pET Expression Vectors |
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Novagen's® pET Systems
Efficiently clone and express your target protein by cloning your gene into one of our industry leading bacterial, mammalian or insect cell systems. Merck’s vast portfolio of expression vectors enables you to choose the perfect combination of promoters, epitope tags, antibiotic resistance, and host compatibility.pET E. coli T7 Expression Vectors
The pET System is the most powerful system for the cloning and expression of recombinant proteins in E. coli. Driven by the strong bacteriophage T7 promoter and translation signals, Novagen’s® pET System has been used to express thousands of different proteins in host cells expressing T7 polymerase. The pET System has continuously expanded to offer new technologies and options for expression. Collectively, our large collection of pET vector types, different host strains and companion products offer complete solutions for high level expression, purification and detection of target proteins:Browse all pET Vectors
Popular Novagen pET vectors
Unique Protein Expression Features |
Vector of Choice |
|---|---|
| high yield bioproduction of peptides and small proteins | pET-31b(+) |
| production of soluble, active target proteins in E. coli | |
| production of target proteins suitable for site-specific 32P-labeling | pET-33b(+) |
| Dsb tags for export and periplasmic folding of target proteins | |
| with popular GST fusion tags for enhanced production and solubility |
pET-41a(+), pET-41b(+), pET-41c(+) ,pET-42a(+), pET-42b(+), pET-42c(+) |
| designed for cloning and high-level expression of polypeptide sequences fused with the 495 aa NusA (Nus•Tag™) protein | |
| with Nus•Tag™ sequence plus N- and C-terminal His•Tag sequences | |
| with amino-terminal His•Tag™ sequence and minimal extraneous sequences | pET-45b(+) |
| prepared vector for ligation-independent cloning, with amino-terminal His•Tag™ sequence | pET-46 Ek/LIC |
| with HRV 3C Protease cleavage site for efficient fusion tag removal |
Nus•Tag™ fusion increases the solubility of recombinant annexin A1.
Soluble annexin A1 was purified on sequential His•Bind and Strep•Tactin columns (lanes 6-7). The N-terminal fusion tags were removed by thrombin cleavage and a subtractive His•Bind column (lanes 8-9).