A novel self-cleavage system for production of soluble recombinant protein in Escherichia coli

2014 ◽  
Vol 99 ◽  
pp. 64-69 ◽  
Author(s):  
Yufei Feng ◽  
Qingyuan Xu ◽  
Tao Yang ◽  
Encheng Sun ◽  
Junping Li ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Soluble Recombinant Protein

scholarly journals Cost analysis based on bioreactor cultivation conditions: Production of a soluble recombinant protein using Escherichia coli BL21(DE3)

2020 ◽  
Vol 26 ◽  
pp. e00441 ◽  
Author(s):  
Valdemir M. Cardoso ◽  
Gilson Campani ◽  
Maurício P. Santos ◽  
Gabriel G. Silva ◽  
Manuella C. Pires ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Cost Analysis ◽  
Cultivation Conditions ◽  
Bioreactor Cultivation ◽  
Escherichia Coli Bl21 ◽  
Soluble Recombinant Protein

scholarly journals Expression byStreptomyces lividansof the RatαIntegrin CD11b A-Domain as a Secreted and Soluble Recombinant Protein

2007 ◽  
Vol 2007 ◽  
pp. 1-6 ◽  
Author(s):  
Dorra Zouari Ayadi ◽  
Hichem Chouayekh ◽  
Sonda Mhiri ◽  
Khaled Zerria ◽  
Dahmani M. Fathallah ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Dna Sequence ◽  
Recombinant Proteins ◽  
Signal Peptide ◽  
Shuttle Vector ◽  
Host Strain ◽  
Blocking Antibody ◽  
Synthetic Signal ◽  
Soluble Recombinant Protein

We already reported the use of a long synthetic signal peptide (LSSP) to secrete theStreptomycessp. TO1 amylase byStreptomyces lividansstrain. We herein report the expression and secretion of the rat CD11b A-domain using the same LSSP andS. lividansas host strain. We have used theEscherichia coli/Streptomycesshuttle vector pIJ699 for the cloning of the A-domain DNA sequence downstream of LSSP and under the control of the constitutiveermE-uppromoter ofStreptomyces erythraeus. Using this construct andS. lividansas a host strain, we achieved the expression of 8 mg/L of soluble secreted recombinant form of the A-domain of the rat leukocyteβ2 integrin CD11/CD18 alpha M subunit (CD11b). This secreted recombinant CD11b A-domain reacted with a function blocking antibody showing that this protein is properly folded and probably functional. These data support the capability ofStreptomycesto produce heterologous recombinant proteins as soluble secreted form using the “LSSP” synthetic signal peptide.

Expression of hepatitis A virus cDNA in Escherichia coli: antigenic VP1 recombinant protein.

1987 ◽  
Vol 61 (11) ◽  
pp. 3645-3647 ◽  
Author(s):  
R Ostermayr ◽  
K von der Helm ◽  
V Gauss-Müller ◽  
E L Winnacker ◽  
F Deinhardt
Keyword(s):  
Escherichia Coli ◽  
Recombinant Protein ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Virus Cdna
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