Thiophilic adsorption or thiophilic chromatography is a routinely used technique for the low cost, simple purification of immunoglobulins. Thiophilic adsorption was first developed by Porath et al1 in 1984 and is a group specific, salt-dependent purification technique that has distinct affinity towards immunoglobulins and α2-macroglobulins. The thiophilic adsorption works on the principle that some proteins in high salt are able to bind to an immobilized ligand that contains a sulfone group in proximity to a thioether group (Figure 1). The bound proteins are then eluted in decreasing salt concentrations.
G-Biosciences’ Thiophilic resin binds immunoglobulins, including IgG, IgY and IgM, from serum, ascites or tissue culture supernatants and the purified immunoglobulins are then eluted in a near neutral aqueous buffer. G-Biosciences’ Thiophilic resin has a high binding capacity (~20mg/ml human IgG/ml resin) and a broad specificity for various species’ immunoglobulin molecules.
Thiophilic adsorption has been used to purify other proteins including horseradish peroxidase2, glutathione peroxidase3, lactate dehydrogenase4 and allergens5.
Supplied with protocols for IgG purification, IgM purification, IgY purification and general protein purification.
- Purify wide range of immunoglobulin molecules, including IgG, IgM and IgY
- High binding capacity (20mg human IgG/ml resin)
- Binds chicken immunoglobulin (IgY)
- Gentle elution conditions in very low salt and near neautral pH
- Adaptable to other proteins
- Enrichment alternative to ammonium sulfate precipitation
- Purify immunoglobulins, including IgG, IgM and chicken IgY
|Material Safety Data Sheet|
|Protein Purification Handbook|