Insect expression systems, particularly the baculovirus system, are widely used for recombinant protein production due to their ability to express complex proteins with eukaryotic modifications. Here are some key characteristics: 

1.   Post-Translational Modifications: Insect cells, being eukaryotic, can perform post-translational modifications similar to mammalian cells, including glycosylation and proper protein folding, making them ideal for expressing complex proteins. 

2.   High Protein Yield: Insect expression systems, such as the baculovirus expression system, can produce high yields of recombinant proteins, especially for large or difficult-to-express proteins. 

3.    Versatility: The system allows expression of a wide range of proteins, including membrane proteins and proteins with disulfide bonds, which are often challenging in bacterial systems. 

4.   Fast Growth: Insect cells grow relatively quickly compared to mammalian cells, allowing for rapid protein production in a shorter time frame. 

5.   Scalability: Insect expression systems can be easily scaled from small lab cultures to large industrial bioreactors, making them suitable for both research and commercial applications. 

6.   Reduced Protease Activity: Insect cells generally have lower levels of proteases compared to mammalian systems, reducing the risk of recombinant protein degradation. 

Insect expression systems are valued for their ability to carry out complex post-translational modifications, high protein yield, versatility, and scalability, making them a powerful tool for expressing recombinant proteins, especially those difficult to produce in simpler systems. 

GenCefe provide one-stop solutions from codon optimization, gene synthesis, to protein expression and purification. In addition to four conventional expression systems of bacterial, yeast, insect cell, and mammalian cell, we have also developed a patented cell free expression technology, which is suitable for the production of difficult proteins such as toxic proteins and membrane proteins.