ServicesAntibody engineering > Purification

Purification

Agro-Bio offers several kinds of purification for biological products with easy and fast methods to be set up and not to denature products.

Purification of IgG on protein A or G

Purifications by chromatography of affinity on Protein A and on Protein G allow isolating specifically the immunoglobulins by binding their Fc portion. They are used to purify immunoglobulins of different species and isotypes from biological fluids like serum, supernatant… This method allows to obtain a yield and a purity superior to 90 %.

Purification by specific affinity or purification of depletion

Affinity purification allows to isolate a molecule of interest thanks to a ligand.

This ligand (protein, peptide, antigen, antibody ...) is fixed to an activated gel by chemical functions to have a specific and stable support to purify the molecules of interest.

This technique provides: 

  • Purified antibody having specific recognition of the antigen by coupling the antigen on the purification gel,
  • Proteins of interest by coupling specific antibodies to the gel,
  • Specific products depleted of proteins or ultra-specific antibodies.

Purification by precipitation

Purification by precipitation is an alternative to the protein A/G purification by performing the purification of total antibodies from serum, in vitro supernatant or ascites by precipitation with caprylic acid and with ammonium sulfate.

Ion exchange purification

Purification ion exchange is based on the principle of hydrophobic charge-induction chromatography. It engages hydrophobic interactions with the immunoglobulins or other proteins, when they are positively or negatively charged. This technique is mainly used to purify specific IgM (negatively charged).

Size exclusion or gel filtration purification

Size exclusion chromatography is a method for separating molecules based on the filtration of different sizes of molecules through a porous gel.

Proteins in solution, or other macromolecules, are applied to a column with a defined support medium. The behaviour of the protein depends on its size and that of the pores in the medium. Thus the different proteins are eluted in the reverse order of their molecular weight.

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