Protein Expression :

E.Coli Expression System:
Our Bacterial Expression Service includes:

	Subcloning of the cDNA (provided by the customer) into an expression vector and confirm by sequencing. We can also pull the target cDNA from libraries for customer, please refer to V. Gene cloning service).
	Tagged protein will be tested for yield and solubility and then in adequate scale (1-10L culture) for affinity purification (Ni-NTA column or GST column).Tagged protein will be expressed in small scale for testing yield and solubility and then in 1L culture for large scale affinity purification.
	Expected yield: 5 mg/L, purity 90%-95%.
	The results of HPLC and protein gel picture will be provided for quality control purpose.

If the target protein cannot be expressed or is not soluble in E.Coli., customer can choose not to continue, a minimum charge will apply. The customer may require protein refolding. An additional charge will apply. Baculovirus Expression System: The baculovirus-insect cell expression system is widely used to produce recombinant proteins for many different biomedical applications. It provides researchers with the means to generate milligram quantities of recombinant proteins that are ideal for functional studies and structural analysis. The system typically produces overexpressed recombinant proteins with proper folding, disulfide bond formation and oligomerization. Additionally, this system is capable of performing several post-translational modifications, including N- and O-linked glycosylation, phosphorylation, acetylation, amidation, methylation, isoprenylation, signal peptide cleavage and proteolytic cleavage. The sites where these modifications occur are often identical to those of the authentic protein in its native cellular environment. Baculovirus-expressed recombinant proteins are usually localized in the same subcellular compartment as the authentic protein. The baculovirus-insect cell expression system is widely used to produce recombinant proteins for many different biomedical applications. It provides researchers with the means to generate milligram quantities of recombinant proteins that are ideal for functional studies and structural analysis. Comparing to traditional E.coli system, the baculovirus system is often chosen for protein production due to it's a higher eukaryotic expression system with easy cell culture. It can be readily adapted to high-density suspension culture for large-scale expression. The system typically produces overexpressed recombinant proteins containing proper folding, disulfide bond formation and oligomerization. Additionally, this system is capable of performing several post-translational modifications, including N- and O-linked glycosylation, phosphorylation, acylation, amidation, carboxymethylation, isoprenylation, signal peptide cleavage and proteolytic cleavage. The sites where these modifications occur are often identical to those of the authentic protein in its native cellular environment. Baculovirus-expressed recombinant proteins are usually localized in the same subcellular compartment as the authentic protein.