Patents by Inventor Richard St. John
Richard St. John has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20230069966Abstract: The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: July 13, 2022Publication date: March 9, 2023Applicant: Genentech, Inc.Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L.E. ADAMS, Bradley R. SNEDECOR
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Publication number: 20220169675Abstract: The current invention reports a method for purifying an antibody by reducing the content of a host cell protein. The method employs a wash step with a low conductivity aqueous solution in an affinity chromatography.Type: ApplicationFiled: May 24, 2021Publication date: June 2, 2022Applicants: Genentech, Inc., Hoffmann-La Roche Inc.Inventors: Paul MCDONALD, Richard ST. JOHN, Marc Wong, Roberto FALKENSTEIN, Wolfgang KOEHNLEIN, Klaus SCHWENDNER, Bernhard SPENSBERGER, Michael WIEDMANN, Frank ZETTL, Annika KLEINJANS, Carina KOPP, Benjamin TRAN, Ryan ERICKSON
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Publication number: 20210171997Abstract: The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: October 9, 2020Publication date: June 10, 2021Applicant: Genentech, Inc.Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L.E. ADAMS, Bradley R. SNEDECOR
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Publication number: 20200199639Abstract: The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: February 7, 2019Publication date: June 25, 2020Applicant: Genentech, Inc.Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L.E. ADAMS, Bradley R. SNEDECOR
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Publication number: 20180291411Abstract: The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: February 28, 2018Publication date: October 11, 2018Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L.E. ADAMS, Bradley R. SNEDECOR
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Publication number: 20180186832Abstract: The current invention reports a method for purifying an antibody by reducing the content of a host cell protein. The method employs a wash step with a low conductivity aqueous solution in an affinity chromatography.Type: ApplicationFiled: February 20, 2018Publication date: July 5, 2018Applicants: Genentech, Inc., Hoffmann-La Roche IncInventors: Paul MCDONALD, Richard ST. JOHN, Marc WONG, Roberto FALKENSTEIN, Wolfgang KOEHNLEIN, Klaus SCHWENDNER, Bernhard SPENSBERGER, Michael WIEDMANN, Frank ZETTL, Annika KLEINJANS, Carina KOPP, Benjamin TRAN, Ryan ERICKSON
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Patent number: 9765379Abstract: The present invention contemplates methods of producing a recombinant protein comprising fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: GrantFiled: September 26, 2014Date of Patent: September 19, 2017Assignee: Genentech, Inc.Inventors: Michael W. Laird, Richard St. John, Jane V. Gunson, Kimberly Kaleas, Deepa Nadarajah, Rachel L E Adams, Bradley R. Snedecor
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Publication number: 20160130624Abstract: The present invention contemplates a method of producing a recombinant protein comprising (a) fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, and (b) harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, and (c) purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: June 9, 2015Publication date: May 12, 2016Applicant: Genentech, Inc.Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L.E. ADAMS, Bradley R. SNEDECOR
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Publication number: 20150225760Abstract: The present invention contemplates methods of producing a recombinant protein comprising fermenting a prokaryotic host cell wherein said prokaryotic host cell has been transformed with a nucleic acid encoding said recombinant protein, harvesting said recombinant protein under conditions where dO2 levels are greater than 0%, purifying said recombinant protein to a filtered bulk, wherein said filtered bulk does not contain detectable DHNA-recombinant protein adduct, as measured by an IEC assay at 310 nm.Type: ApplicationFiled: September 26, 2014Publication date: August 13, 2015Applicant: Genentech, Inc.Inventors: Michael W. LAIRD, Richard ST. JOHN, Jane V. GUNSON, Kimberly KALEAS, Deepa NADARAJAH, Rachel L E ADAMS, Bradley R. SNEDECOR
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Patent number: 8710197Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: GrantFiled: November 5, 2010Date of Patent: April 29, 2014Assignee: Barofold, Inc.Inventors: Theodore W. Randolph, John F. Carpenter, Richard St. John
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Publication number: 20110046357Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: ApplicationFiled: November 5, 2010Publication date: February 24, 2011Inventors: Theodore W. Randolph, John F. Carpenter, Richard St. John
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Publication number: 20100255536Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: ApplicationFiled: June 21, 2010Publication date: October 7, 2010Inventors: Theodore W. RANDOLPH, John F. Carpenter, Richard St. John
