Heterologous protein expression often encounters yield, toxicity, solubility,
and stability problems. Our cell strains are specifically engineered to solve
these protein expression problems. Currently all of our cell strains are E.coli
strains. These E.coli strains are genetically engineered to over-express one or
more genes. These over-expressed genes may increase the yield, overcome the
toxicity, improve the solubility, stability, and/or activity of the recombinant
proteins. Following cell strains may be used to solve one or more problems in
gene cloning and protein expression.
These cell strains are for general cloning and expression studies.
- tRNA Plus
Different organisms use different set of genetic codons. Some
heavily used codons in mammal may be rarely used in E.coli. Codon starvation
results in no expression or low yield of some mammalian proteins. tRNA plus
strains are designed to solve these problems.
Many proteins have effects on cellular proliferation and
differentiation. As a result, they are toxic to the host cells. Majority
proteins have different degree of toxicity. The mechanism
of toxicity is different for each protein. We developed detoxification cell
strains to overcome toxicity of most recombinant proteins.
- Heat Shock
Heat shock proteins (hsps) are important in folding of many
proteins. They are directly or indirectly involved in protein folding,
solubility, stability, and function. We engineered cell strains over
expressing human hsps.
- Other Chaperones
- Molecular chaperones are important in cellular protein production. Some
chaperones are involved in protein folding. Others are required for protein
secretion. Still others are needed for disulfide bond formation. Lack or
insufficient chaperones result in non-functional, insoluble, or unstable
recombinant proteins. Chaperones are critical for the function of many
- We also provide customized cell strains for both academic and industrial
entities. We will make E.coli strains over expressing genes you specify.