Difference between revisions of "Part:BBa K2271060:Design"

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Gerst, Jeffrey E. (1997) <br>
 
Gerst, Jeffrey E. (1997) <br>
 
<i>J. Biol. Chem. 272 (26), pp. 16591–16598.</i> DOI: 10.1074/jbc.272.26.16591.
 
<i>J. Biol. Chem. 272 (26), pp. 16591–16598.</i> DOI: 10.1074/jbc.272.26.16591.
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[2] <b>Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites. </b> <br>
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André Halbach, Christiane Landgraf, Stephan Lorenzen, Katja Rosenkranz, Rudolf Volkmer-Engert, Ralf Erdmann, and Hanspeter Rottensteiner (2006)
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In Journal of Cell Science 119, 2508-2517 Published by The Company of Biologists 2006 doi:10.1242/jcs.02979

Latest revision as of 22:40, 1 November 2017


Snc1


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

We used the truncated Snc1(aa 1-95) without the transmembrane domain

Source

Synthesized by IDT.

References

[1] Conserved α-Helical Segments on Yeast Homologs of the Synaptobrevin/VAMP Family of v-SNAREs Mediate Exocytic Function.
Gerst, Jeffrey E. (1997)
J. Biol. Chem. 272 (26), pp. 16591–16598. DOI: 10.1074/jbc.272.26.16591.

[2] Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites.
André Halbach, Christiane Landgraf, Stephan Lorenzen, Katja Rosenkranz, Rudolf Volkmer-Engert, Ralf Erdmann, and Hanspeter Rottensteiner (2006) In Journal of Cell Science 119, 2508-2517 Published by The Company of Biologists 2006 doi:10.1242/jcs.02979