Part:BBa_K1694023
Pcons+B0034+Lpp-OmpA-N+scFv(Anti-VEGF)
Introduction:
By ligating the constitutive promoter (BBa_J23101), strong ribosome binding site (BBa_B0034) and Lpp-OmpA(BBa_K1694002) connected to anti-VEGF (BBa_K1694003), we were able to display scFv(anti-VEGF) outside the E. coli cell membrane.
This year we want to supply a customized platform. We provide two plasmids libraries of Pcon+RBS+OmpA-scFv and Pcons+RBS+Fluorescence+Ter for customers. Therefore,customers can choose any scFv and fluorescence proteins combination they want. We will co-transform the two plasmids, which helps us tailor our product to the wishes of our customers.
Introduction of basic parts:
Lpp-OmpA-N
Anti-VEGF
Experiment
1.Cloning
After assembling the DNA sequences from the basic parts, we recombined each Pcons+RBS+Lpp-OmpA-N+scFv gene to pSB1C3 backbones and conducted a PCR experiment to check the size of each part. The DNA sequence length of these parts is around 1100~1300 bp. In this PCR experiment, the scFv product's size should be near at 1300~1500 bp. The Fig.2 showed the correct size of the scFv, and proved that we successfully ligated the scFv sequence onto an ideal backbone.
2. Co-transform (Two plasmids)
(1) Parts
(2) Cell staining
After cloning the part of anti-VEGF, we were able to co-transform anti-VEGF with different fluorescence protein into our E. coli.
The next step was to prove that our co-transformed product have successfully displayed scFv of anti-VEGF and expressed fluorescence protein.
To prove this, we conducted the cell staining experiment by using the co-transformed E. coli to detect VEGF in the cancer cell line.
Modeling
In the modeling part, we discover optimum protein expression time by using the genetic algorithm (GA) in Matlab.
We want to characterize the actual kinetics of this Hill-function based model that accurately reflects protein expression time.
By using the differential function which was derived from these optimum parameters which were calculated by GA can help us to simulate the optimum protein expression.
When we have the simulated protein expression rate, the graph of protein expression versus time can be drawn.Thus, we can find the optimum protein expression time. However, the simulated protein expression curve is slower than the experimental curve by one hour. Therefore, to find the most exact optimum protein expression time, we infer that subtracting one hour of the optimum protein expression time would be correct.
Co-transform
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 7
Illegal NheI site found at 30 - 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 451
- 1000COMPATIBLE WITH RFC[1000]
None |