A T7 promoter-specific, inducible protein expression system forBacillus subtilis

1996 ◽  
Vol 250 (2) ◽  
pp. 230-236 ◽  
Author(s):  
Birgit Conrad ◽  
Regina S. Savchenko ◽  
Roland Breves ◽  
Jürgen Hofemeister
Keyword(s):  
Protein Expression ◽  
Expression System ◽  
T7 Promoter ◽  
Protein Expression System ◽  
Inducible Protein

A T7 promoter-specific, inducible protein expression system for

1996 ◽  
Vol 250 (2) ◽  
pp. 230 ◽  
Author(s):  
Birgit Conrad ◽  
R. S. Savchenko ◽  
Roland Breves ◽  
J. Hofemeister
Keyword(s):  
Protein Expression ◽  
Expression System ◽  
T7 Promoter ◽  
Protein Expression System ◽  
Inducible Protein

scholarly journals Construction of a Low-Temperature Protein Expression System Using a Cold-Adapted Bacterium, Shewanella sp. Strain Ac10, as the Host

2007 ◽  
Vol 73 (15) ◽  
pp. 4849-4856 ◽  
Author(s):  
Ryoma Miyake ◽  
Jun Kawamoto ◽  
Yun-Lin Wei ◽  
Masanari Kitagawa ◽  
Ikunoshin Kato ◽  
...  
Keyword(s):  
Low Temperature ◽  
Protein Expression ◽  
Recombinant Protein Expression ◽  
Expression System ◽  
Maximum Yield ◽  
Broad Host Range ◽  
Psychrophilic Bacterium ◽  
T7 Promoter ◽  
Cold Adapted ◽  
Protein Expression System

ABSTRACT A recombinant protein expression system working at low temperatures is expected to be useful for the production of thermolabile proteins. We constructed a low-temperature expression system using an Antarctic cold-adapted bacterium, Shewanella sp. strain Ac10, as the host. We evaluated the promoters for proteins abundantly produced at 4°C in this bacterium to express foreign proteins. We used 27 promoters and a broad-host-range vector, pJRD215, to produce β-lactamase in Shewanella sp. strain Ac10. The maximum yield was obtained when the promoter for putative alkyl hydroperoxide reductase (AhpC) was used and the recombinant cells were grown to late stationary phase. The yield was 91 mg/liter of culture at 4°C and 139 mg/liter of culture at 18°C. We used this system to produce putative peptidases, PepF, LAP, and PepQ, and a putative glucosidase, BglA, from a psychrophilic bacterium, Desulfotalea psychrophila DSM12343. We obtained 48, 7.1, 28, and 5.4 mg/liter of culture of these proteins, respectively, in a soluble fraction. The amounts of PepF and PepQ produced by this system were greater than those produced by the Escherichia coli T7 promoter system.

Optimization of a Fusion Protein Expression System using Human Cell Lines to Create a Practical Immunoassay Reagent

2015 ◽  
Vol 41 (1) ◽  
pp. 38-42 ◽  
Author(s):  
Kounosuke Hayashi ◽  
Yusuke Tomozoe ◽  
Kenji Nagai ◽  
Kyoichi Matsuba ◽  
Masayuki Mitsumori ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Protein Expression ◽  
Cell Lines ◽  
Human Cell ◽  
Expression System ◽  
Human Cell Lines ◽  
Fusion Protein Expression ◽  
Protein Expression System

scholarly journals Expression of Recombinant Fusion Protein of Newcastle Disease Virus from Escherichia coli Plasmid Clone C-2a by In-vitro Cell-free Protein Expression System

2020 ◽  
Vol 20 ◽  
pp. 04004
Author(s):  
Ahmad Pandu Satria Wiratama ◽  
Aris Haryanto
Keyword(s):  
Protein Expression ◽  
Newcastle Disease ◽  
Recombinant Plasmid ◽  
Expression System ◽  
Free Protein ◽  
F Protein ◽  
E Coli ◽  
Protein Expression System ◽  
Sds Page

Newcastle Disease Virus (NDV) is an infectious disease that infect many kinds of wild and domesticated birds. Infection of NDV become a massive problem for poultry industry around the world especially in Indonesia. Vaccination is an effort to prevent the infection of NDV in poultry. NDV vaccine that used in Indonesia is a conventional life vaccine from LaSota and B1 strains. These type of vaccine is 21%-23% genetically distinct with the virus that spread in the environment. The antibody protection provided by the vaccine is not effective. Therefore, vaccination with new local NDV strain is needed to prevent the NDV infection in Indonesia. The previously study research reported that the local isolate of NDV from Kulon Progo, Indonesia has been isolated. Fusion (F) protein encoding gene that has been inserted into pBT7-N-His expression p lasmid which isolated from clone C-2a of E. coli, then it was expressed by the Cell-free protein expression system. The aim of this study was to confirm whether clone C-2a of E.coli carrying a recombinant plasmid pBT7-N-His-Fusion NDV and to express a recombinant F protein of NDV in-vitro from expression plasmid by cell-free protein expression system. This work started by detection of recombinant plasmid pBT7-N-His-Fusion NDV by DNA plasmid extraction followed by agarose gel electrophoresis. The recombinant F protein was in-vitro expressed by cell-free protein expression kit. The expressed F protein of NDV then was visualized by SDS-PAGE and Westernblott to analyse the expression of NDV recombinant F protein. It confirmed that clone C-2a of E. coli contained plasmid pBT7-N-His (4.001 bp) inserted by recombinant F protein of NDV gene (642 bp). The visualisation of expressed recombinant F protein by SDS-PAGE and Westernblott showed the NDV recombinant F protein was a specific protein fragment with molecular weight of 25,6 kDa..

scholarly journals The establishment of new protein expression system using N starvation inducible promoters in Chlorella

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Jun-Hye Shin ◽  
Juyoung Choi ◽  
Jeongmin Jeon ◽  
Manu Kumar ◽  
Juhyeon Lee ◽  
...  
Keyword(s):  
Protein Expression ◽  
Expression System ◽  
Inducible Promoters ◽  
Protein Expression System ◽  
N Starvation ◽  
New Protein
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