Difference between revisions of "Part:BBa K4164997"
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This part includes the ddRFPB1 fused by a 3*GS Linker to the RXR , which can form a heterodimer with activated FXR-3*GS Linker-ddRFPA1 and exhibit red fluorescence. | This part includes the ddRFPB1 fused by a 3*GS Linker to the RXR , which can form a heterodimer with activated FXR-3*GS Linker-ddRFPA1 and exhibit red fluorescence. | ||
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We tried to determine the solubility of RXR-ddRFPB1 by purifying 6xHis-tagged proteins under native conditions and performing SDS-PAGE to compare the abundance of the band with the size of interest.As shown in the Figure 1, RXR-ddRFPB1(78.9kDa) is soluble and can be purified by Ni-NTA affinity chromatography. | We tried to determine the solubility of RXR-ddRFPB1 by purifying 6xHis-tagged proteins under native conditions and performing SDS-PAGE to compare the abundance of the band with the size of interest.As shown in the Figure 1, RXR-ddRFPB1(78.9kDa) is soluble and can be purified by Ni-NTA affinity chromatography. | ||
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| − | <p style="text-align: center;"><b>Fig.1 Purification of FXR-ddRFPA1 and RXR-ddRFPB1.Lane 1: protein contained in the pellet after bacterial disruption. Lane 2: RXR-ddRFPB1 purified from supernatant of bacteria liquid. Lane 3: FXR-ddRFPA1 purified from supernatant of bacteria liquid in optimized expression conditon | + | <p style="text-align: center;"><b>Fig.1 Purification of FXR-ddRFPA1 and RXR-ddRFPB1.Lane 1: protein contained in the pellet after bacterial disruption. Lane 2: RXR-ddRFPB1 purified from supernatant of bacteria liquid. Lane 3: FXR-ddRFPA1 purified from supernatant of bacteria liquid in optimized expression conditon.</b></p> |
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Latest revision as of 11:57, 12 October 2022
RXR-3*GS Linker-ddRFPB1
This part includes the ddRFPB1 fused by a 3*GS Linker to the RXR , which can form a heterodimer with activated FXR-3*GS Linker-ddRFPA1 and exhibit red fluorescence.
We tried to determine the solubility of RXR-ddRFPB1 by purifying 6xHis-tagged proteins under native conditions and performing SDS-PAGE to compare the abundance of the band with the size of interest.As shown in the Figure 1, RXR-ddRFPB1(78.9kDa) is soluble and can be purified by Ni-NTA affinity chromatography.
Fig.1 Purification of FXR-ddRFPA1 and RXR-ddRFPB1.Lane 1: protein contained in the pellet after bacterial disruption. Lane 2: RXR-ddRFPB1 purified from supernatant of bacteria liquid. Lane 3: FXR-ddRFPA1 purified from supernatant of bacteria liquid in optimized expression conditon.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 1867
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 357
Illegal AgeI site found at 1384 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 739