Jim SwartzSummaryAffiliation: Stanford University Country: USA Publications
Research Grants
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Detail Information
Publications
Developing cell-free biology for industrial applicationsJim Swartz
Department of Chemical Engineering, Stauffer III, Rm 113, Stanford University, Stanford, CA 94305 5025, USA
J Ind Microbiol Biotechnol 33:476-85. 2006..Although many challenges remain, this newly expanded ability to activate and control protein production holds much promise for both research and commercial applications...- Rapid expression of vaccine proteins for B-cell lymphoma in a cell-free systemJunhao Yang
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Bioeng 89:503-11. 2005..Between the two amino-terminal GM-CSF fusion proteins, GM-VL-VH showed a higher total and soluble yield than GM-VH-VL... 
Cell-free production of Gaussia princeps luciferase--antibody fragment bioconjugates for ex vivo detection of tumor cellsKedar G Patel
Department of Chemical Engineering, Stanford University, 381 North South Mall, Stanford, CA 94305 5025, USA
Biochem Biophys Res Commun 390:971-6. 2009..GLuc-scFv conjugates were shown to differentiate between cells expressing a surface target of the scFv and cells that did not carry this marker...- Multiply mutated Gaussia luciferases provide prolonged and intense bioluminescenceJohn P Welsh
Department of Chemical Engineering, Stanford University, 381 North South Mall, Stanford, CA 94305 5025, USA
Biochem Biophys Res Commun 389:563-8. 2009.... - Cell-free metabolic engineering promotes high-level production of bioactive Gaussia princeps luciferaseAaron R Goerke
Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA
Metab Eng 10:187-200. 2008..The cell-free product had a specific activity of 4.2x10(24)photons/s/mol, the highest reported activity for any characterized luciferase... 
Cell-free production of scFv fusion proteins: an efficient approach for personalized lymphoma vaccinesGregory Kanter
Department of Medicine, Division of Oncology, Stanford University Medical Center, Stanford, CA 94305, USA
Blood 109:3393-9. 2007..The cell-free E coli system offers a platform for rapidly generating individualized vaccines, thereby allowing much more efficient application in the clinic...- Development of cell-free protein synthesis platforms for disulfide bonded proteinsAaron R Goerke
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Bioeng 99:351-67. 2008..Establishing general CFPS platforms enhances the potential for cell-free protein synthesis to reliably produce complex protein products at low production and capital costs with very rapid process development timelines... - Total amino acid stabilization during cell-free protein synthesis reactionsKara A Calhoun
Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA
J Biotechnol 123:193-203. 2006..The extract from strain KC6 maintains stable amino acid concentrations of all 20 amino acids in a 3-h batch reaction. Yields for three different proteins improved 75-250% relative to cell-free expression using the control extract... - Cell-free synthesis and maturation of [FeFe] hydrogenasesMarcus E Boyer
Department of Chemical Engineering, Stanford University, 381 North South Mall, Stanford, California 94305, USA
Biotechnol Bioeng 99:59-67. 2008.... - Escherichia coli-based cell-free synthesis of virus-like particlesBradley C Bundy
Department of Chemical Engineering, Stanford University, Stanford, California 94305 5025, USA
Biotechnol Bioeng 100:28-37. 2008..The scalability of this technology was tested without loss in production yields. To our knowledge, this is the first time a prokaryote-based in vitro transcription/translation system has generated a virus-like particle... - Expression of active murine granulocyte-macrophage colony-stimulating factor in an Escherichia coli cell-free systemJunhao Yang
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Prog 20:1689-96. 2004..Finally, successful folding of the cell-free synthesized GM-CSF-his6 was confirmed by its cell-proliferation activity after purification with a Ni2+ chelating column... - Cell-free protein synthesis with prokaryotic combined transcription-translationJames R Swartz
Department of Chemical Engineering, Stanford University, CA, USA
Methods Mol Biol 267:169-82. 2004..We describe the preparation of materials necessary for the expression, quantification, and purification of rDNA proteins from active Escherichia coli extracts... - Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesisMichael C Jewett
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Bioeng 86:19-26. 2004.... - A cell-free microtiter plate screen for improved [FeFe] hydrogenasesJames A Stapleton
