Recombinant Protein

ITI BioChem is specialized in providing recombinant protein. The recombinant protein is defined as a modified or manipulated protein encoded by a recombinant DNA. The recombinant DNA comprises of a plasmid in which the gene(s) of a target protein of interest is cloned downstream of a promoter region.
Recombinant protein production, as one of the recombinant protein technologies, plays a critical role in academic research and biotech/pharmaceutical drug discoveries.
Comparison of Protein Expression Systems
The selection of the system depends on the type of protein,the requirements for functional activity and the desired yield.These expression systems include mammalian, bacterial, yeast and insect .Several factors need to be taker into consideration, including target protein property, intended ,application, protein yield and cost. Furthermore, challenges exist for many protein expression projects, especially for large protein, membrane protein, and proteins with heavy post-translational modifications. Each system has advantages and challenges, and choosing the right system is important for successful recombinant protein expression.
Bacterial expression system
Offer large scale production of recombinant protein in a short time.
Yeast expression system
This system is used to express secretary as well as intracellular proteins. This system offers high protein yield, lesser expression time, post translational modifications and requires simple media. This system can be optimized for high level protein expression (grams) using fermentors.
Insect cell expression system
This system is most similar to mammalian expression systems. It can be used both in adherent and suspension cultures. Purification process is easy and baculoviruses are safe to work with compared to mammalian viruses.
Mammalian expression system
This system offers desired post translational modifications and proper protein folding.
Cell free expression system
Unlike those mentioned above, here the protein is expressed in a cell free environment using cell extract, DNA template, amino acids and cofactors. It is a simple process, protein expression and purification can be done in a short period of time (1-2 days). Labeling of proteins for structural studies like NMR, X-ray crystallography with labelled unnatural amino acids (Se-Met), heavy isotopes (C13, N15) can be done easily.