In molecular biology, biochemistry, and biotechnology, protein purification is a crucial procedure used to separate a particular protein from a complicated mixture.

- Affinity Chromatography ( IMAC, GST, Sepharose, Streptavidin, Protein A, Protein G )
- Ion Exchange Chromatography ( Mono-Q, DEAE Sepharose, SP Sepharose, CM Sepharose )
- Hydrophobic Interaction Chromatography Phenyl and (CH2)n Sepharose )
- Size Exclusion Chromatography

Affinity Chromatography

One of the most popular methods for purifying proteins is affinity chromatography, which relies on the unique interaction between the target protein and an antibody or ligand that is affixed to a chromatography resin. Other proteins are removed by washing, while the protein of interest is separated according on its propensity for binding to the ligand.

Ion Exchange Purification

Ion exchange chromatography uses positively or negatively charged resins to bind proteins based on their net surface charge in a buffer with a given pH, according to their isoelectric point (pI).

Hydrophobic Interaction Purification

This technique relies on the hydrophobic interactions between the target protein and the hydrophobic groups in the resin. It is often used for the separation of proteins or peptides with different hydrophobicity profiles.:

Size Exclusion Chromatography (SEC)

SEC, sometimes referred to as gel filtration, separates proteins according to their size. Smaller proteins are held in the porous matrix for a longer period of time, while larger proteins move along the column more quickly.:

 

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