Patents by Inventor Xinli Lin
Xinli Lin 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: 20230092348Abstract: A safety design system assists in the development of compliant industrial safety systems. User interfaces provided by the design system guide the user through an intuitive workflow for carrying out risk assessment analysis on industrial assets and designing safety functions for mitigating risks associated with the industrial assets. These user interfaces offer multiple views of safety system design aspects, including a layout view and a table view that offer alternative views of hazard and safety function data. The system also guides the user to the selection of suitable input, logic, and output devices for each safety function based on results of the risk assessment and local industrial safety standards.Type: ApplicationFiled: September 22, 2021Publication date: March 23, 2023Inventors: David Main-Reade, Xinli Lin, Jonathan B. Johnson, Susan Stuebe, Matthew R. Kuenzi, KEVIN ZOMCHEK, TODD M. BISSELL, Burt Sacherski, LINDA A. FREEMAN, USHA R. KOLUKULA, IAN MURGATROYD
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Publication number: 20210330762Abstract: Provided are methods for producing biologically active mutant recombinant plasminogen polypeptides with desired pharmaceutical properties. The refolded polypeptides may be treated with a plasminogen activator, such as tPA, urokinase, or streptokinase to generate biologically active mutant plasmin polypeptide for pharmaceutical use. Methods are also provided to producing biologically active fusion recombinant mutant plasminogen/plasmin polypeptides that can cross the BBB through receptor mediated transcytosis. The fusion partner may carry the mutant plasminogen/plasmin polypeptides into the brain for increased therapeutic efficiency.Type: ApplicationFiled: April 23, 2020Publication date: October 28, 2021Inventors: Xinli LIN, Jiali GAO
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Publication number: 20210121419Abstract: The present disclosure is related to a metformin compounded composition and application thereof. The disclosure provides active ingredients of composition dosage forms, comprising active ingredients including metformin, omega-3 fatty acid, statin, and vitamins. The whole or part of the active ingredients can be manufactured into a single dosage form for preventing or treating a special disease or enhance health in general. The diseases that can be prevented or treated include cardiovascular diseases, nervous system diseases, cancer, diabetes, autoimmune diseases, or any other diseases that can be treated with the provided formulations. Because of the broad applicability for preventing diseases and enhancing health, the application of the invented formulation may provide “health and longevity” for general population.Type: ApplicationFiled: January 3, 2021Publication date: April 29, 2021Inventor: Xinli LIN
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Publication number: 20200354433Abstract: Provided is a new AAT triple-mutant, and methods to produce and purify the new entity. The new mutant is produced by a structure-based protein design to provide a more thermostable and oxidation-resistant agent for various pharmaceutical applications. The present invention also provides methods for E. coli expression, inclusion body refolding, and purification of the triple-mutant. Furthermore, the invention also provides methods for chemically modifying the purified drug candidate to provide a longer in vivo half-life and achieve better drug efficacy.Type: ApplicationFiled: July 29, 2020Publication date: November 12, 2020Inventors: Xinli LIN, Lanfen LI
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Publication number: 20120165268Abstract: Biologically active tetrameric p53 proteins and p53 fusion proteins are provided. These proteins may be generated and refolded into tetrameric form using denatured proteins produced from E. coli. Therapeutic uses of p53 proteins and p53 fusion proteins are also provided.Type: ApplicationFiled: May 28, 2009Publication date: June 28, 2012Applicant: Proteom Tech, Inc.Inventors: Xinli Lin, Michelle Lafevre-Bernt
