Difference between revisions of "Part:BBa K1896004"

 
 
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<partinfo>BBa_K1896004 short</partinfo>
 
<partinfo>BBa_K1896004 short</partinfo>
  
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This is an improved version of [[Part:BBa_K283010|Part:BBa_K283010]], which encodes for the core Streptavidin protein of ''Streptomyces avidinii''. The start codon was replaced by a GSTGS linker, a His-tag was added to the C-terminus and one BsaI site was removed.
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This is an improved version of [[Part:BBa_K283010|Part:BBa_K283010]], which encodes for the core Streptavidin protein of ''Streptomyces avidinii''. The start codon was replaced by a GSTGS linker [1], a His-tag was added to the C-terminus and a BamHI site was removed.
  
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Streptavidin tetramers have a very high affinity to biotin and this interaction is often used in biotechnology for purification of nucleic acids and proteins. Compared to the wildtype sequence, the core protein lacks an N-terminal signal peptide and it has also been further truncated at both termini to improve solubility.[2]
  
 
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<partinfo>BBa_K1896004 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K1896004 SequenceAndFeatures</partinfo>
  
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===References===
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# Biggs, B. W., Lim, C. G., Sagliani, K., Shankar, S., Stephanopoulos, G., De Mey, M., &amp; Ajikumar, P. K. (2016). Overcoming heterologous protein interdependency to optimize P450-mediated Taxol precursor synthesis in Escherichia coli. Proceedings of the National Academy of Sciences, 201515826.
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# Pähler, A., Hendrickson, W. A., Kolks, M. A., Argarana, C. E., &amp; Cantor, C. R. (1987). Characterization and crystallization of core streptavidin. ''Journal of Biological Chemistry'', 262(29), 13933-13937.
  
 
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Latest revision as of 09:44, 13 October 2016


linker-Streptavidin-His (tetrameric)

This is an improved version of Part:BBa_K283010, which encodes for the core Streptavidin protein of Streptomyces avidinii. The start codon was replaced by a GSTGS linker [1], a His-tag was added to the C-terminus and a BamHI site was removed.

Streptavidin tetramers have a very high affinity to biotin and this interaction is often used in biotechnology for purification of nucleic acids and proteins. Compared to the wildtype sequence, the core protein lacks an N-terminal signal peptide and it has also been further truncated at both termini to improve solubility.[2]

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 97
    Illegal AgeI site found at 148
  • 1000
    COMPATIBLE WITH RFC[1000]

References

  1. Biggs, B. W., Lim, C. G., Sagliani, K., Shankar, S., Stephanopoulos, G., De Mey, M., & Ajikumar, P. K. (2016). Overcoming heterologous protein interdependency to optimize P450-mediated Taxol precursor synthesis in Escherichia coli. Proceedings of the National Academy of Sciences, 201515826.
  2. Pähler, A., Hendrickson, W. A., Kolks, M. A., Argarana, C. E., & Cantor, C. R. (1987). Characterization and crystallization of core streptavidin. Journal of Biological Chemistry, 262(29), 13933-13937.