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

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

@@ Line 14: / Line 14: @@
 ===References===
-Gerst, Jeffrey E. (1997): Conserved α-Helical Segments on Yeast Homologs of the Synaptobrevin/VAMP Family of v-SNAREs Mediate Exocytic Function. In J. Biol. Chem. 272 (26), pp. 16591–16598. DOI: 10.1074/jbc.272.26.16591.
+[1] <b> Conserved α-Helical Segments on Yeast Homologs of the Synaptobrevin/VAMP Family of v-SNAREs Mediate Exocytic Function. </b> <br>
+Gerst, Jeffrey E. (1997) <br>
+<i>J. Biol. Chem. 272 (26), pp. 16591–16598.</i> DOI: 10.1074/jbc.272.26.16591.
+[2] <b>Targeting of the tail-anchored peroxisomal membrane proteins PEX26 and PEX15 occurs through C-terminal PEX19-binding sites. </b> <br>
+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