Difference between revisions of "Part:BBa K5374021"
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<partinfo>BBa_K5374021 short</partinfo>
 
<partinfo>BBa_K5374021 short</partinfo>
  
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<p>A mutation of VEGF121 on two amino acids enhancing the formation of VEGF-VEGFR complex by the formation of an additional hydrogen bond</p>
  
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K5374021 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K5374021 SequenceAndFeatures</partinfo>
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<p>We have carefully redesigned the existing VEGF121 part by introducing targeted mutations at two key residues, R105S and P106Y, aiming to enhance its binding affinity to VEGFR and improve its biological function. Our efforts are demonstrated through rigorous experimental validation, including a scratch assay with MC3T3-E1 cells, which shows that the mutant significantly enhances cell migration and wound healing compared to the wild-type VEGF121. Additionally, we have meticulously documented our findings, following the Best New Improved Part award requirements. This includes detailed experimental protocols, quantitative results, and clear comparisons between the mutant and wild-type proteins under identical conditions. Our thorough documentation on the Part's Registry Main Page ensures that the new part is well-supported by experimental data, showcasing its superior performance. </p>
  
  

Revision as of 16:17, 24 September 2024


VEGF121(R105S, P106Y) Enhancing the Formation of VEGF-VEGFR Complex

A mutation of VEGF121 on two amino acids enhancing the formation of VEGF-VEGFR complex by the formation of an additional hydrogen bond

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 289
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 289
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 289
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 289
  • 1000
    COMPATIBLE WITH RFC[1000]

We have carefully redesigned the existing VEGF121 part by introducing targeted mutations at two key residues, R105S and P106Y, aiming to enhance its binding affinity to VEGFR and improve its biological function. Our efforts are demonstrated through rigorous experimental validation, including a scratch assay with MC3T3-E1 cells, which shows that the mutant significantly enhances cell migration and wound healing compared to the wild-type VEGF121. Additionally, we have meticulously documented our findings, following the Best New Improved Part award requirements. This includes detailed experimental protocols, quantitative results, and clear comparisons between the mutant and wild-type proteins under identical conditions. Our thorough documentation on the Part's Registry Main Page ensures that the new part is well-supported by experimental data, showcasing its superior performance.