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10.1186/s12934-015-0241-5 http://scihub22266oqcxt.onion/10.1186/s12934-015-0241-5 C4404585!4404585!25890161     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Microb+Cell+Fact 2015 ; 14 (ä): ä Nephropedia Template TP {{tp|p=25890161|t=2015. Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins |pdf=|usr=}}{{25890161}} gab.com Text Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins JO: Microb Cell Fact http://www.kidney.de/pget.php?&tw=1&pmid=25890161 #FOAvip Background: Lipopolysaccharide (LPS), also referred to as endotoxin, is the major constituent of the outer leaflet of the outer membrane of virtually all Gram-negative bacteria. The lipid A moiety, which anchors the LPS molecule to the outer membrane, acts as a potent agonist for Toll-like receptor 4/myeloid differentiation factor 2-mediated pro-inflammatory activity in mammals and, thus, represents the endotoxic principle of LPS. Recombinant proteins, commonly manufactured in Escherichia coli, are generally contaminated with endotoxin. Removal of bacterial endotoxin from recombinant therapeutic proteins is a challenging and expensive process that has been necessary to ensure the safety of the final product. Results: As an alternative strategy for common endotoxin removal methods, we have developed a series of E. coli strains that are able to grow and express recombinant proteins with the endotoxin precursor lipid IVA as the only LPS-related molecule in their outer membranes. Lipid IVA does not trigger an endotoxic response in humans typical of bacterial LPS chemotypes. Hence the engineered cells themselves, and the purified proteins expressed within these cells display extremely low endotoxin levels. Conclusions: This paper describes the preparation and characterization of endotoxin-free E. coli strains, and demonstrates the direct production of recombinant proteins with negligible endotoxin contamination. Electronic supplementary material: The online version of this article (doi:10.1186/s12934-015-0241-5) contains supplementary material, which is available to authorized users. Twit Text FOAVip Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins ????Microb Cell Fact http://www.kidney.de/pget.php?&tw=1&pmid=25890161 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25890161 #FOAvip English Wikipedia <ref>{{Cite pmid|25890161}}</ref> Detoxifying Escherichia coli for endotoxin-free production of recombinant proteins #MMPMID25890161 Mamat U; Wilke K; Bramhill D; Schromm AB; Lindner B; Kohl TA; Corchero JL; Villaverde A; Schaffer L; Head SR; Souvignier C; Meredith TC; Woodard RW Microb Cell Fact 2015[]; 14 (ä): ä PMID25890161show ga Background: Lipopolysaccharide (LPS), also referred to as endotoxin, is the major constituent of the outer leaflet of the outer membrane of virtually all Gram-negative bacteria. The lipid A moiety, which anchors the LPS molecule to the outer membrane, acts as a potent agonist for Toll-like receptor 4/myeloid differentiation factor 2-mediated pro-inflammatory activity in mammals and, thus, represents the endotoxic principle of LPS. Recombinant proteins, commonly manufactured in Escherichia coli, are generally contaminated with endotoxin. Removal of bacterial endotoxin from recombinant therapeutic proteins is a challenging and expensive process that has been necessary to ensure the safety of the final product. Results: As an alternative strategy for common endotoxin removal methods, we have developed a series of E. coli strains that are able to grow and express recombinant proteins with the endotoxin precursor lipid IVA as the only LPS-related molecule in their outer membranes. Lipid IVA does not trigger an endotoxic response in humans typical of bacterial LPS chemotypes. Hence the engineered cells themselves, and the purified proteins expressed within these cells display extremely low endotoxin levels. Conclusions: This paper describes the preparation and characterization of endotoxin-free E. coli strains, and demonstrates the direct production of recombinant proteins with negligible endotoxin contamination. Electronic supplementary material: The online version of this article (doi:10.1186/s12934-015-0241-5) contains supplementary material, which is available to authorized users. äDetoxifying Escherichia coli for endotoxin-free production of recombin(epmc).pdf DeepDyve Pubget Overpricing