Difference between revisions of "Part:BBa K1620002"

 
 
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The IbpA is a small heat shock protein. It is expressed under stress conditions which associates with aggregated proteins. Together with IbpB, to stabilize and protect them 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/P0C054>. In our project, we have figured out to construct a protein solubilization device for high rate expressed proteins.
 
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===Usage and Biology===
 
  
 
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===Usage and Biology===
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IbpA is a small heat shock protein. It is expressed under stress conditions which associate with aggregated proteins. It acts together with IbpB 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/P0C054. In our project, we have figured out to construct a protein solubilization device for high rate expressed proteins.
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Latest revision as of 21:20, 13 September 2015

small heat shock protein IbpA

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

IbpA is a small heat shock protein. It is expressed under stress conditions which associate with aggregated proteins. It acts together with IbpB 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/P0C054. In our project, we have figured out to construct a protein solubilization device for high rate expressed proteins.