prospec

Technology License

Technology License

ProSpec offers full Technology-License packages, which include a comprehensive course at our/customer lab facility.
Over the past 16 years, ProSpec developed simple, cost effective and easy to implement proprietary technologies for the production of ultra-pure bulk proteins in bacterial expression system.
ProSpec batch productions consist of 4-5 working days and yield 300mg-1000mg protein per 5 liter fermentation.
The technologies offered give a clear edge over the competition resulting from low production costs, high yield and production efficiency.
ProSpec offers its unique protein refolding techniques, purification and separation processes for all recombinant proteins produced in bacterial system.

For custom tailored production please contact: info@prospecbio.com

  • Product
  • Description
    • Human IFN-a 2a
    • Interferon-Alpha 2a
    • Human IFN-a 2b
    • Interferon-Alpha 2b
    • Human G-CSF
    • Granulocyte Colony Stimulating Factor
    • Human GM-CSF
    • Granulocyte Macrophage Colony Stimulating Factor
    • Human IL-2
    • Interleukin-2
    • Human GH
    • Growth Hormone

Our customers receive highly detailed technology book and the producing clone at the end of the technology implementation course which can last up to 14 working days. Below is a sample index of technology book.

Note: Our laboratory is non-GMP/GLP/ISO regulated. 

Index of technology-license book:


  1. Introduction.
  2. Manufacturing
    2.1 General. 
    2.2 Construction of the plasmid expressingof the protein. 
    2.3 DNA sequence. 
    2.4 Expression of the protein in E.coli. 
  3. Biosynthesis of the protein substance 
    3.1 Fermentation process: 
    3.2 Inoculum. 
    3.3 Seed fermentor.
    3.4 Production fermentor. 
    3.5 Fermentor Harvest. 
    3.6 Cell disruption.
    3.7 Water Washes. 
  4. Purification of the protein from inclusion bodies
    4.1 Dissolution of the protein inclusion bodies. 
    4.2 Dilution and refolding of the protein. 
    4.3 Clarification and concentration. 
    4.4 Purification of the protein by ion-exchange Chromatography.
    4.5 Purification of the protein by preparative RP-HPLC (if needed).
    4.6 Dialysis and Lyophilization. 
  5. Detailedcharacterization of the protein 
    5.1 Polyacrylamide gel electrophoresis. 
    5.2 UV spectroscopy. 
    5.3 N-terminal amino acid sequence determination. 
    5.4 Analytical reversed-phase HPLC. 
    5.5 Biological activity in-vitro.