Purification methods are determined by the source of your sample tissue and the antibody you are eliciting from the procedure. The following describes our purification procedures and details what you can expect from us.
1) Ammonium sulphate precipitation
This method is useful for concentration and partial purification of antibodies from most sources and all species. Although on its own, the yields of antibodies are impure, it is the method of choice when combined with ion exchange for large volumes of antisera. It is not recommended for purification of tissue culture supernatant.
2) Protein A
This process binds the Fc region of major sub-classes of mouse and rat immunoglobulin to varying degrees. The results with protein A are usually high purity and high yields. It is useful for large-scale purifications of tissue culture supernatants.
3) Protein G
Protein G can be used for purifying antibodies from most sources. Like protein A, the results are usually of high purity and high yield. It is applicable to a wider range of immunoglobulins than protein A, but elution procedures can be much harsher.
4) Ion exchange chromatography
This method is used for all sources of antibodies. It is applicable to all immunoglobulin isotypes.
5) Ig affinity
This method can be used to isolate mouse IgM and IgG3, and for isolating monoclonal antibodies from supernatants which contain high levels of serum Ig.
6) Antigen affinity
This is the method of choice when a specific antibody is required from polyclonal antisera. It requires pure antigen for the best results and can sometimes result in an inactive antibody.
7) Size exclusion
This method is appropriate for IgM antibodies from all sources. It is used when IgM antibodies need to be separated from polyclonal antisera. It is not recommended as a single stage.