Department of Chemical Engineering, Stanford University, Stanford, California, United States of America
PLoS ONE 5:e10554. 2010..Directed evolution has been used to improve the characteristics of a range of natural catalysts, but has been largely unsuccessful for [FeFe] hydrogenases because of a lack of convenient screening platforms... - Cell-free production of transducible transcription factors for nuclear reprogrammingWilliam C Yang
Department of Bioengineering, Stanford University, California 94305, USA
Biotechnol Bioeng 104:1047-58. 2009.... - Continued protein synthesis at low [ATP] and [GTP] enables cell adaptation during energy limitationMichael C Jewett
Department of Chemical Engineering, Stanford University, Stanford, CA 94305 5025, USA
J Bacteriol 191:1083-91. 2009..We anticipate that cell-free studies in which complex metabolic systems are activated will be valuable tools for elucidating the behavior of such systems... - High-level cell-free synthesis yields of proteins containing site-specific non-natural amino acidsAaron R Goerke
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Bioeng 102:400-16. 2009..The desired specificity for incorporation of the nnAA by the cell-free system was confirmed. Additionally, the modified proteins were enzymatically active and reactive for copper(I)-catalyzed (3 + 2) cycloadditions (click chemistry)... - Energy systems for ATP regeneration in cell-free protein synthesis reactionsKara A Calhoun
Department of Chemical Engineering, Stanford University, Stanford, CA, USA
Methods Mol Biol 375:3-17. 2007..We describe the various types of energy sources used in cell-free reactions, give examples of the major classes, and demonstrate protocols for successful use of three recently developed energy systems: PANOxSP, cytomim, and glucose... - Comparing the functional properties of the Hsp70 chaperones, DnaK and BiPJeanne Bonomo
Department of Chemical Engineering, Stanford University, 381 North South Mall, Stanford, CA 94305 5025, USA
Biophys Chem 149:58-66. 2010..Our results support previous reports suggesting that DnaK provides both post-translational and co-translational folding assistance while BiP predominantly provides folding assistance that is contemporaneous with translation... - An integrated cell-free metabolic platform for protein production and synthetic biologyMichael C Jewett
Department of Chemical Engineering, Stanford University, Stanford, CA 94305 5025, USA
Mol Syst Biol 4:220. 2008.... - Quantitative polysome analysis identifies limitations in bacterial cell-free protein synthesisKelly A Underwood
Biophysics Program, D118 Fairchild Science Building, Stanford, California 94305-5126, USA
Biotechnol Bioeng 91:425-35. 2005.... - Substrate replenishment extends protein synthesis with an in vitro translation system designed to mimic the cytoplasmMichael C Jewett
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Bioeng 87:465-72. 2004..4 mg/mL of CAT. These results underscore the critical role that nucleotides play in the combined transcription-translation reaction and highlight the importance of understanding metabolic processes influencing substrate depletion... - Efficient and scalable method for scaling up cell free protein synthesis in batch modeAlexei M Voloshin
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Bioeng 91:516-21. 2005..We believe that this approach provides a general reaction scale-up technology that will be suitable for any protein target, cell free system, and reaction volume... - Energizing cell-free protein synthesis with glucose metabolismKara A Calhoun
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Bioeng 90:606-13. 2005.... - Rapid expression of functional genomic librariesKim A Woodrow
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
J Proteome Res 5:3288-300. 2006..These improvements in the parallel synthesis of linear ETs combined with enhanced in vitro enzyme activation help to make CFPS systems more attractive platforms for high-throughput evaluation of protein function... - Cell-free production of active E. coli thioredoxin reductase and glutathione reductaseKurtis G Knapp
Department of Chemical Engineering, Stanford University, Stanford, CA 94305 5025, USA
FEBS Lett 559:66-70. 2004..The specific activity for both TR and GR decreased without FAD supplementation. This research demonstrates that CFPS can be used to produce enzymes that are multimeric and require a cofactor... - An economical method for cell-free protein synthesis using glucose and nucleoside monophosphatesKara A Calhoun
