Protein Purification of Recombinant Proteins
Proteins made this way are considered recombinant because they aren’t natively produced in the organism that you got them from. We really like recombinant technology because it allows us to scale up protein production and generate therapeutic and/or interesting fusion proteins that we can use.
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Strategies for Protein Purification
Depending on the characteristics, different cleaning methods can be used:
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• Protein Load: If your protein has an overall load due to excess arginine or aspartame residues, it can be purified by passing it through an ion-exchange column. Use anion exchange chromatography for negatively charged proteins and cation exchange chromatography for positively charged proteins.
• The steps here are simple, just dissolve your protein in the buffer and incubate with the resin. Wash the resin with a low-salt buffer. And then the elution protein is bound with some high salt buffer (which interferes with the ionic interaction with the resin).
• Protein sizing: Dialysis and size exclusion chromatography can help you isolate proteins based on their size. In the case of dialysis, incubate your protein in a dialysis bag and stir while changing the buffer on the outside. Your proteins and larger proteins are stored in the bag, while the smaller proteins are filtered by diffusion.
• Protein affinity: If you are lucky enough to buy a resin with antibodies to your protein, you can run your protein through the resin and it will selectively bind to your protein. Then wash slightly with buffer to prevent binding of other proteins and finally eluted by breaking the antibody-protein interaction.