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Patent number: 7829669Abstract: Methods for the production of purified, catalytically active, recombinant memapsin 2 have been developed. The substrate and subsite specificity of the catalytically active enzyme have been determined. The substrate and subsite specificity information was used to design substrate analogs of the natural memapsin 2 substrate that can inhibit the function of memapsin 2. The substrate analogs are based on peptide sequences, shown to be related to the natural peptide substrates for memapsin 2. The substrate analogs contain at least one analog of an amide bond which is not capable of being cleaved by memapsin 2. Processes for the synthesis of two substrate analogues including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues, OMR99-1 and OM99-2, were synthesized. OM99-2 is based on an octapeptide Glu-Val-Asn-Leu-Ala-Ala-Glu-Phe (SEQ ID NO:28) with the Leu-Ala peptide bond substituted by a transition-state isostere hydroxyethylene group (FIG. 1).Type: GrantFiled: August 3, 2007Date of Patent: November 9, 2010Assignees: Oklahoma Medical Research Foundation, The Board of Trustees of the University of IllinoisInventors: Gerald Koelsch, Jordan J. N. Tang, Lin Hong, Arun K. Ghosh, Xinli Lin
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Publication number: 20100144622Abstract: Methods of producing properly refolded recombinant plasminogen and plasmin polypeptide are provided. Denatured recombinant plasminogen polypeptide is refolded by first solubilizing the polypeptide with a chaotroph and reducing and oxidizing agents at high pH, followed by refolding in the presence of reduced concentration of chaotroph and reducing and oxidizing agents and in the presence of arginine.Type: ApplicationFiled: September 28, 2007Publication date: June 10, 2010Inventors: Xinli Lin, Daniel Medynski
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Publication number: 20080112946Abstract: Methods for the production of purified, catalytically active, recombinant memapsin 2 have been developed. The substrate and subsite specificity of the catalytically active enzyme have been determined. The substrate and subsite specificity information was used to design substrate analogs of the natural memapsin 2 substrate that can inhibit the function of memapsin 2. The substrate analogs are based on peptide sequences, shown to be related to the natural peptide substrates for memapsin 2. The substrate analogs contain at least one analog of an amide bond which is not capable of being cleaved by memapsin 2. Processes for the synthesis of two substrate analogues including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues, OMR99-1 and OM99-2, were synthesized. OM99-2 is based on an octapeptide Glu-Val-Asn-Leu-Ala-Ala-Glu-Phe (SEQ ID NO:28) with the Leu-Ala peptide bond substituted by a transition-state isostere hydroxyethylene group (FIG. 1).Type: ApplicationFiled: August 3, 2007Publication date: May 15, 2008Inventors: Gerald Koelsch, Jordan J. N. Tang, Lin Hong, Arun K. Ghosh, Xinli Lin
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Publication number: 20070218535Abstract: Methods of producing properly folded recombinant ?1-antitrypsin (AAT) polypeptide are provided. Denatured recombinant AAT polypeptide is refolded by first solubilizing the polypeptide with a chaotroph at high pH, followed by refolding in the presence of reduced concentrations of chaotroph and in the presence of PEG, glycerol or sucrose, or a detergent while the pH is slowly reduced and is generally maintained.Type: ApplicationFiled: November 28, 2006Publication date: September 20, 2007Inventors: Xinli Lin, Daniel Medynski
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Publication number: 20070009506Abstract: Highly efficient methods of producing properly folded recombinant urokinase are provided. Denatured recombinant pro-urokinase is refolded by first solubilizing the protein with a chaotroph at high pH, followed by refolding in the presence of reduced concentrations of chaotroph while the pH is slowly reduced.Type: ApplicationFiled: May 31, 2006Publication date: January 11, 2007Inventor: Xinli Lin
