Part:BBa_K1405003:Design
INPN
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 429
- 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI.rc site found at 238
Design Notes
INP has been successfully used to display several proteins, such as levansucrase, carboxymethylcellulase (CMCase), Hepatitis B surface antigen (HbsAg), human immunodeficiency virus type 1 (HIV-1) gp120 and so on.Importantly, INP can be expressed at the cell surface of E. coli at a very high level, without affecting cell viability: comparable to the endogenous expression of the OmpA porin
Then we found that using INP derivatives containing only N-domain (INPN) as display system successfully is possible. There is also literature which alleges that since full-length INP is quite large (1,200–1,500 amino acid residues), functional truncated INP molecules may serve as better anchoring motifs to carry large heterologous proteins.
So we start thinking that we also could use INP derivatives containing only N-domain (INPN) as display system. As we say early, inaZ has less support. At last, we use inaK as ingredient.
Source
The sequence of inaK can be found in the The National Center for Biotechnology Information advances science and health by providing access to biomedical and genomic information(NCBI) and the gene was synthesized by a company.