Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems
By K. Terpe. Applied Microbiology and Biotechnology, 2002
1,443 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging
View Paper: https://www.semanticscholar.org/paper/62cf465bbf50dae7906de5492d721452086c9744
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Citations in the corpus
- Fusion Protein Linkers: Property, Design and Functionality (2012, background): “Besides their wide applications in biological research such as protein purification [1] and imaging [2], recombinant fusion proteins have also become an important category of biopharmaceuticals (Figure 1) [3, 4].”
- Overview of Affinity Tags for Protein Purification (2004, background): “Unfortunately, the phenylarsine oxide matrix used to purify thioredoxin fusion proteins often does not provide high-yield, high-purity product, likely because of nonspecific background protein binding (Terpe, 2003).”
- Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications (2012, background): “[4] Terpe, K.”
- Advanced genetic strategies for recombinant protein expression in Escherichia coli. (2005, background): “Several other affinity tags exist and have been extensively reviewed (Terpe, 2003).”
- A Versatile Nanotrap for Biochemical and Functional Studies with Fluorescent Fusion Proteins*S (2008, background): “Those limitations are often bypassed by fusing the protein of interest to specific epitope or protein tags including hemagglutinin, c-Myc, FLAG, or GST (7, 8 ). Curiously GFP, the most widely used labeling tag in cell biology, is rarely used for biochemical analyses, although various mono- and poly”
- Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. (2006, neutral): “Softag1, Softag 3 13, 8 Recognized by polyol-responsive mAb [46–48] c-myc 10 mAb-based puriWcation [31] T7-tag 11–16 mAb-based puriWcation [56]”