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Self-assembling membranes Results.html
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(New page: {{SLOtemp| Content= __NOTOC__ ==Results== <br> The genes encoding protein domains were fused according to our BioBrick standard. The proteins APH1-p53, APH-p53, p53-APH, BCR-p53 and p53-B...)
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(New page: {{SLOtemp| Content= __NOTOC__ ==Results== <br> The genes encoding protein domains were fused according to our BioBrick standard. The proteins APH1-p53, APH-p53, p53-APH, BCR-p53 and p53-B...)
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Revision as of 14:57, 21 October 2009
{{SLOtemp| Content=
Results
The genes encoding protein domains were fused according to our BioBrick standard. The proteins APH1-p53, APH-p53, p53-APH, BCR-p53 and p53-BCR were expressed in E. coli BL21(DE3) pLysS mostly in form of inclusion bodies (Figure 1, Figure 2, Figure 3).
Figure 1: Production and purification of APH1-p53. SDS-PAGE analysis of the cell lysate supernatant (lane 1), insoluble fraction (lane 2), and purified polypeptide (lane 3). The band of calculated size of the polypeptide APH1-p53, 8.44 kDa is visible and was confirmed by mass spectrometry.
Figure 1: Production and purification of APH1-p53. SDS-PAGE analysis of the cell lysate supernatant (lane 1), insoluble fraction (lane 2), and purified polypeptide (lane 3). The band of calculated size of the polypeptide APH1-p53, 8.44 kDa is visible and was confirmed by mass spectrometry.
