Antibody purification using thiolophilic resins is a simple, robust, and economical alternative to protein A, the most widely used method of immunoglobulin purification. Although Protein A antibody purification is very common, there are certain classes of antibodies, such as scFv IgE, IgY, and IgM, that cannot be purified using Protein A. Another antibody purification method, Thiophilic Affinity Chromatography (TAC), is ideal for these types of applications, as well as immunoglobulin purification in general, including IgG, IgM, IgA, Fab and Fc fragments, and C3 and C4 complement factor.
TAC is a powerful and simple method for purifying proteins, especially immunoglobulins. It is an economical alternative to Protein A for purified antibodies from whole serum and tissue culture. Thiophilic adsorbents have a broader range of affinity for immunoglobulins than protein-based immunosorbents. Furthermore, more than 99% of the total protein was recovered using the thiophilic sorbent, compared to less than 92% for the benzene sorbent and 75% for the octyl-agarose sorbent.
TAC has broad specificity for different classes and subclasses of immunoglobulins from a wide range of species and has similar capabilities to other affinity methods.
Its advantages are simple sample preparation, suitable for various source materials and protein concentration ranges, and mild elution conditions, unlike popular protein A/protein G separation methods that require extreme pH for elution, and antibodies may not be stable enough.
Thiophilic superfluid resin adopts thiophilic adsorption chromatography. Using this technique, proteins are adsorbed to sulfone thioether ligands. Adding different salts to the mixture can facilitate the adsorption of different proteins. Changing the concentration of loading salt can affect the adsorption affinity of IgG, IgM, IgA, Fab and Fc fragments and C3 and C4 complement factors.