Patent application number | Description | Published |
20100203589 | METHOD FOR OBTAINING ACTIVE BETA-NGF - The invention relates to a method for producing biologically active β-NGF from the proform proNGF. After expressing the proform of the β-NGF in a prokaryotic host cell, the recombinant protein is isolated in the form of insoluble inactive aggregates (inclusion bodies). After the solubilization thereof in a strong denaturing agent and the subsequent conversion thereof into the natural conformation, which is determined by the disulfide bridges present in the natural β-NGF, biologically active β-NGF is obtained by subsequently splitting-off the prosequence. | 08-12-2010 |
20110034672 | PURIFICATION OF NOT-GLYCOSYLATED POLYPEPTIDES - The current invention reports a method for the purification of a not-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second chromatography step is not a hydroxylapatite chromatography step in case of polypeptides with an isoelectric point below 6.0, and the third chromatography step can be performed in flow-through mode with polypeptides having a low or high isoelectric point. | 02-10-2011 |
20110086026 | ANTIBODIES AGAINST IL-13 RECEPTOR ALPHA 1 AND USES THEREOF - An antibody binding to IL-13Rα1, inhibiting IL-13 bioactivity and comprising a variable heavy and a variable light chain, characterized in that the variable heavy chain amino acid sequence CDR3 of said antibody is selected from the group consisting of the heavy chain CDR3 sequences of SEQ ID NO: 1, 3, 5, 7 or 9 is useful in the treatment of asthma and allergic diseases. | 04-14-2011 |
20120190609 | METHOD FOR PRODUCING A LIPID PARTICLE, THE LIPID PARTICLE ITSELF AND ITS USE - A method for producing a lipid particle comprising the following: i) providing a first solution comprising denatured apolipoprotein, ii) adding the first solution to a second solution comprising at least two lipids and a detergent but no apolipoprotein, and iii) removing the detergent from the solution obtained in ii) and thereby producing a lipid particle. | 07-26-2012 |
20120214200 | PROKARYOTIC EXPRESSION CONSTRUCT - A pro-polypeptide which is useful for the expression of a polypeptide of interest in a prokaryotic cell. Therefore the pro-polypeptide is fused to the N-terminus of the polypeptide of interest. The pro-polypeptide as reported herein provides for improved expression yields and improves the handling of the fusion polypeptide (downstream processing, purification). For example, efficient endotoxin removal is effected while the protein of interest comprising the pro-polypeptide is bound e.g. to an affinity chromatography material. Thereafter the pro-polypeptide can efficiently be cleaved from the polypeptide of interest by the incorporated protease cleavage site with the cognate protease. | 08-23-2012 |
20130190478 | PURIFICATION OF NOT-GLYCOSYLATED POLYPEPTIDES - The current invention reports a method for the purification of a non-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second chromatography step is not a hydroxylapatite chromatography step in case of polypeptides with an isoelectric point below 6.0, and the third chromatography step can be performed in flow-through mode with polypeptides having a low or high isoelectric point. | 07-25-2013 |
20140142283 | METHOD FOR SEPARATION OF MONOMERIC POLYPEPTIDES FROM AGGREGATED POLYPEPTIDES - The present invention relates to methods for obtaining a polypeptide in a monomeric form, the method comprising a) providing a solution containing the polypeptide in monomeric form and in aggregated form, wherein the ratio of monomeric to aggregated form is 4:1 or less, as determined by size exclusion chromatography, b) performing mixed-mode chromatography in bind-and-elute mode, or hydrophobic interaction chromatography in flow-through mode, or a size-exclusion chromatography, and c) performing a weak cation exchange chromatography in bind-and-elute mode or flow-through mode, and thereby obtaining the polypeptide in monomeric form. | 05-22-2014 |
20140220633 | PURIFICATION OF NOT-GLYCOSYLATED POLYPEPTIDES - The current invention reports a method for the purification of a not-glycosylated, heterologous polypeptide, which has been recombinantly produced in a prokaryotic cell, wherein the method comprises three chromatography steps of which the first chromatography step selected from i) hydrophobic charge induction chromatography, or ii) hydrophobic interaction chromatography, or iii) affinity chromatography, or iv) ion exchange chromatography, the second chromatography step is selected from i) anion exchange chromatography, or ii) cation exchange chromatography, or iii) hydroxylapatite chromatography, or iv) hydrophobic interaction chromatography, and the a third chromatography step is selected from i) hydrophobic charge induction chromatography, or ii) anion exchange chromatography, or iii) cation exchange chromatography, or iv) hydrophobic interaction chromatography, whereby the first chromatography step is an affinity chromatography in case of polypeptides capable of interacting with metal ligands, the second chromatography step is not a hydroxylapatite chromatography step in case of polypeptides with an isoelectric point below 6.0, and the third chromatography step can be performed in flow-through mode with polypeptides having a low or high isoelectric point. | 08-07-2014 |
20150041375 | MICRO FLOW FILTRATION SYSTEM AND INTEGRATED MICROFLUIDIC ELEMENT - A micro fluid filtration system ( | 02-12-2015 |
20150041395 | MICRO FLOW FILTRATION SYSTEM AND FLOW FILTRATION METHOD - A micro flow filtration system comprises a fluid circuitry ( | 02-12-2015 |
20150044718 | ON-COLUMN ENZYMATIC CLEAVAGE - Herein is reported a method for obtaining a polypeptide by an immobilized metal ion affinity chromatography from a pro-polypeptide that comprise at its N- or C-terminus an metal ion affinity chromatography tag and a protease cleavage site comprising the step of recovering the polypeptide from the immobilized metal ion affinity chromatography column by incubating the bound pro-polypeptide with a protease, whereby the immobilized metal ion affinity chromatography material has been washed at least once with an urea solution. | 02-12-2015 |
20150056656 | METHOD FOR REDUCTION OF 1->2 READING FRAME SHIFTS - Herein is reported a method for the recombinant production of a polypeptide, which comprises the dipeptide AR, characterized in that the method comprises the recovering of the polypeptide from the cells or the cultivation medium of a cultivation of a cell comprising a nucleic acid encoding the polypeptide and thereby producing the polypeptide, whereby the dipeptide AR comprised in the polypeptide is encoded by the oligonucleotide gca cgt, or the oligonucleotide gcg cgt, or the oligonucleotide gcc cgt. | 02-26-2015 |
20150064746 | METHOD FOR REDUCTION OF 1->3 READING FRAME SHIFTS - Herein is reported a method for the recombinant production of a polypeptide, which comprises the tripeptide QKK, characterized in that the method comprises the step of recovering the polypeptide from the cells or the cultivation medium of a cultivation of a cell comprising a nucleic acid encoding the polypeptide and thereby producing the polypeptide, whereby the tripeptide QKK comprised in the polypeptide is encoded by the oligonucleotide cag aaa aaa or the oligonucleotide caa aag aaa. | 03-05-2015 |
20150083665 | MICRO FLOW FILTRATION SYSTEM AND FLOW FILTRATION METHOD FOR A FLUID SAMPLE - A flow filtration system ( | 03-26-2015 |