Department of Chemical Engineering, Stanford University, Stanford, CA 94305-5025, USA
Biotechnol Prog 21:1146-53. 2005..The glucose/NMP cell-free reaction system dramatically reduces reagent costs while supplying high protein yields... - A sequential expression system for high-throughput functional genomic analysisKim A Woodrow
Department of Chemical Engineering, Stanford University, Stanford, CA 94305 5025, USA
Proteomics 7:3870-9. 2007..This sequential CFPS system provides a unique format for the functional genomic identification of broadly diverse metabolic activities... - Enhancing multiple disulfide bonded protein folding in a cell-free systemGang Yin
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Bioeng 86:188-95. 2004..Taken together, the modifications enabled the production of more than 60 microg/mL of bioactive PA in a simple 3-h batch reaction... - Tyrosine, cysteine, and S-adenosyl methionine stimulate in vitro [FeFe] hydrogenase activationJon M Kuchenreuther
Department of Chemical Engineering, Stanford University, Stanford, California, United States of America
PLoS ONE 4:e7565. 2009..This unique [6Fe-6S] complex contains multiple non-protein moieties and requires several maturation enzymes for its assembly. The pathways and biochemical precursors for H-cluster biosynthesis have yet to be elucidated... - Efficient production of a bioactive, multiple disulfide-bonded protein using modified extracts of Escherichia coliDong-Myung Kim
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Bioeng 85:122-9. 2004..This result not only demonstrates efficient production of complex proteins, it also emphasizes the control and flexibility offered by the cell-free approach... - Simultaneous expression and maturation of the iron-sulfur protein ferredoxin in a cell-free systemMarcus E Boyer
Department of Chemical Engineering, Stanford University, California 94305, USA
Biotechnol Bioeng 94:128-38. 2006..To our knowledge, this is the first demonstration of directed, high-yield production and maturation of an Fe-S protein in a cell-free system... - Streamlining Escherichia coli S30 extract preparation for economical cell-free protein synthesisDavid V Liu
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Prog 21:460-5. 2005..These insights suggest that consistent cell extract can be produced more quickly and with considerably less expense for large-scale cell-free protein production, especially when combined with high-density fermentation protocols... - Evidence for an additional disulfide reduction pathway in Escherichia coliKurtis G Knapp
Department of Chemical Engineering, Stanford University, 381 North South Mall, Stanford, CA 94305, USA
J Biosci Bioeng 103:373-6. 2007..However, significant glutathione reductase activity remained. The unknown glutathione reductase pathway is disabled by iodoacetamide, is inhibited by NADH, and appears to use NADPH as an electron source... - Rapid expression and purification of 100 nmol quantities of active protein using cell-free protein synthesisMichael C Jewett
Department of Chemical Engineering, Stanford University, Stanford, California 94305-5025, USA
Biotechnol Prog 20:102-9. 2004..To our knowledge, this is the largest amount of actively expressed protein to be reported in a simple, fed-batch cell-free protein synthesis reaction... - High yield cell-free production of integral membrane proteins without refolding or detergentsJessica J Wuu
Department of Chemical Engineering, Stanford University, Stanford, CA 94305, USA
Biochim Biophys Acta 1778:1237-50. 2008..Whereas TetA incorporates efficiently into vesicle membranes with over two-thirds of the synthesized protein being inserted, MtlA yields appear to be limited by insufficient concentrations of a membrane-associated chaperone... - Cell-free synthesis of proteins that require disulfide bonds using glucose as an energy sourceKurtis G Knapp
Department of Chemical Engineering, Stanford University, Stanford, California 94305, USA
Biotechnol Bioeng 97:901-8. 2007..This new protocol offers an economically feasible cell-free system for the production of secreted mammalian proteins as human therapeutics or vaccines...
Research Grants
- Increasing The Utility Of Cell-Free Protein SynthesisJames Swartz; Fiscal Year: 2003..When successful, this project will provide exciting new technology for the efficient synthesis and modification of a wide variety of proteins. ..
- Designing Proximal Chaperones for Cell-Free Protein SynthesisJames Swartz; Fiscal Year: 2007..If successful, the project will produce new knowledge about eukaryotic protein folding and will also produce improved technology for the production of important protein therapeutics. ..