Recombinant antibody expression can be performed in all types of systems. Many dissimilar cell lines can be used to express antibodies, containing mammalian cells such as CHO, or even yeast, plant. You can get the best service for Mammalian Cell-Based Protein Expression in Pleasanton.
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Each expression system has its own benefits for different applications and purposes.
The main difference between bacterial and mammalian expression systems lies in the anatomy of the cell. Bacteria do not have a nucleus, endoplasmic reticulum, or Golgi apparatus, all of which are key elements in cell transport and after translational modification.
Protein expression in bacteria
The most commonly used bacterial expression system is the E. coli cell line. E. coli cultures grow very quickly, making them easy to keep healthy and use.
Bacteria are easily transfused using methods such as heat shock. Unlike eukaryotes, cardiac cell walls and their simple anatomy can withstand drastic temperature fluctuations and survive shocking heat processes, while eukaryotes can suffer severe permanent damage that can interfere with proper cell expression, replication, or cell death.
The easiest way to see the benefits of E. coli is with several types of protein. In particular, cytosolic and secreted proteins with slight post-translational modifications can be easily developed in E. coli.
Unluckily, Tran’s membrane proteins, glycoproteins, and other membrane-bound proteins are not expressed willingly because there is not any endoplasmic reticulum to facilitate proper structural translation.
Protein expression in mammalian cells
Mammalian cells are usually more difficult to work with bacteria because they are much more fragile, generally produce fewer products, and can be much more expensive.
However, the use of mammalian cells for protein expression has the great advantage that they can produce mammalian proteins with all the correct post-translational modifications provided by natural structures.
Most post-translation changes occur during or immediately after translation. Eliminate waste proteins are produced in the endoplasmic reticulum, where there are enzymes that enable disulfide bonding, proper folding, and N-linked glycosylation.