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Publication number: 20060287504Abstract: A universal folding method that has been demonstrated to be effective in refolding a variety of very different proteins expressed in bacteria as inclusion bodies has been developed. Representative proteins that can be dissolved and refolded in biologically active form, with the native structure, are shown in Table I. The method has two key steps to unfold and then refold the proteins expressed in the inclusion bodies. The first step is to raise the pH of the protein solution in the presence of denaturing agents to pH greater than 9, preferably 10. The protein solution may be maintained at the elevated pH for a period of up to about 24 hours, or the pH immediately decreased slowly, in increments of about 0.2 pH units/24 hours, until the solution reaches a pH of about 8.0, or both steps used. In the preferred embodiment, purified inclusion bodies are dissolved in 8 M urea, 0.1 M Tris, 1 mM glycine, 1 mM EDTA, 10 mM beta-mercaptoethanol, 10 mM dithiothreitol (DTT), 1 mM redued glutathion (GSH), 0.Type: ApplicationFiled: August 18, 2006Publication date: December 21, 2006Inventor: Xinli Lin
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Patent number: 7119166Abstract: A universal folding method that has been demonstrated to be effective in refolding a variety of very different proteins expressed in bacteria as inclusion bodies has been developed. Representative proteins that can be dissolved and refolded in biologically active form, with the native structure, are shown in Table I. The method has two key steps to unfold and then refold the proteins expressed in the inclusion bodies. The first step is to raise the pH of the protein solution in the presence of denaturing agents to pH greater than 9, preferably 10. The protein solution may be maintained at the elevated pH for a period of up to about 24 hours, or the pH immediately decreased slowly, in increments of about 0.2 pH units/24 hours, until the solution reaches a pH of about 8.0, or both steps used. In the preferred embodiment, purified inclusion bodies are dissolved in 8 M urea, 0.1 M Tris, 1 mM glycine, 1 mM EDTA, 10 mM beta-mercaptoethanol, 10 mM dithiothreitol (DTT), 1 mM reduced glutathione (GSH), 0.Type: GrantFiled: April 17, 2003Date of Patent: October 10, 2006Assignee: Oklahoma Medical Research FoundationInventor: Xinli Lin
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Publication number: 20050233961Abstract: The invention features methods and compositions for treating cancer by administering an effective amount of a VEGI-192A polypeptide. In some embodiments, the cancer is lung cancer or breast cancer.Type: ApplicationFiled: December 13, 2004Publication date: October 20, 2005Inventors: Xinli Lin, Luyuan Li
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Publication number: 20050227920Abstract: Methods of producing properly folded recombinant VEGI polypeptide are provided. Denatured recombinant VEGI polypeptide is refolded by first solubilizing the polypeptide with a chaotroph at high pH, followed by refolding in the presence of reduced concentrations of chaotroph and in the presence of a detergent while the pH is slowly reduced.Type: ApplicationFiled: December 13, 2004Publication date: October 13, 2005Inventor: Xinli Lin
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Publication number: 20050037486Abstract: An apparatus for refolding proteins and a method of using an apparatus for refolding proteins is provided in which a refolding process for proteins can be carried out for various proteins, efficiently and accurately, and without manual intervention.Type: ApplicationFiled: May 13, 2004Publication date: February 17, 2005Applicants: Universal Bio Research Co., Ltd., ProteomTech, Inc.Inventors: Xinli Lin, Peter Burrowes, Chris Kusumoto, Hideji Tajima
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Publication number: 20040265298Abstract: Highly efficient methods of producing properly folded recombinant urokinase are provided. Denatured recombinant pro-urokinase is refolded by first solubilizing the protein with a chaotroph at high pH, followed by refolding in the presence of reduced concentrations of chaotroph while the pH is slowly reduced.Type: ApplicationFiled: April 16, 2004Publication date: December 30, 2004Inventor: Xinli Lin
