Difference between revisions of "Part:BBa K103004"

Revision as of 01:09, 28 October 2008

protein Z_SPA-1

Artificially created strong interactor of B domain of Staphylococcal protein A ( BBa_K103003)[http://www.ncbi.nlm.nih.gov/pubmed/15238637?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]. Codon usage optimized for expresion in E.coli. It autoaggregates easily even in fusion with soluble protein. Preferentially binds B domain of Staphylococcal protein A ( BBa_K103003).

Z_SPA-1-tagged proteins can be easily purified (more 99% of the protein is present in postsonication debris)
We have used Z_SPA-1 protein fusions with BBa_K103019 or BBa_K103020 as a prey in our 'hunter and prey' selection system
This part uses our NdeI/SacI/BamHI fusion cloning substandard

Source: [http://www.pdb.org/pdb/explore.do?structureId=2B88 PDB]

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]

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-Artificially created strong interactor of B domain of Staphylococcal protein A (BBa_K103003)[http://www.ncbi.nlm.nih.gov/pubmed/15238637?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]. Codon usage optimized for expresion in E.coli. It autoaggregates easily even in fusion with soluble protein. Preferentially binds B domain of Staphylococcal protein A (BBa_K103003).
+Artificially created strong interactor of B domain of Staphylococcal protein A ([[Part:BBa_K103020 | BBa_K103003]])[http://www.ncbi.nlm.nih.gov/pubmed/15238637?ordinalpos=1&itool=EntrezSystem2.PEntrez.Pubmed.Pubmed_ResultsPanel.Pubmed_DefaultReportPanel.Pubmed_RVDocSum]. Codon usage optimized for expresion in E.coli. It autoaggregates easily even in fusion with soluble protein. Preferentially binds B domain of Staphylococcal protein A ([[Part:BBa_K103020 | BBa_K103003]]).
 *Z<sub>SPA-1</sub>-tagged proteins can be easily purified (more 99% of the protein is present in postsonication debris)