Difference between revisions of "Part:BBa K4164005"
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dRFPA1 can form a heterodimer with ddRFPB1, increasing the fluorescence intensity ten times more than the dissociation state.The use of ddRFP-A1B1 has been demonstrated in three applications, including the detection of a protein-protein interaction in vitro, imaging of the reversible Ca<sup>2+</sup>-dependent association of calmodulin, M13 in live cells, and imaging of caspase-3 activity during apoptosis.
 
dRFPA1 can form a heterodimer with ddRFPB1, increasing the fluorescence intensity ten times more than the dissociation state.The use of ddRFP-A1B1 has been demonstrated in three applications, including the detection of a protein-protein interaction in vitro, imaging of the reversible Ca<sup>2+</sup>-dependent association of calmodulin, M13 in live cells, and imaging of caspase-3 activity during apoptosis.
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The use of ddRFP-A1B1 has been demonstrated in three applications, including the detection of a protein-protein interaction in vitro, imaging of the reversible Ca<sup>2+</sup>-dependent association of calmodulin, M13 in live cells, and imaging of caspase-3 activity during apoptosis.
 
  
 
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Revision as of 06:54, 11 October 2022


dimerization-dependent red fluorescent protein-B1(ddRFP-B1)

The dimerization-dependent red fluorescent protein-B1(ddRFP-B1) is a variant of the dimeric Tomato. DdRFP-B1 is a monomer protein of the red fluorescent protein heterodimer, with a size of 26.4kDa, which is a dTomato-derived partner capable of forming dimers with ddRFPA1. ddRFPA1 interacts with ddRFPB1 with a Kd of 33 μM, and, therefore,the heterodimers can exist primarily in a free state at cytoplasmic concentrations sufficient for live cell imaging. ddRFPB1 does not form a chromatography group and exhibits no fluorescence in the monomeric state.

dRFPA1 can form a heterodimer with ddRFPB1, increasing the fluorescence intensity ten times more than the dissociation state.The use of ddRFP-A1B1 has been demonstrated in three applications, including the detection of a protein-protein interaction in vitro, imaging of the reversible Ca2+-dependent association of calmodulin, M13 in live cells, and imaging of caspase-3 activity during apoptosis.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 436
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]