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Patent number: 7767795Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: GrantFiled: January 27, 2006Date of Patent: August 3, 2010Assignee: BaroFold Inc.Inventors: Theodore W. Randolph, John F. Carpenter, Richard St. John
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Publication number: 20090054628Abstract: A method of recovering a refolded protein involves static mixing a concentrated solution of a denatured protein with a refolding diluent to obtain the refolded protein. The method is particularly suitable for microbially produced recombinant proteins in large processing volumes. The denatured protein solution can be obtained by isolating protein from the microbial host and exposing them to a denaturant. This solution is mixed with a suitable refolding diluent under static mixing conditions compatible with proper folding of the protein so that the refolded protein is obtained, preferably rapidly and with high yield. A system for implementing the refolded protein recovery method includes a static mixer, a conduit inline with and upstream from the static mixer, and an inlet to the conduit upstream of the static mixer, and optionally a dynamic, preferably non-turbulent, mixing vessel downstream from the static mixer.Type: ApplicationFiled: October 29, 2008Publication date: February 26, 2009Inventors: Richard St. John, Jeffrey Luk, Thucdoan Le
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Publication number: 20080161242Abstract: Protein compositions with reduced immunogenicity are disclosed, as well as methods for producing such compositions.Type: ApplicationFiled: September 17, 2007Publication date: July 3, 2008Inventors: Theodore W. Randolph, John F. Carpenter, Richard St. John, Lyndal K. Hesterberg, Matthew B. Seefeldt
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Publication number: 20070027305Abstract: A method of recovering a refolded protein involves static mixing a concentrated solution of a denatured protein with a refolding diluent to obtain the refolded protein. The method is particularly suitable for microbially produced recombinant proteins in large processing volumes. The denatured protein solution can be obtained by isolating protein from the microbial host and exposing them to a denaturant. This solution is mixed with a suitable refolding diluent under static mixing conditions compatible with proper folding of the protein so that the refolded protein is obtained, preferably rapidly and with high yield. A system for implementing the refolded protein recovery method includes a static mixer, a conduit inline with and upstream from the static mixer, and an inlet to the conduit upstream of the static mixer, and optionally a dynamic, preferably non-turbulent, mixing vessel downstream from the static mixer.Type: ApplicationFiled: July 28, 2006Publication date: February 1, 2007Applicant: Novartis AGInventors: Richard St. John, Jeffrey Luk, Thucdoan Le
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Publication number: 20060188970Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: ApplicationFiled: January 27, 2006Publication date: August 24, 2006Inventors: Theodore Randolph, John Carpenter, Richard St. John
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Patent number: 7064192Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: GrantFiled: November 12, 2002Date of Patent: June 20, 2006Assignee: The Regents of the University of ColoradoInventors: Theodore W. Randolph, John F. Carpenter, Richard St. John
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Publication number: 20050035839Abstract: A magnetic core assembly for an ignition coil assembly allows unique exterior shapes to be formed by an outer insulation layer, while speeding up the manufacturing process. Generally, the magnetic core assembly comprises a core of ferromagnetic material and an overmold over the exterior of the core. The overmold generally comprises an insulating layer injection molded over the core. Various structures may be incorporated into the core assembly for injection molding, while a second insulative layer provides additional thermal and electrical insulation.Type: ApplicationFiled: August 11, 2003Publication date: February 17, 2005Inventors: Alex Widiger, Todd Sexton, William Walker, Richard St. John
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Publication number: 20030083475Abstract: The present disclosure provides an effective method for the refolding of denatured proteins in solution so that properly folded, biologically active protein in solution is recovered in high yield. The refolding takes place at pressures between about 0.25 kbar to about 3.5 kbar, advantageously at about 1.5 kbar to about 3 kbar. Typically a chaotropic agent is present at a concentration which is not effective for denaturing protein at atmospheric pressure, and optionally, oxidation-reduction reagents can be incorporated in the refolding solution so that native intramolecular disulfide bonds can be formed where that is desired. The method is applicable to substantially all proteins, especially after solubilization and/or denaturation of insoluble protein aggregates, inclusion bodies, or abnormal oligomeric (soluble) aggregates.Type: ApplicationFiled: November 12, 2002Publication date: May 1, 2003Applicant: University Technology CorporationInventors: Theodore W. Randolph, John F. Carpenter, Richard St. John