Difference between revisions of "Part:BBa K1890052"
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<h2>Usage and Biology</h2> | <h2>Usage and Biology</h2> | ||
− | 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 | + | 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. |
<h2>References</h2> | <h2>References</h2> | ||
[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. | [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. |
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.