Difference between revisions of "Part:BBa K5101006:Design"

(Design Notes)
(Source)
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===Source===
 
===Source===
  
The genes encoding these antibody fragments were synthesized based on sequences adapted for bacterial expression and optimized for E. coli, including an ompA signal sequence to direct the proteins to the periplasm. This localization is critical for proper protein folding and disulfide bond formation, essential for the functionality of the antibody. Certolizumab Pegol, used as the model for these fragments, is known for its efficacy in neutralizing TNF-α without Fc-mediated functions, which can be advantageous in reducing immunogenicity. For validation and scientific comparison, similar sequences used in this design are accessible in the NCBI database, which provides extensive data on various therapeutic antibodies.
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The genes encoding these antibody fragments were synthesized based on sequences adapted for bacterial expression and optimized for <i>E. coli</i>, including an ompA signal sequence to direct the proteins to the periplasm. This localization is critical for proper protein folding and disulfide bond formation, essential for the functionality of the antibody. Certolizumab Pegol, used as the model for these fragments, is known for its efficacy in neutralizing TNF-&#945; without Fc-mediated functions, which can be advantageous in reducing immunogenicity. For validation and scientific comparison, similar sequences used in this design are accessible in the NCBI database, which provides extensive data on various therapeutic antibodies.
  
 
===References===
 
===References===

Revision as of 02:37, 25 September 2024


Certolizumab (Anti-TNF-α )Light Chain With OmpA


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

The genes encoding these antibody fragments were synthesized based on sequences adapted for bacterial expression and optimized for E. coli, including an ompA signal sequence to direct the proteins to the periplasm. This localization is critical for proper protein folding and disulfide bond formation, essential for the functionality of the antibody. Certolizumab Pegol, used as the model for these fragments, is known for its efficacy in neutralizing TNF-α without Fc-mediated functions, which can be advantageous in reducing immunogenicity. For validation and scientific comparison, similar sequences used in this design are accessible in the NCBI database, which provides extensive data on various therapeutic antibodies.

Source

The genes encoding these antibody fragments were synthesized based on sequences adapted for bacterial expression and optimized for E. coli, including an ompA signal sequence to direct the proteins to the periplasm. This localization is critical for proper protein folding and disulfide bond formation, essential for the functionality of the antibody. Certolizumab Pegol, used as the model for these fragments, is known for its efficacy in neutralizing TNF-α without Fc-mediated functions, which can be advantageous in reducing immunogenicity. For validation and scientific comparison, similar sequences used in this design are accessible in the NCBI database, which provides extensive data on various therapeutic antibodies.

References