Difference between revisions of "Part:BBa K1391113:Experience"
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This experience page is provided so that any user may enter their experience using this part.<BR>Please enter | This experience page is provided so that any user may enter their experience using this part.<BR>Please enter | ||
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===Applications of BBa_K1391113=== | ===Applications of BBa_K1391113=== | ||
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| + | PirB (paired immunoglobin-like receptor B) is a transmembrane protein found in murine neurons, shown to bind to beta-amyloid. The interactions is mediated by the first two extracellular immunoglobulin (Ig) domains. Upon binding to beta-amyloid (extracellular), PirB induces enhanced cofilin signaling (intracellular). In this construct, PirB is under hEF1a promoter. | ||
| + | Taeho Kim, George S. Vidal, Maya Djurisic, et al. "Human LilrB2 is a beta-amyloid recptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's Model". Science. 20 Sep 2013. <http://www.sciencemag.org/content/341/6152/1399>. 16 Oct 2014. | ||
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| + | In this detection system, LilrB2 was fused to a linker, a TEV protease (TEVp) cleavage site and a transcription factor (in that order) at its intracellular domain. Cofilin was fused to TEV protease. These modifications allowed the manipulation of the natural operational system of LilrB2 such that when beta-amyloid oligomers bind to the receptor (and activate it) the TEV protease on the recruited cofilin cleaves at the TEVp cleavage site. This releases the transcription factor in to the cytosol, where it is guided to the nucleus of the cell and activates some subsequent (reporter or treatment) module. | ||
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===User Reviews=== | ===User Reviews=== | ||
Latest revision as of 21:20, 1 November 2014
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how you used this part and how it worked out.
Applications of BBa_K1391113
PirB (paired immunoglobin-like receptor B) is a transmembrane protein found in murine neurons, shown to bind to beta-amyloid. The interactions is mediated by the first two extracellular immunoglobulin (Ig) domains. Upon binding to beta-amyloid (extracellular), PirB induces enhanced cofilin signaling (intracellular). In this construct, PirB is under hEF1a promoter. Taeho Kim, George S. Vidal, Maya Djurisic, et al. "Human LilrB2 is a beta-amyloid recptor and its murine homolog PirB regulates synaptic plasticity in an Alzheimer's Model". Science. 20 Sep 2013. <http://www.sciencemag.org/content/341/6152/1399>. 16 Oct 2014.
In this detection system, LilrB2 was fused to a linker, a TEV protease (TEVp) cleavage site and a transcription factor (in that order) at its intracellular domain. Cofilin was fused to TEV protease. These modifications allowed the manipulation of the natural operational system of LilrB2 such that when beta-amyloid oligomers bind to the receptor (and activate it) the TEV protease on the recruited cofilin cleaves at the TEVp cleavage site. This releases the transcription factor in to the cytosol, where it is guided to the nucleus of the cell and activates some subsequent (reporter or treatment) module.
User Reviews
UNIQb554e94ce9a9ea3a-partinfo-00000000-QINU UNIQb554e94ce9a9ea3a-partinfo-00000001-QINU