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Recombinant proteins have a broad range of applications from basic research to pharmaceutical development, they are widely used in research, medicine, and industry. They can be used to study the structure and function of proteins, to develop new drugs and vaccines, and to produce enzymes and other proteins for industrial applications.

Over the last 30 years, there have been considerable advances in the technologies for expressing recombinant proteins. Alpha Lifetech Inc. provides four main protein expression systems to produce recombinant proteins: Bacteria, yeast, insect cells and mammalian systemsAlpha Lifetech Inc. provides a portfolio of recombinant proteins from different hosts, different species, the products can be used for research and diagnostic reference purposes. Recombinant proteins includes enzymes, growth factors, cytokines, Fc receptor proteins, immune-checkpoint proteins and membrane proteins. These recombinant proteins can be used for a variety of applications, including cell culture, bioassays, and in vitro diagnostics.

 

 

Escherichia coli (E. coli) is a widely used organism to produce recombinant proteins. There are several advantages in E. coli system: Lower cost and time-saving. Very short doubling times with simple culture conditions (20 minute doubling time with ~10% mass/protein ratio). Plasmid design allows for wide use cases.

While the disadvantages are needed to be considered: E. coli is a prokaryotic organism, and therefore lacks the complex chaperone and folding machinery found in eukaryotic cells. This can lead to incorrect folding and aggregation of recombinant proteins, particularly for large or complex proteins. Post-translational modifications may have effects on stability and function of some proteins. Endotoxin level. Protein solubility: Some proteins may be insoluble or form inclusion bodies in E. coli, which can make purification more difficult and result in lower yields of active protein.

 

 

The Pichia (GS115, X33) and Saccharomyces cerevisiae (ATCC26612, ATCC38434) expression system combines the advantages of prokaryotic and eukaryotic protein expression systems. It is a cost-effective eukaryotic protein expression system. The medium is relatively cheap, and the culture conditions are not high, which is suitable for industrial scale-up. Compared with the prokaryotic protein expression system, the yeast protein expression system can perform some post-translational modifications on the expressed protein, such as glycosylation, acylation, lipidation, phosphorylation, etc., and can be used to prepare proteins with high additional Valuable protein reagents.

 

 

The baculovirus-insect cells (Sf9/Sf21) expression system, with its strong post-translational modification ability and high culture density, is suitable for the expression of various types of proteins and has become an excellent choice for expressing complex proteins and viral proteins.

 

 

Mammalian cells (HEK293, CHO) have become the host cell of choice to produce many biopharmaceuticals. Mammalian cell expression system can be post-translationally modified, and the expressed recombinant protein is close to the human conformation, so it is widely used in the production of therapeutic recombinant proteins.