Difference between revisions of "Part:BBa K3396001"
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<partinfo>BBa_K3396001 short</partinfo> | <partinfo>BBa_K3396001 short</partinfo> | ||
− | The Coch2 module | + | The Coch2 module binds DocS (BBa_K3396000) modules constitutively. |
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===Usage and Biology=== | ===Usage and Biology=== | ||
− | + | The Coch2[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary DocS modules harbored by each of the catalytic subunits. They can be used as a proof-of-concept tool to demonstrate whether a split-protein approach works. These pairs can also be replaced with other inducible protein dimerization pairs for signal-controlled purposes. | |
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<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K3396001 SequenceAndFeatures</partinfo> | <partinfo>BBa_K3396001 SequenceAndFeatures</partinfo> | ||
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<partinfo>BBa_K3396001 parameters</partinfo> | <partinfo>BBa_K3396001 parameters</partinfo> | ||
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+ | ===Reference=== | ||
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+ | [1] BARAK Y, HANDELSMAN T, NAKAR D, et al. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction [J]. J Mol Recognit, 2005, 18(6): 491-501. |
Revision as of 01:58, 25 October 2020
Coh2
The Coch2 module binds DocS (BBa_K3396000) modules constitutively.
Usage and Biology
The Coch2[1] module comes from The C. thermocellum scaffoldin and it could recognize and bind tightly to complementary DocS modules harbored by each of the catalytic subunits. They can be used as a proof-of-concept tool to demonstrate whether a split-protein approach works. These pairs can also be replaced with other inducible protein dimerization pairs for signal-controlled purposes.
Sequence and Features
Assembly Compatibility:
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference
[1] BARAK Y, HANDELSMAN T, NAKAR D, et al. Matching fusion protein systems for affinity analysis of two interacting families of proteins: the cohesin-dockerin interaction [J]. J Mol Recognit, 2005, 18(6): 491-501.