Difference between revisions of "Part:BBa K4375007"

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==Usage and Biology==
 
==Usage and Biology==
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The INP (Ice Nucleation Protein) is a membrane-bound protein from bacteria, like Pseudomonas and Erwinia, and can be used as an anchor motif for cell surface display. INPNC contains the N -and C-terminal domains of this protein in a truncated form. This is the codon optimized version of partinfo>BBa_K811003</partinfo for expression in E. Coli.
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The INP (Ice Nucleation Protein) is a membrane-bound protein from bacteria, like Pseudomonas and Erwinia, and can be used as an anchor motif for cell surface display. INPNC contains the N -and C-terminal domains of this protein in a truncated form. This is the codon optimized version of <partinfo>BBa_K811003</partinfo> for expression in E. Coli.
  
 
==Sequence and Features==
 
==Sequence and Features==

Revision as of 20:15, 10 October 2022


Codon optimalised INPNC for Surface Display

INPNC codes for N- and C- terminal domain of Ice Nucleation Protein (INP) from Pseudomonas syringae, and it can be used for displaying proteins on bacteria's outer membrane.



Usage and Biology

The INP (Ice Nucleation Protein) is a membrane-bound protein from bacteria, like Pseudomonas and Erwinia, and can be used as an anchor motif for cell surface display. INPNC contains the N -and C-terminal domains of this protein in a truncated form. This is the codon optimized version of BBa_K811003 for expression in E. Coli.

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 NgoMIV site found at 72
    Illegal NgoMIV site found at 405
    Illegal AgeI site found at 823
  • 1000
    COMPATIBLE WITH RFC[1000]


Reference

Wu, P.-H.; Giridhar, R.; Wu, W.-T. Surface Display of Transglucosidase onEscherichia Coli by Using the Ice Nucleation Protein ofXanthomonas Campestris and Its Application in Glucosylation of Hydroquinone. Biotechnology and Bioengineering 2006, 95 (6), 1138–1147. https://doi.org/10.1002/bit.21076.