Comparison of expression optimization of new derivative of staphylokinase (SAK‐2RGD‐TTI) with the rSAK

2019 ◽  
Vol 35 (4) ◽  
Author(s):  
Habibollah Faraji ◽  
Mohammad Ramezani ◽  
Baratali Mashkani ◽  
Hamid R. Sadeghnia ◽  
Hamid M. Benhangi ◽  
...  
Keyword(s):  
Expression Optimization

Production and Expression Optimization of Heterologous Serratiopeptidase

2020 ◽  
Author(s):  
Maryam ROUHANI ◽  
Vahideh VALIZADEH ◽  
Sara MOLASALEHI ◽  
Dariush NOROUZIAN
Keyword(s):  
Recombinant Protein ◽  
Western Blot ◽  
Blot Analysis ◽  
Western Blot Analysis ◽  
Expression Vector ◽  
Incubation Temperature ◽  
Restriction Enzyme Digestion ◽  
Post Induction ◽  
Expression Optimization ◽  
Esherichia Coli

Background: Serratiopeptidase is a bacterial metalloprotease, which is useful for the treatment of pain and inflammation. It breaks down fibrin, thins the fluids formed during inflammation and acts as an anti-biofilm agent. Because of medicinally important role of the enzyme, we aimed to study the cloning and the expression optimization of serratiopeptidase. Methods: The heat-stable serratiopeptidase (5d7w) was selected as the template. Cloning into pET28a expression vector was performed and confirmed by colony PCR and double restriction enzyme digestion. The recombinant protein was expressed in Esherichia coli BL21 and confirmed by SDS-PAGE and Western blot analysis. Different parameters such as expression vector, culture media, post-induction incubation temperature, inducer concentration, and post-induction incubation time were altered to obtain the highest amount of the recombinant protein. Results: Serratiopeptidase was successfully cloned and expressed under optimized conditions in E. coli which confirmed by western blot analysis. The optimal conditions of expression were determined using pQE30 as vector, cultivating the host bacteria in Terrific Broth (TB) medium, at 37º C, induction by IPTG concentration equal to 0.5 mM, and cells were harvested 4 h after induction. Conclusion: As serratiopeptidase is a multi-potent enzyme, the expressed recombinant protein can be considered as a valuable agent for pharmaceutical applications in further studies.

scholarly journals Improving cytidine and adenine base editors by expression optimization and ancestral reconstruction

2018 ◽  
Vol 36 (9) ◽  
pp. 843-846 ◽  
Author(s):  
Luke W Koblan ◽  
Jordan L Doman ◽  
Christopher Wilson ◽  
Jonathan M Levy ◽  
Tristan Tay ◽  
...  
Keyword(s):  
Ancestral Reconstruction ◽  
Expression Optimization ◽  
Adenine Base

Expression Optimization and Biochemical Characterization of a Recombinant γ-Glutamyltranspeptidase from Escherichia coli Novablue

2006 ◽  
Vol 25 (6) ◽  
pp. 431-441 ◽  
Author(s):  
Ya-Feng Yao ◽  
Yih-Ming Weng ◽  
Hui-Yu Hu ◽  
Kuo-Lung Ku ◽  
Long-Liu Lin
Keyword(s):  
Escherichia Coli ◽  
Biochemical Characterization ◽  
Expression Optimization

Techniques for chromosomal integration and expression optimization inEscherichia coli

2018 ◽  
Vol 115 (10) ◽  
pp. 2467-2478 ◽  
Author(s):  
Bingming Ou ◽  
Carolina Garcia ◽  
Yejun Wang ◽  
Weiping Zhang ◽  
Guoqiang Zhu
Keyword(s):  
Chromosomal Integration ◽  
Inescherichia Coli ◽  
Expression Optimization

scholarly journals Publisher Correction: Engineered bidirectional promoters enable rapid multi-gene co-expression optimization

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Thomas Vogl ◽  
Thomas Kickenweiz ◽  
Julia Pitzer ◽  
Lukas Sturmberger ◽  
Astrid Weninger ◽  
...  
Keyword(s):  
Bidirectional Promoters ◽  
Expression Optimization

scholarly journals Modular Protein Expression Toolbox (MoPET), a standardized assembly system for defined expression constructs and expression optimization libraries

PLoS ONE ◽  
2017 ◽  
Vol 12 (5) ◽  
pp. e0176314 ◽  
Author(s):  
Ernst Weber ◽  
Jörg Birkenfeld ◽  
Jürgen Franz ◽  
Uwe Gritzan ◽  
Lars Linden ◽  
...  
Keyword(s):  
Protein Expression ◽  
Assembly System ◽  
Expression Optimization
Sign in / Sign up

Export Citation Format

Share Document