Difference between revisions of "Part:BBa K1846007"

<p>We characterised this construct by analysing the soluble protein fraction of the cell lysate (Figure 1,2). Under the TetR regulation, tfa gene is expressed under a tight control, and can thus be visualised on the gel, 194 aa, MW: 21602.2 Da, Figure 1, samples 7,8,9 & 11,12 and 13; Figure 2, samples 4,5 and 6. Tfa gene circuit does not produce tfa protein bands, Figure 1, samples 1, 2 and 3. We attribute the lack of bands in these samples to protein overexpression and aggregation into insoluble fraction. Under regulation of TetR, even when induced, the expression of tfa is considerably lower than when unregulated and hence, we hypothesise, a considerable amount of soluble material can be recovered. Our next step is to analyse the cell pellet to determine the presence of the tfa gene in the insoluble fraction.</p>

<p>We characterised this construct by analysing the soluble protein fraction of the cell lysate (Figure 1,2). Under the TetR regulation, tfa gene is expressed under a tight control, and can thus be visualised on the gel, 194 aa, MW: 21602.2 Da, Figure 1, samples 7,8,9 & 11,12 and 13; Figure 2, samples 4,5 and 6. Tfa gene circuit does not produce tfa protein bands, Figure 1, samples 1, 2 and 3. We attribute the lack of bands in these samples to protein overexpression and aggregation into insoluble fraction. Under regulation of TetR, even when induced, the expression of tfa is considerably lower than when unregulated and hence, we hypothesise, a considerable amount of soluble material can be recovered. Our next step is to analyse the cell pellet to determine the presence of the tfa gene in the insoluble fraction.</p>

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