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.
The Thiophilic Adsorption kits is designed for the purification of IgG and contains all the necessary buffers and columns.
For IgM purification, IgY purification and general protein purification we recommend our Thiophilic Resin.
Features
- Purify immunoglobulin G molecules
- High binding capacity (20mg human IgG/ml resin)
- Gentle elution conditions in very low salt and near neautral pH
- Enrichment alternative to ammonium sulfate precipitation
Applications
- For the purification of IgG molecules
