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Catalog Number: PTNXPRESS

Protein Expression and Purification

Protein molecules are the most complex group of molecules pivotal to the vast majority of biological functions. Not only due to the shear number of amino acids forming the backbone of proteins, but also their reactivities to other molecules or post translational modifications (PTM) enabling their reactivity under different biological conditions.

1st, 2nd, 3rd base, Homerun!

Protein folding or absence of PTM is not vital, in general, when they are used as immunogen for antibody production, unless those PTM such as phospho-group are the target of detection. E. coli or yeast can be used as host for these situations for their high productivity and simiplicity of culturing.

These post translational modifications could be vital when active proteins are desired for activity assays. Producing the proteins in their native host would provide best opportunity in achieving active proteins. Mammalian cells would be the best host to express and purify mammalian gene. Insect cells act like mammalian cells in terms of protein production but much easier to culture, and can produce large quantities of exogenous proteins without harming the host, which is most desirable when over-expression of the target gene would be disruptive to mammmalian cells.

Generating a stable Drosophila S2 cell line would be best option when large quantities of a protein is needed for the long run. It is easier to maintain than baculovirus without the tendency of mutations. 

  • Time consuming, expression clone construction, sequencing, mutation...
  • Low or no expression
  • Protein insoluble, aggregated
  • Degradation
  • Low purity

Let Lifeome take care of the 1st base, 2nd base and 3rd base issues, you hit the homerun! Proteins purified with quality, purity and amount you need!*

Over 50000 proteins expressed and purified! Our team is experienced and dedicated!

Check out our existing clones, listed by first two letters of their UniProt IDs. There are a lot, so take a moment to load!

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