We can perform the most widely used antibody purification methods, including affinity purification, size exclusion chromatography (gel filtering), ion exchange chromatography, and hydrophobic chromatography. These services are intended to extract proteins from complex mixtures, like cell lysates, tissues, or culture media, in order to achieve high purity for additional study or applications.

- Affinity purification
- Protein A, G, and A/G Purification
- Antigen-specific affinity purification
- Monospecific affinity purification

Affinity purification

The main use of affinity chromatography is the extraction of a particular protein or class of proteins from complex mixtures. A physiologically active molecule's capacity to selectively and reversibly attach to a corresponding molecule, which is frequently coupled to a solid support, is the foundation of affinity chromatography. These ligand molecules might be metals, lectins, biotin, aptamers, antibodies, or other types of molecules.

Protein A, G, and A/G Purification

Four domains of Protein A/G attach to Protein A's Fc region, whereas the remaining two domains link to Protein G. Additionally, unlike Protein A, this fusion protein has the additive binding qualities of both proteins and is not pH dependent.

Antigen-specific affinity purification

We purify your antibodies by using the following steps:
- immobilisation of antigen on agarose beads
- Loading of the antiserum on the affinity chromatography column
- Elution of bound antigen-specific antibodies
- Analysis with ELISA