enzymes, transcription factors etc) or classical purification methods (e.g. ion exchange, hydroxyapatite, phosphocellulose, hydrophobic, industrial dyes, size-exclusion chromatography etc.).
2. Protein concentration from dilute solutions (e.g. using ultrafiltration, salt precipitation etc.)
3. Analytical gel filtration for native mass determination of proteins (see also Macromolecular analysis)
4. Preparation of proteins (through solution purification or gel extraction) for antibody production.
5. Purification of antibodies from nitrocellulose or from antigens immobilized on cyanogen bromide activated sepharose.
6. Fractionation of native proteins on sucrose gradients by sedimentation equilibrium analytical ultracentrifugation.
7. Analysis of native oligomeric complexes by native-Page and blue-native Page.

Links
Minotech
Fermentation Facility