Difference between revisions of "Part:BBa K1150021"
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<div align="justify"; margin-right:10px>Krüppel-associated Box repressor domains - commonly termed as [https://parts.igem.org/Part:BBa_K1150002 KRAB] - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (<i>Rosati et al.</i>, 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (<i>Witzgall et al.</i>, 1994).  Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (<i>Birtle</i>, 2006). Even though KRAB minimal domains are usually no longer than 50-75 amino acids, their mechanism of function remains complex. </div><br>
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<div align="justify"; margin-right:10px>Krüppel-associated Box repressor domains - commonly termed as KRAB - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (<i>Rosati et al.</i>, 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (<i>Witzgall et al.</i>, 1994).  Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (<i>Birtle</i>, 2006). Even though KRAB minimal domains are usually no longer than 50-75 amino acids, their mechanism of function remains complex. </div><br>
  
 
[[File:Freiburg2013 Plasmid Cas9-KRAB-1.jpg|800px|thumb|left|<b>Fig. 1</b> Schematic overview of dCas9-KRAB composite part with all features.]]  
 
[[File:Freiburg2013 Plasmid Cas9-KRAB-1.jpg|800px|thumb|left|<b>Fig. 1</b> Schematic overview of dCas9-KRAB composite part with all features.]]  

Revision as of 18:31, 4 October 2013

uniCAS Repressor (SV40 promoter)

SV40:HA-NLS-dCas9-Linker-KRAB-NLS:BGH
Function Transcriptional Repression
Use in Mammalian cells
RFC standard RFC 25
Backbone pSB1C3
Organism Streptococcus pyogenes, Homo sapiens
Source Feng Zhang, Addgene
Konrad Müller, University of Freiburg
Submitted by [http://2013.igem.org/Team:Freiburg Freiburg 2013]
Krüppel-associated Box repressor domains - commonly termed as KRAB - are highly conserved polypeptide motifs and were first functionally characterized in 1991 (Rosati et al., 1991). As they constitute about one third of all human zinc finger transcription factors, key regulatory features in higher eukaryotic transcriptomics are suggested (Witzgall et al., 1994). Even in terms of tetrapod evolution, the role of their great abundance has been extensively discussed (Birtle, 2006). Even though KRAB minimal domains are usually no longer than 50-75 amino acids, their mechanism of function remains complex.

Fig. 1 Schematic overview of dCas9-KRAB composite part with all features.


Usage and Biology

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 664
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 4784
    Illegal SapI.rc site found at 4748

Functional Parameters