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Publication number: 20030199676Abstract: A universal folding method that has been demonstrated to be effective in refolding a variety of very different proteins expressed in bacteria as inclusion bodies has been developed. Representative proteins that can be dissolved and refolded in biologically active form, with the native structure, are shown in Table I. The method has two key steps to unfold and then refold the proteins expressed in the inclusion bodies. The first step is to raise the pH of the protein solution in the presence of denaturing agents to pH greater than 9, preferably 10. The protein solution may be maintained at the elevated pH for a period of up to about 24 hours, or the pH immediately decreased slowly, in increments of about 0.2 pH units/24 hours, until the solution reaches a pH of about 8.0, or both steps used. In the preferred embodiment, purified inclusion bodies are dissolved in 8 M urea, 0.1 M Tris, 1 mM glycine, 1 mM EDTA, 10 mM beta-mercaptoethanol, 10 mM dithiothreitol (DTT), 1 mM redued glutathion (GSH), 0.Type: ApplicationFiled: April 17, 2003Publication date: October 23, 2003Applicant: Oklahoma Medical Research FoundationInventor: Xinli Lin
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Patent number: 6583268Abstract: A universal folding method that has been demonstrated to be effective in refolding a variety of very different proteins expressed in bacteria as inclusion bodies has been developed. Representative proteins that can be dissolved and refolded in biologically active form, with the native structure, are shown in Table I. The method has two key steps to unfold and then refold the proteins expressed in the inclusion bodies. The first step is to raise the pH of the protein solution in the presence of denaturing agents to pH greater than 9, preferably 10. The protein solution may be maintained at the elevated pH for a period of up to about 24 hours, or the pH immediately decreased slowly, in increments of about 0.2 pH units/24 hours, until the solution reaches a pH of about 8.0, or both steps used. In the preferred embodiment, purified inclusion bodies are dissolved in 8 M urea, 0.1 M Tris, 1 mM glycine, 1 mM EDTA, 10 mM beta-mercaptoethanol, 10 mM dithiothreitol (DTT), 1 mM redued glutathion (GSH), 0.Type: GrantFiled: December 28, 2000Date of Patent: June 24, 2003Assignee: Oklahoma Medical Research FoundationInventor: Xinli Lin
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Patent number: 6545127Abstract: Methods for the production of purified, catalytically active, recombinant memapsin 2 have been developed. The substrate and subsite specificity of the catalytically active enzyme have been determined. The substrate and subsite specificity information was used to design substrate analogs of the natural memapsin 2 substrate that can inhibit the function of memapsin 2. The substrate analogs are based on peptide sequences, shown to be related to the natural peptide substrates for memapsin 2. The substrate analogs contain at least one analog of an amide bond which is not capable of being cleaved by memapsin 2. Processes for the synthesis of two substrate analogues including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues, OMR99-1 and OM99-2, were synthesized. OM99-2 is based on an octapeptide Glu-Val-Asn-Leu-Ala-Ala-Glu-Phe (SEQ ID NO:28) with the Leu-Ala peptide bond substituted by a transition-state isostere hydroxyethylene group (FIG. 1).Type: GrantFiled: June 27, 2000Date of Patent: April 8, 2003Assignee: Oklahoma Medical Research FoundationInventors: Jordan J. N. Tang, Xinli Lin, Gerald Koelsch, Lin Hong
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Publication number: 20020164760Abstract: Methods for the production of purified, catalytically active, recombinant memapsin 2 have been developed. The substrate and subsite specificity of the catalytically active enzyme have been determined. The substrate and subsite specificity information was used to design substrate analogs of the natural memapsin 2 substrate that can inhibit the function of memapsin 2. The substrate analogs are based on peptide sequences, shown to be related to the natural peptide substrates for memapsin 2. The substrate analogs contain at least one analog of an amide bond which is not capable of being cleaved by memapsin 2. Processes for the synthesis of two substrate analogues including isosteres at the sites of the critical amino acid residues were developed and the substrate analogues, OMR99-1 and OM99-2, were synthesized. OM99-2 is based on an octapeptide Glu-Val-Asn-Leu-Ala-Ala-Glu-Phe (SEQ ID NO:28) with the Leu-Ala peptide bond substituted by a transition-state isostere hydroxyethylene group (FIG. 1).Type: ApplicationFiled: February 28, 2001Publication date: November 7, 2002Applicant: Oklahoma Medical Research FoundationInventors: Xinli Lin, Gerald Koelsch, Jordan J.N. Tang