What Are the Common Methods for Protein Purification?
Protein purification is a fundamental technique used to isolate and purify a protein of interest, aiming to obtain samples with both high quantity and purity.
Common methods of protein purification include:
Precipitation
This technique relies on the differences in protein solubility under various conditions, such as changes in pH, electrolyte concentration, temperature, and the presence of organic solvents. Precipitants like ammonium sulfate, acetic acid, and PEG are commonly used to achieve protein separation.
Chromatography
Chromatography is a powerful tool that separates proteins based on their biochemical properties. This includes methods like affinity chromatography, ion exchange chromatography, gel filtration chromatography, and reverse-phase chromatography.
Electrophoresis
Proteins with different surface charges migrate at different rates when subjected to an electric field. Electrophoresis allows for separation based on these differences in migration distance within the gel. Common techniques include agarose gel electrophoresis and polyacrylamide gel electrophoresis.
Ultracentrifugation
This method takes advantage of the differences in mass between proteins. Under centrifugal force, heavier proteins or particles sediment more quickly, while lighter ones remain suspended or move more slowly, enabling separation. Density gradient centrifugation is one of the commonly used ultracentrifugation methods.
These methods are typically used in combination to achieve high-purity proteins, with specific steps tailored to the characteristics of the target protein.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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