Protein Expression in E. coli Expression System

The E. coli expression system is the most widely used expression system for recombinant proteins. There are many advantages of using a E. coli protein expression system including:

  • low costs
  • high expression level
  • ease of scaling
  • short turnaround times

Protein Expression in E. coli Highlights:

  • High Efficiency: our collection of more than 10 host strains and various proprietary or non-proprietary vectors guarantees the selection of the most efficient expression system.
  • High Productivity: multiple fusion tags and our proprietary AIE technology are available in house to increase protein solubility and production, and to decrease purification cost, even for toxic proteins.
  • Refolding: we have established an effective protein refolding system consisting of 20 refolding buffers optimized with 9 parameters to increase the chance to obtain soluble and bioactive proteins.
  • Large-Scale Production: we are able to produce up to 500L of E. coli cell culture for gram scale production.
  • Modifications: metabolic labeling with stable isotopes (13C and 15N) and biotinylation are available.
  • Competitive Pricing: 5mg protein at 80% purity from only $1000!

Our Services:

Cloning and Expression

  • Codon optimization and gene synthesis (optional): $0.40 per base pair
  • Subcloning gene of interest into E. coli expression vector: $195 each
  • Construction of expression strains and optimization of expression conditions: $100

Pilot Scale Expression and Production

  • 2 liters of bacterial cell culture
  • Inducing cells with IPTG and cell harvesting for purification
  • Purifying protein with or without tag by affinity column, gel filtration, ion exchange, orhydrophobic column
  • Removal of fusion/purification tag
  • 5mg of protein from $1000

Large-Scale Production

  • Large-scale fermentation up to 500L with 60-80g cell pellet/liter
  • Large-scale purification up to gram scale

Additional Services

  • Protein refolding
  • Metabolic labeling with stable isotopes (13C and 15N)
  • Biotinylation
  • Large-scale fermentation
  • Large-scale purification
  • Process development
References:

Stout TE, et al. Recombinant Filaggrin Is Internalized and Processed to Correct Filaggrin Deficiency.

PMID: 23792461 [PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/pubmed/23792461

In addition to our E. coli protein expression system, we also offer a number of other expression systems including:yeast expression system, baculovirus expression system, and mammalian cell expression system.