The Protein Production Platform of NTU
Welcome to the Protein Production Platform (PPP) at NTU School of Biological Sciences. We have created this website to make our collaboration with you as smooth as possible. You will find a detailed description of our pipeline as well as instructions for submitting your targets and constructs on this page.
We use technology and a workflow that is largely identical to that of the former Biotechnology unit at the Structural Genomics Consortium at Karolinska Institutet in Stockholm, Sweden. In addition, we create in-house solutions such as new expression vectors to better serve your protein production needs.
In-silico to in-vitro
Use the LIMS to create and manage your protein constructs
The platform will clone your protein constructs into E. coli
High-throughput protein purification
Your protein constructs will be purified using IMAC and SEC
Purification using affinity chromatography
All constructs will be fused to a N-terminal cleavable HIS6-tag
Expression in insect cells for difficult proteins
We are currently implementing high-throughput cloning using baculovirus
Transmembrane proteins will be screened for optimal detergent conditions
Multiple quality control steps
All protein batches will be verified using mass spectrometry and/or sequencing
Receive plasmids, expression strain glycerol stocks and protein batches
In short, we are a high-throughput protein production facility with a cloning capacity of roughly 2*96 clones per month and a large-scale purification capacity of 12 proteins per week by using Escherichia coli as expression host. We also perform cloning, small-scale expression tests and large-scale protein expression in insect cells and most recently, mammalian cells. Please contact us for more details.
We have relocated from Proteos, Biopolis to NTU School of Biological Sciences. Our current visiting address is 60 Nanyang Drive, SBS-02s-94, Singapore 637551.
The PPP team
We now offer bacterial expression vectors that encode an N-terminal SUMO tag (pSUMO-LIC) and an N-terminal thioredoxin tag (pNH-TrxT).
Solubility-enhancing effects are target-dependent. Please note that solubility does not necessarily imply good folding (the fusion protein may exist mainly as soluble aggregates), and that tag removal may result in loss of solubility and stability. Caveat emptor!
Talk to us if you need suggestions, and good luck!