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