Difference between revisions of "Part:BBa K2665026"
 
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SED1 anchoring domain is a domain derived from <i>S.cerevisiae</i> SED1 gene.<br>
 
SED1 anchoring domain is a domain derived from <i>S.cerevisiae</i> SED1 gene.<br>
−
This domain can be used for cell-surface display of heterologous proteins. [1]<br>
+
This domain can be used for cell-surface display of various proteins. [1]<br>
 
Using this part with the SED1 secretion signal  ''' [https://parts.igem.org/Part:BBa_K2665025  BBa_K2665025] ''', you can anchor your objective protein on <i>S.cerevisiae</i> cell wall.<br>
 
Using this part with the SED1 secretion signal  ''' [https://parts.igem.org/Part:BBa_K2665025  BBa_K2665025] ''', you can anchor your objective protein on <i>S.cerevisiae</i> cell wall.<br>
 
The usage example of this part can be referred in the pages of    ''' [https://parts.igem.org/Part:BBa_K2665020  BBa_K2665020] '''    ''' [https://parts.igem.org/Part:BBa_K2665021  BBa_K2665021] '''
 
The usage example of this part can be referred in the pages of    ''' [https://parts.igem.org/Part:BBa_K2665020  BBa_K2665020] '''    ''' [https://parts.igem.org/Part:BBa_K2665021  BBa_K2665021] '''

Latest revision as of 01:11, 17 October 2018


SED1 anchoring domain

SED1 anchoring domain is a domain derived from S.cerevisiae SED1 gene.
This domain can be used for cell-surface display of various proteins. [1]
Using this part with the SED1 secretion signal BBa_K2665025 , you can anchor your objective protein on S.cerevisiae cell wall.
The usage example of this part can be referred in the pages of BBa_K2665020 BBa_K2665021


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 388
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI site found at 325

Reference

[1]K. Inokuma, T.Bamba, J.Ishii et al. (2016) "Enhanced cell-surface display and secretory production of cellulolytic enzymes with Saccharomyces cerevisiae Sed1 signal peptide" Biotechnology and Bioengineering 2358-2366