ArticleFrontiers in physiology2017
Preparative SDS PAGE as an Alternative to His-Tag Purification of Recombinant Amelogenin.
Article in Frontiers in physiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Comparative antibacterial activity of N-terminal and C-terminal domains of a recombinant endolysin againstApplied and environmental microbiology · 2025Article
- Scale up of fermentation of recombinant Escherichia coli for efficient production of spider drag silk protein MaSp1s and its dimers.Microbial cell factories · 2025Article
- Micropreparative Gel Electrophoresis for Purification of Nanoscale Bioconjugates.Bioconjugate chemistry · 2024Article
- Gel Protein Extraction's Impact on Conformational Epitopes of Linear Non-Tagged MPT64 Protein.Gels (Basel, Switzerland) · 2023Article
- Regaining enamel color quality using enamel matrix derivative.Medical molecular morphology · 2023Article
- The Establishment and Application of Indirect 3AB-ELISA for the Detection of Antibodies against Senecavirus A.Viruses · 2023Article
- A novel chimeric recombinant protein PDHB-P80 ofMolecular biology research communications · 2020Article
- Nrp-1 Mediated Plasmatic Ago2 Binding miR-21a-3p Internalization: A Novel Mechanism for miR-21a-3p Accumulation in Renal Tubular Epithelial Cells during Sepsis.BioMed research international · 2020Article
- Comparison of simple and rapid extracting methods of free-tagsJournal of advanced pharmaceutical technology & researchArticle
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Recombinant protein technology provides an invaluable source of proteins for use in structure-function studies, as immunogens, and in the development of therapeutics. Recombinant proteins are typically engineered with "tags" that allow the protein to be purified from crude host cell extracts using affinity based chromatography techniques. Amelogenin is the principal component of the developing enamel matrix and a frequent focus for biomineralization researchers. Several groups have reported the successful production of recombinant amelogenins but the production of recombinant amelogenin free of any tags, and at single band purity on silver stained SDS PAGE is technically challenging. This is important, as rigorous structure-function research frequently demands a high degree of protein purity and fidelity of protein sequence. Our aim was to generate His-tagged recombinant amelogenin at single band purity on silver stained SDS PAGE for use in functionality studies after His-tag cleavage. An acetic acid extraction technique (previously reported to produce recombinant amelogenin at 95% purity directly from
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.