Difference between revisions of "Part:BBa K385004:Experience"

(Applications of BBa_K385004)
 
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[[Image:N25 + Gal-3.jpg|center|400 px]]
 
[[Image:N25 + Gal-3.jpg|center|400 px]]
  
A control culture of the same transformant was grown using glucose as the carbon source;  these conditions do not activate the GAL promoter. The results (Figure 2) show no GFP fluorescence.
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A control culture of the same transformant was grown using glucose as the carbon source;  these conditions do not activate the GAL promoter, and as expected no GFP fluorescence was detectable (data not shown).  
  
 
Overall the results indicate that the N-peptide can be successfully expressed as a protein fusion with other standard parts.
 
Overall the results indicate that the N-peptide can be successfully expressed as a protein fusion with other standard parts.

Latest revision as of 20:55, 24 October 2010

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Applications of BBa_K385004

The N-peptide tandem repeat reading frame was fused in-frame to GFP to make a translational fusion. It was placed under control of the yeast GAL1 promoter (BBa_J63006), and transformed into yeast Saccharomyces cerevisiae in the single copy shuttle vector pRS415.

The transformants were grown overnight in synthetic defined medium containing 2% w/v galactose, and observed using a fluorescence microscope optimised for GFP visualisation (Figure 1).

N25 + Gal-3.jpg

A control culture of the same transformant was grown using glucose as the carbon source; these conditions do not activate the GAL promoter, and as expected no GFP fluorescence was detectable (data not shown).

Overall the results indicate that the N-peptide can be successfully expressed as a protein fusion with other standard parts.

User Reviews

UNIQef0fc4e7629baf83-partinfo-00000000-QINU UNIQef0fc4e7629baf83-partinfo-00000001-QINU