Expression and Purification of Bioactive High-Purity Recombinant Mouse CXCL14 in Escherichia coli

2011 ◽  
Vol 164 (8) ◽  
pp. 1366-1375 ◽  
Author(s):  
Jingjing Li ◽  
Jin Gao ◽  
Sunita Sah ◽  
Uttam Satyal ◽  
Ruliang Zhang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification ◽  
Recombinant Mouse

Expression and Purification of Bioactive High-Purity Recombinant Mouse SPP1 in Escherichia coli

2014 ◽  
Vol 173 (2) ◽  
pp. 421-432 ◽  
Author(s):  
Yunsheng Yuan ◽  
Xiyuan Zhang ◽  
Shunyan Weng ◽  
Wen Guan ◽  
Di Xiang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification ◽  
Recombinant Mouse

scholarly journals Expression and purification of bioactive high-purity human midkine in Escherichia coli

2009 ◽  
Vol 10 (2) ◽  
pp. 79-86 ◽  
Author(s):  
Zhong-hui Zhang ◽  
Li-juan Du ◽  
Di Xiang ◽  
Shun-ying Zhu ◽  
Ming-yuan Wu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification

Expression and purification of bioactive high-purity mouse monokine induced by IFN-γ in Escherichia coli

2007 ◽  
Vol 55 (1) ◽  
pp. 132-138 ◽  
Author(s):  
Huili Lu ◽  
Mei Yu ◽  
Ye Sun ◽  
Wenwei Mao ◽  
Qun Wang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification ◽  
Ifn Γ

Expression and purification of bioactive high-purity human S100A6 in Escherichia coli

2012 ◽  
Vol 83 (1) ◽  
pp. 98-103 ◽  
Author(s):  
Honglin He ◽  
Tingxu Yang ◽  
Shixiang Jia ◽  
Ruliang Zhang ◽  
Ping Tu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Purity ◽  
Expression And Purification

scholarly journals Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion

2009 ◽  
Vol 13 (12) ◽  
pp. 3274-3284 ◽  
Author(s):  
Kimberly Trabbic-Carlson ◽  
Li Liu ◽  
Bumjoon Kim ◽  
Ashutosh Chilkoti
Keyword(s):  
Escherichia Coli ◽  
Recombinant Proteins ◽  
Expression And Purification

scholarly journals CONSTRUCTION, EXPRESSION AND PURIFICATION OF RECOMBINANT PRE-MATURE PEPTIDE OF PLANTARICIN F FROM Lactobacillus plantarum S34 IN Escherichia coli

2015 ◽  
Vol 16 (1) ◽  
pp. 31
Author(s):  
Kusdianawati Kusdianawati ◽  
Apon Zaenal Mustopa ◽  
Suharsono Suharsono ◽  
Bugi Ratno Budiarto ◽  
Fatimah Fatimah ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Lactobacillus Plantarum ◽  
Proteolytic Enzymes ◽  
Leader Peptide ◽  
Human Consumption ◽  
Mature Peptide ◽  
Expression And Purification ◽  
Food Preservative ◽  
E Coli ◽  
Sds Page

Plantaricin is one of bacteriocins that have the potential to be used as food preservative. Plantaricin is safe for human consumption because it can be easily degraded by proteolytic enzymes. The objective of this study was to express and purify recombinant pre-mature peptide of plantaricin F from <em>Lactobacillus plantarum</em> S34 in <em>Escherichia coli</em>. Plantaricin gene-specific primer was used to obtain pln F structural gene amplicon from L. <em>plantarum</em> S34. This amplicon was cloned in pET32a vector and expressed in E. coli BL21 (DE3) pLysS. Pre-mature plantaricin F peptide was expressed as Histagged-fusion protein and separated by Co2+-chelating affinity chromatography. L. <em>plantarum</em> S34-derived pre-mature plantaricin F peptide fused with thioredoxin-(His)6tag had successfully been expressed in E. <em>coli</em> BL21 (DE3) pLysS using pET32a as an expression vector. The fused recombinant pln F as pre-mature state expressed had a molecular mass of +24 kDa, meanwhile the fused recombinant that contained only the leader peptide of pln F appeared as +20 kDa based on SDS-PAGE separations. The optimal production of fused recombinant pln F as soluble fraction was obtained when culture condition was added with 0.5 mM of IPTG and incubated at 22°C for 5 hours (OD~1). Furthermore, the expression of fused recombinant pln F as its pre-mature peptide pointed out that the pln F’s leader peptide could be proteolytically cleaved by a system in heterologous cells. Overall, heterologous pln F production as pre-mature peptide fused with thioredoxin-(His)6tag had been well established. From this research, we expect plantaricin F can be expressed and purified in E. coli.

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