Bacterial Expression
E. coli is often the system of choice for biomanufacturing because of its amenability to genetic manipulation, low production cost, and rapid timelines for bioexpression.
Short affinity tags, such as polyhistidine, Flag, and Twin-Strep, are often fused to recombinant proteins to aid in detection and purification of proteins. After affinity capture, tags can be removed using recombinant proteases such as TEV, HRV3C, thrombin, or SUMOStar.
| Catalog # | Name | Timeline | Price |
|---|---|---|---|
| 1024 | Bacterial Scale-up Expression | Dependent on scale | Request |
| 25110 | Cloning into expression plasmid with 1 liter expression (18 or 37 degrees C) and affinity purification using Ni resin | 3-4 weeks | Request |
| 25120 | Cloning into expression plasmid with 1 liter expression (18 or 37 degrees C) and tandem affinity purification using Ni and streptactin resins | 3-4 weeks | Request |
| 25130 | Cloning into expression plasmid with 1 liter expression (18 or 37 degrees C) and tandem affinity purification using Ni and streptactin resins with a SEC polishing | 4 weeks | Request |