Protein Purification Services FAQs
Frequently asked questions
The following cell types are offered:
- Mammalian cells (FreeStyle™ 293, FreeStyle™ CHO, Expi293™, ExpiCHO™)
- Insect cells
The following cell types are used for expression:
- Mammalian cells (FreeStyle 293, FreeStyle CHO, Expi293, ExpiCHO)
- Insect cells
The cells we use are adapted for growth in suspension, but we can use adherent cells for protein expression if necessary.
We use shaker cultures and WAVE™ bag technology. Currently, 25 L is our maximum culture volume.
No. Currently we focus on intracellular or secreted proteins (e.g., antibodies, cytokines), and secretable proteins with an artificial secretion leader.
No, the prices are only for the protein services; gene synthesis, subcloning, and plasmid preparation work are not included.
We recommend that you let us produce an expression-optimized gene subcloned into a vector of your choice for the production of your protein. But we can produce protein from your construct as long as you test it for expression first and send us the results of your analysis; e.g., estimated protein quantification with Coomassie staining, and information on the cell culture volume you used.
In order to provide a firm price estimate, we need information on the productive performance of your protein. That is the purpose or the GeneArt Genes-to-Proteins Pilot production where we evaluate expression and purification performance of your construct. Once the pilot is complete, we can provide you with a binding quote for a specific protein amount
Unfortunately, we do not. Since cell line and protein production projects are so different and individual, each project is priced separately. Please define a specific project in an email to our customer support and we will get back to you with a price quote.
We use all available methods for purification, for example, affinity tag for purification, ProteinG/A (for antibodies or their derivatives), or combinations of ion exchange/hydrophobic interaction chromatography and gel filtration chromatography.
Yes, we use tags that can be cleaved off after purification and removed from the purified protein (for example, by introducing a thrombin or TEV protease cleavage sequence during gene synthesis—some amino acids may be left on the protein after cleavage).