Team:Washington

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=== The Idealized Protein Purification System: Improving the lives of molecular biologists ===
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[1] Target Vector produces tagged protein of interest.
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Recombinant, purified protein production is a decades-old technology that has revolutionized research in biotechnology and medicine.  However, the traditional method of purified protein production is a time-consuming and laborious procedure requiring expensive and specialized equipment.  Our project, the Idealized Protein Purification (IPP) system, is an all-in-one protein expression and purification platform built on BioBrick standards that will reduce costs, save time, and simplify procedures associated with recombinant protein production.  The key to our IPP system is a novel combination of three subsystems: expression, secretion and display.  We use ''E. coli'' bacteria that we have genetically modified to be a chassis for expressing your favorite protein, secreting it to the media, then binding and displaying the protein on the cell surface.  At this point, collecting your favorite ''purified protein'' is as simple as pelleting and re-suspending a sufficient quantity of bacterial cells in an elution buffer.  The speed and simplicity of our IPP system exhibits the utility of synthetic biology for developing new techniques that improve upon established practices.
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[2] A secretion tag directs protein via secretion system into media.
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<div style="text-align:right">'''Continue to [https://2009.igem.org/Team:Washington/Project Project Description &gt;]'''</div>
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[3] A Nano-Tag binds to Display protein on cell surface.
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[4] Target protein released upon addition of elutant.
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The use of recombinant protein production using E. coli-based expression
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systems has revolutionized the fields of biotechnology and medicine.
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However, the ability to utilize such proteins hinges upon their capacity to
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be isolated from their expression systems.  Our project aims to create an
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all-in-one protein expression and purification system using BioBrick
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standards to greatly simplify protein production for synthetic biologists,
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reducing the time and cost involved in standard protein purification
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methods.  Our method uses a novel combination of two systems: secretion and
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display.  By fusing two tags to the protein it can be secreted into the
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expression media, and subsequently directed to bind to the outside of the
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cell.  To collect the pure proteins, cells only need to be spun down and
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then resuspended in an elution buffer, releasing the protein of interest.
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Our research exhibits the utility of synthetic biology for developing new
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techniques that improve upon established practices.''
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Latest revision as of 03:10, 22 October 2009

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IPP System Overview Target System Secretion System Display System Release System

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secretion
display
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The Idealized Protein Purification System: Improving the lives of molecular biologists

Recombinant, purified protein production is a decades-old technology that has revolutionized research in biotechnology and medicine. However, the traditional method of purified protein production is a time-consuming and laborious procedure requiring expensive and specialized equipment. Our project, the Idealized Protein Purification (IPP) system, is an all-in-one protein expression and purification platform built on BioBrick standards that will reduce costs, save time, and simplify procedures associated with recombinant protein production. The key to our IPP system is a novel combination of three subsystems: expression, secretion and display. We use E. coli bacteria that we have genetically modified to be a chassis for expressing your favorite protein, secreting it to the media, then binding and displaying the protein on the cell surface. At this point, collecting your favorite purified protein is as simple as pelleting and re-suspending a sufficient quantity of bacterial cells in an elution buffer. The speed and simplicity of our IPP system exhibits the utility of synthetic biology for developing new techniques that improve upon established practices.

Continue to Project Description >
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