Difference between revisions of "Part:BBa K1620003"
Celio.dias (Talk | contribs) |
Celio.dias (Talk | contribs) |
||
Line 2: | Line 2: | ||
<partinfo>BBa_K1620003 short</partinfo> | <partinfo>BBa_K1620003 short</partinfo> | ||
− | |||
− | |||
− | |||
− | |||
− | |||
− | |||
<span class='h3bb'>Sequence and Features</span> | <span class='h3bb'>Sequence and Features</span> | ||
<partinfo>BBa_K1620003 SequenceAndFeatures</partinfo> | <partinfo>BBa_K1620003 SequenceAndFeatures</partinfo> | ||
Line 16: | Line 10: | ||
<partinfo>BBa_K1620003 parameters</partinfo> | <partinfo>BBa_K1620003 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
+ | |||
+ | ===Usage and Biology=== | ||
+ | |||
+ | <p align="justify"> | ||
+ | IbpB is a small heat shock protein. It is expressed under stress conditions which associate with aggregated proteins. It acts together with IbpA to stabilize and protect aggregated proteins from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. It is extensively documented in the following link: http://www.uniprot.org/uniprot/P0C058. In our project, we have figured out to construct a protein solubilization device for high rate expressed proteins. | ||
+ | </p> |
Latest revision as of 21:19, 13 September 2015
small heat shock protein IbpB
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]
Usage and Biology
IbpB is a small heat shock protein. It is expressed under stress conditions which associate with aggregated proteins. It acts together with IbpA to stabilize and protect aggregated proteins from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. It is extensively documented in the following link: http://www.uniprot.org/uniprot/P0C058. In our project, we have figured out to construct a protein solubilization device for high rate expressed proteins.