Difference between revisions of "Part:BBa K5036029"

 
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<partinfo>BBa_K5036029 short</partinfo>
 
<partinfo>BBa_K5036029 short</partinfo>
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==Part Description==
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In our first receptor chain, we've engineered a system that responds to tissue injury. An external domain, VEGF-R1, is attached to an internal domain composed of C terminal domain of TEV protease, a nuclear localization signal (NLS), a TEV cleavage site(TCS(Q,L)), and dCas9(C) which is linked to transcription activator VP64
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==Usage==
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this is our receptor's first chain. our receptor is activated after binding of VEGF to the external domain which is designed to attach specifically to it. after activation the two domains of TEV dimerizes forming catalytically active TEV protease which will cleave the two chains at TCS. upon cleavage of the two chains the two domains of dCas9 dimerize and is released attached to transcription activator to be guided to its direction
  
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In our first receptor chain, we've engineered a system that responds to tissue injury. An external domain, VEGF-R1, is attached to a protein sequence containing TEV protease, a nuclear localization signal (NES), a TEV cleavage site(TCS), and dCas9(C). When an injury occurs, VEGF levels rise outside the cell. This binds to VEGF-R1, activating the receptor and triggering the TEV protease to cleave the chain at the TCS site. This releases dCas9(C), which can then associate with a complementary dCas9 fragment (dCas9(N)) to form a fully functional dCas9 enzyme
 
  
  

Revision as of 17:43, 21 September 2024


dCas9(C)_NLS-Syn-VEGFR-1 (VEGF-R1, C-TEV, NLS, TCS(Q,L), HA,dCas9(C),VP64,GFP)

Part Description

In our first receptor chain, we've engineered a system that responds to tissue injury. An external domain, VEGF-R1, is attached to an internal domain composed of C terminal domain of TEV protease, a nuclear localization signal (NLS), a TEV cleavage site(TCS(Q,L)), and dCas9(C) which is linked to transcription activator VP64

Usage

this is our receptor's first chain. our receptor is activated after binding of VEGF to the external domain which is designed to attach specifically to it. after activation the two domains of TEV dimerizes forming catalytically active TEV protease which will cleave the two chains at TCS. upon cleavage of the two chains the two domains of dCas9 dimerize and is released attached to transcription activator to be guided to its direction



Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 2173
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 3973
    Illegal NgoMIV site found at 4046
    Illegal NgoMIV site found at 4531
    Illegal NgoMIV site found at 5440
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 6737
    Illegal SapI.rc site found at 3268