One-Step Purification of Recombinant Proteins Using a Nanomolar-Affinity Streptavidin-Binding Peptide, the SBP-Tag

2001 ◽  
Vol 23 (3) ◽  
pp. 440-446 ◽  
Author(s):  
Anthony D. Keefe ◽  
David S. Wilson ◽  
Burckhard Seelig ◽  
Jack W. Szostak
Keyword(s):  
Recombinant Proteins ◽  
Binding Peptide ◽  
One Step ◽  
Streptavidin Binding

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

2004 ◽  
Vol 33 (1) ◽  
pp. 39-47 ◽  
Author(s):  
Thorsten Lamla ◽  
Volker A Erdmann
Keyword(s):  
Recombinant Proteins ◽  
Binding Peptide ◽  
Streptavidin Binding

Stable one-step technetium-99m labeling of His-tagged recombinant proteins with a novel Tc(I)–carbonyl complex

10.1038/12890 ◽  
1999 ◽  
Vol 17 (9) ◽  
pp. 897-901 ◽  
Author(s):  
Robert Waibel ◽  
Roger Alberto ◽  
Jörg Willuda ◽  
Ricarda Finnern ◽  
Roger Schibli ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Carbonyl Complex ◽  
Technetium 99M ◽  
One Step

One-Step Purification of Recombinant Proteins with the 6xHis Tag and Ni-NTA Resin

2003 ◽  
pp. 491-510 ◽  
Author(s):  
Joanne Crowe ◽  
Brigitte Steude Masone ◽  
Joachim Ribbe
Keyword(s):  
Recombinant Proteins ◽  
One Step

scholarly journals Development of a nanobody tagged with streptavidin-binding peptide and its application in a Luminex fluoroimmunoassay for alpha fetal protein in serum

RSC Advances ◽  
2020 ◽  
Vol 10 (40) ◽  
pp. 23767-23774
Author(s):  
Qi Chen ◽  
Danyang Sun ◽  
Hua Pei ◽  
Benchao Su ◽  
Kunlu Bao ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Binding Peptide ◽  
Immunological Diagnosis ◽  
Streptavidin Binding

A nanobody/streptavidin-binding peptide fusion protein was developed and proved to be a very promising immunological diagnosis reagent for disease-related biomarkers.

scholarly journals Control of protein trafficking by reversible masking of transport signals

2016 ◽  
Vol 27 (8) ◽  
pp. 1310-1319 ◽  
Author(s):  
Omer Abraham ◽  
Karnit Gotliv ◽  
Anna Parnis ◽  
Gaelle Boncompain ◽  
Franck Perez ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Trafficking ◽  
Protein Transport ◽  
Protein Import ◽  
Binding Peptide ◽  
Protein Traffic ◽  
Alternative Approach ◽  
Targeting Signal ◽  
Regulated Trafficking ◽  
Streptavidin Binding

Systems that allow the control of protein traffic between subcellular compartments have been valuable in elucidating trafficking mechanisms. Most current approaches rely on ligand or light-controlled dimerization, which results in either retardation or enhancement of the transport of a reporter. We developed an alternative approach for trafficking regulation that we term “controlled unmasking of targeting elements” (CUTE). Regulated trafficking is achieved by reversible masking of the signal that directs the reporter to its target organelle, relying on the streptavidin–biotin system. The targeting signal is generated within or immediately after a 38–amino acid streptavidin-binding peptide (SBP) that is appended to the reporter. The binding of coexpressed streptavidin to SBP causes signal masking, whereas addition of biotin causes complex dissociation and triggers protein transport to the target organelle. We demonstrate the application of this approach to the control of nuclear and peroxisomal protein import and the generation of biotin-dependent trafficking through the endocytic and COPI systems. By simultaneous masking of COPI and endocytic signals, we were able to generate a synthetic pathway for efficient transport of a reporter from the plasma membrane to the endoplasmic reticulum.

scholarly journals Heparin-binding peptide as a novel affinity tag for purification of recombinant proteins

2016 ◽  
Vol 126 ◽  
pp. 93-103 ◽  
Author(s):  
Jacqueline Morris ◽  
Srinivas Jayanthi ◽  
Rebekah Langston ◽  
Anna Daily ◽  
Alicia Kight ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Heparin Binding ◽  
Affinity Tag ◽  
Binding Peptide

scholarly journals Simplifying plant gene silencing and genome editing logistics by a one-Agrobacterium system for simultaneous delivery of multipartite virus vectors

2021 ◽  
Author(s):  
Verónica Aragonés ◽  
Flavio Aliaga ◽  
Fabio Pasin ◽  
José-Antonio Daròs
Keyword(s):  
Gene Silencing ◽  
Genome Editing ◽  
Recombinant Proteins ◽  
Viral Vectors ◽  
Tobacco Rattle Virus ◽  
Vector System ◽  
Efficient Production ◽  
Virus Induced Gene Silencing ◽  
Guide Rnas ◽  
One Step

Genome editing and gene expression engineering using CRISPR-Cas systems in plants usually rely on labor-intensive tissue culture approaches to generate stably transformed plants that express the components of the reaction. Viral vectors have demonstrated to be a quick and effective alternative to express multiple guide RNAs, DNA templates for homologous recombination, and even Cas nucleases. Here we have developed an improved vector system based on tobacco rattle virus (TRV) to simplify logistics in genome editing and gene silencing approaches. The new system consists in a single Agrobacterium tumefaciens clone co-transformed with two compatible mini binary vectors from which TRV RNA1 and an engineered version of TRV RNA2 are expressed. Sequences of recombinant proteins, gene fragments for virus-induced gene silencing (VIGS) or guide RNAs can be easily inserted by one-step digestion-ligation and homology-based cloning methods in the RNA2 plasmid to produce vectors with a size substantially smaller than usual. Using this new one-Agrobacterium TRV mini vector system, we show robust VIGS of an endogenous host gene after infiltration of bacterial suspensions at low optical densities, and efficient production of recombinant proteins in Nicotiana benthamiana. Most importantly, we also show highly efficient heritable genome editing in more than half of the seedling originating from inoculated N. benthamiana plants that express Cas9.

Controlled presentation of recombinant proteins via a zinc-binding peptide-linker in two and three dimensional formats

Biomaterials ◽  
2009 ◽  
Vol 30 (34) ◽  
pp. 6614-6620 ◽  
Author(s):  
Michael R. Doran ◽  
Brandon D. Markway ◽  
Tristan I. Croll ◽  
Sergio Sara ◽  
Trent P. Munro ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Three Dimensional ◽  
Zinc Binding ◽  
Binding Peptide
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