ArticleProtein expression and purification2008
BacMam system for high-level expression of recombinant soluble and membrane glycoproteins for structural studies.
Article in Protein expression and purification, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.
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Who cites it
92 citing papers in PubMed, 137 citations in OpenAlex.
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- The Use of Baculovirus-Mediated Gene Expression in Mammalian Cells for Recombinant Protein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Recombinant Protein Production in Suspension Mammalian Cells Using the BacMam Baculovirus Expression System.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Specific protonation of acidic residues confers KThe Journal of biological chemistry · 2024Article
- A Na pump with reduced stoichiometry is up-regulated by brine shrimp in extreme salinities.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Cell-cycle arrest at the G1/S boundary enhances transient voltage-gated ion channel expression in human and insect cells.Cell reports methods · 2023Article
- Deep learning driven de novo drug design based on gastric proton pump structures.Communications biology · 2023Article
32 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Baculovirus mediated gene transduction of mammalian cells (BacMam) is an emerging technique for rapid recombinant protein expression in mammalian cells. We constructed two baculovirus transfer vectors that incorporate several mammalian transcriptional regulatory elements necessary for high-level protein expression in mammalian cells. Using these vectors, we show that the BacMam system in combination with the 293 GnTI(-) cell line can be used for production of milligram quantities of soluble glycoproteins. Moreover, for crystallization trials, the purified glycoproteins are sensitive to EndoH treatment resulting in a loss of the bulk of the attached N-linked glycosylation. In addition, we also show that a combination of the BacMam system and 293 GnTI(-) cell line can be used for producing milligram quantities of a GPCR-protein ligand complex suitable for crystallization trials.
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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.