Difference between revisions of "Part:BBa K1890052"

 
 
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<partinfo>BBa_K1890052 short</partinfo>
 
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The transmembrane domain of OmpA together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), both of which are native proteins from Escherichia coli.
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<h2>Usage and Biology</h2>
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Outer membrane protein A (OmpA) is a native membrane protein from <i>Escherichia coli</i>. This biobrick contains the transmembrane domain of OmpA together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), which is also a native protein from Escherichia coli [1]. This part is used for cell surface display of proteins. This biobrick is a subpart of <partinfo>BBa_K1890002</partinfo>. It does not exist individually.
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
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<partinfo>BBa_K1890052 SequenceAndFeatures</partinfo>
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<h2>References</h2>
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===Functional Parameters===
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[1] Francisco, J. a, Earhart, C. F., & Georgiou, G. (1992). Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 89(April), 2713–2717.
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<partinfo>BBa_K1890052 parameters</partinfo>
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Latest revision as of 13:12, 18 October 2016

OmpA transmembrane domain

Usage and Biology

Outer membrane protein A (OmpA) is a native membrane protein from Escherichia coli. This biobrick contains the transmembrane domain of OmpA together with the signaling peptide and the first nine N-terminal amino acids of lipoprotein (Lpp), which is also a native protein from Escherichia coli [1]. This part is used for cell surface display of proteins. This biobrick is a subpart of BBa_K1890002. It does not exist individually.

References

[1] Francisco, J. a, Earhart, C. F., & Georgiou, G. (1992). Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proceedings of the National Academy of Sciences of the United States of America, 89(April), 2713–2717.