The Nano-tag, a streptavidin-binding peptide for the purification and detection of recombinant proteins

Screening for soluble expression constructs using cell-free protein synthesis

“…Furthermore, the influence of several mutations to the amount of soluble protein can easily be tested. It was already shown that the comparatively low yields of the in vitro translation compared to the in vivo expression are sufficient for activity testing [16,[18][19][20]. Therefore, it is also possible to screen for activity as long as an activity assay for the particular protein does exist.…”

“…Thirty cycles of thermal cycling were carried out as follows: 94 • C for 30 s, 65 • C for 30 s and 72 • C for 45 s; finally, one cycle at 72 • C for 5 min. The PCR products were digested with XbaI/BamHI (Roche Molecular Biochemicals, Mannheim, Germany) and subsequently cloned into the adequately digested pASK-IBA2 vector (IBA, Göttingen, Germany) and pFA vector [16]. The pASK-IBA2 vector works with the tightly regulated tet promoter and is well suited for the expression of recombinant proteins in E. coli.…”

Arabidopsis Small Ubiquitin-Like Modifier Paralogs Have Distinct Functions in Development and Defense

“…The protein tag consisted of the HIS tag and the streptavidin binding peptide NANO15-tag (HN-tag) fused to the free N terminus (Lamla and Erdmann, 2004). Expression of the chimaeras was driven by the 35S promoter.…”

The nature of target-unrelated peptides recovered in the screening of phage-displayed random peptide libraries with antibodies

“…Peptides with specificity for SA have been well characterized and have been used as affinity tags for protein purification [19,20] and direct capture of bifunctional recombinant phage in immunoassays [21]. SA-binding peptides were originally identified in screenings of a PDPL by Devlin et al [22]; most of their peptides contained the motif HPQ, leading to the conclusion that the HPQ was responsible for SA-binding activity.…”