Difference between revisions of "Part:BBa K5374025:Design"
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+ | __NOTOC__ | ||
+ | <partinfo>BBa_K5374003 short</partinfo> | ||
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+ | <partinfo>BBa_K5374003 SequenceAndFeatures</partinfo> | ||
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+ | ===Design Notes=== | ||
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+ | The fusion protein was designed to balance the strong collagen-binding affinity of the FTD with the bioactivity of BMP-4. Codon optimization was applied to enhance expression in E. coli, ensuring efficient production and folding of the fusion protein. Special attention was given to preserving the osteogenic properties of BMP-4, allowing for controlled release and effective stimulation of bone formation when embedded in collagen matrices. | ||
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+ | |||
+ | ===Source=== | ||
+ | |||
+ | The FTD is derived from proteins involved in ECM interactions, particularly those associated with collagen and tissue repair. BMP-4 is a well-characterized growth factor in the TGF-β superfamily that plays a crucial role in osteogenesis and bone healing. |
Latest revision as of 12:04, 24 September 2024
DDR.A receptor domain activated by collagen, playing a role in ECM remodeling.
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 253
Illegal EcoRI site found at 337
Illegal EcoRI site found at 820
Illegal PstI site found at 259 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 253
Illegal EcoRI site found at 337
Illegal EcoRI site found at 820
Illegal PstI site found at 259 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 253
Illegal EcoRI site found at 337
Illegal EcoRI site found at 820
Illegal BglII site found at 459 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 253
Illegal EcoRI site found at 337
Illegal EcoRI site found at 820
Illegal PstI site found at 259 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 253
Illegal EcoRI site found at 337
Illegal EcoRI site found at 820
Illegal PstI site found at 259
Illegal NgoMIV site found at 588 - 1000COMPATIBLE WITH RFC[1000]
Design Notes
The fusion protein was designed to balance the strong collagen-binding affinity of the FTD with the bioactivity of BMP-4. Codon optimization was applied to enhance expression in E. coli, ensuring efficient production and folding of the fusion protein. Special attention was given to preserving the osteogenic properties of BMP-4, allowing for controlled release and effective stimulation of bone formation when embedded in collagen matrices.
Source
The FTD is derived from proteins involved in ECM interactions, particularly those associated with collagen and tissue repair. BMP-4 is a well-characterized growth factor in the TGF-β superfamily that plays a crucial role in osteogenesis and bone healing.