Abstract: A display device includes first and second pixel electrodes on a substrate to be spaced apart from each other, an inorganic insulating layer on the substrate to partially cover the first pixel electrode and the second pixel electrode, a bank structure on the inorganic insulating layer, where first and second openings overlapping the first and second pixel electrodes are defined through the bank structure, first and second light emitting layers on the first and second pixel electrodes, and first and second common electrodes on the first and second light emitting layers. The bank structure includes first and second bank layers and including different organic insulating materials from each other, the second bank layer has different thicknesses depending on positions thereof, the second bank layer includes tips protruding more than side surfaces of the first bank layer defining the first and second openings, and the first bank layer includes AlNiLaCu.

Abstract: A display device is provided. The display device includes a substrate including a display area and a pad area, which is disposed on one side of the display area, a plurality of conductive layers disposed on the substrate, in the display area and the pad area, a passivation layer disposed on the conductive layers, and a plurality of light-emitting elements disposed on the passivation layer, in the display area, and spaced apart from one another, wherein at least one of the conductive layers includes a first metal layer, a second metal layer, which is disposed on the first metal layer, and a third metal layer, which is disposed on the second metal layer, the first metal layer includes vanadium (V), the second metal layer includes aluminum (Al) or an Al alloy, and the third metal layer includes V or titanium (Ti).

Abstract: A display device includes first and second pixel electrodes on a substrate and spaced apart from each other, an inorganic insulating layer on the substrate and including portions on the first and second pixel electrodes, a bank structure on the inorganic insulating layer with first and second openings overlapping the first and second pixel electrodes, first and second light emitting layers on the first and second pixel electrodes, and first and second common electrodes on the first and second light emitting layers. The bank structure includes a first bank layer, a second bank layer on the first bank layer and including a different metal material from the first bank layer, and a third bank layer on the second bank layer and including an oxide semiconductor layer, and each of the second bank layer and the third bank layer includes a tip on sidewalls defining the first and second openings.

Abstract: The present disclosure relates to separation and purification methods for a vaccine virus using affinity chromatography, and more particularly, to a purification method for a virus capable of obtaining a vaccine virus with a high purity and a high yield using affinity chromatography containing a vaccine virus-affinity resin.

Abstract: The present invention relates to a method for purifying darbepoetin alfa by selectively separating only a structural isoform having a high content of sialic acid from a mixture of structural isoforms of darbepoetin alfa having various contents of sialic acid. Since the method of the present invention is a novel method for purifying darbepoetin alfa which can be conveniently and simply produced, it is possible to remarkably increase productivity due to process efficiency improvement, as well as to yield high purity darbepoetin alfa when mass-producing darbepoetin alfa according to the present invention.

Abstract: The present invention relates to a long-acting human growth hormone NexP-hGH protein and its production method. More specifically, it relates to a specific isoform of long-acting human growth hormone NexP-hGH protein in which human growth hormone is fused with a highly glycosylated alpha-1 antitrypsin mutant whereby long-acting properties in vivo are increased.

Abstract: The present invention relates to a method for purifying darbepoetin alfa by selectively separating only a structural isoform having a high content of sialic acid from a mixture of structural isoforms of darbepoetin alfa having various contents of sialic acid. Since the method of the present invention is a novel method for purifying darbepoetin alfa which can be conveniently and simply produced, it is possible to remarkably increase productivity due to process efficiency improvement, as well as to yield high purity darbepoetin alfa when mass-producing darbepoetin alfa according to the present invention.

Abstract: The present invention relates to a long-acting human growth hormone NexP-hGH protein and its production method. More specifically, it relates to a specific isoform of long-acting human growth hormone NexP-hGH protein in which human growth hormone is fused with a highly glycosylated alpha-1 antitrypsin mutant whereby long-acting properties in vivo are increased.

Abstract: The present invention relates to a fusion protein in which a carboxy terminal of human erythropoietin (EPO) is fused with a carboxy terminal peptide fragment of ? subunit of human chorionic gonadotropin (HCG), to DNA encoding the fusion protein, and to a method for preparation of the fusion protein. The fusion protein has the enhanced in vivo activity of erythropoietin.

Abstract: Provided is a process for purifying human interferon beta from a recombinant human interferon beta-containing culture comprising performing affinity chromatography and cation exchange chromatography, wherein the affinity chromatography includes: adsorbing the interferon beta-containing culture to an equilibrated affinity chromatography column, followed by washing with an equilibration buffer solution; washing the column with a washing buffer solution A of pH 6.5-7.5 containing 30-60 wt % of propylene glycol and a washing buffer solution B of pH 6.5-7.5 containing 10-30 wt % of propylene glycol and 1-2M NaCl; and eluting a human interferon beta-containing fraction with a buffer solution of pH 6.5-7.5 containing 40-60 wt % of propylene glycol and 1-2M NaCl.

Abstract: Provided is a process for purifying human interferon beta from a recombinant human interferon beta-containing culture comprising performing affinity chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC), wherein the affinity chromatography includes: adsorbing the interferon beta-containing culture to an equilibrated affinity chromatography column, followed by washing with an equilibration buffer solution; washing the column with a washing buffer solution A of pH 6.5-7.5 containing 30-60 wt % of propylene glycol and a washing buffer solution B of pH 6.5-7.5 containing 10-30 wt % of propylene glycol and 1-2M NaCl; and eluting a human interferon beta-containing fraction with a buffer solution of pH 6.5-7.5 containing 40-60 wt % of propylene glycol and 1-2M NaCl.

Abstract: The present invention relates to a fusion protein in which a carboxy terminal of human erythropoietin (EPO) is fused with a carboxy terminal peptide fragment of ? subunit of human chorionic gonadotropin (HCG), to DNA encoding the fusion protein, and to a method for preparation of the fusion protein. The fusion protein has the enhanced in vivo activity of erythropoietin.

Abstract: The present invention relates to a fusion protein having enhanced in vivo activity of erythropoietin wherein a carboxy terminal peptide fragment of thrombopoietin is fused with the carboxy terminal of human erythropoietin. This fusion protein has highly enhanced in vivo half-life due to increased carbohydrate content without loss of the inherent activity of erythropoietin, and does not cause any antigenicity when applied to the human body.

Abstract: Provided is a fusion protein comprising, at its carboxy terminal of human erythropoietin (EPO), a mutant having one to four amino acid substitutions in the carboxy terminal peptide (CTP) fragment of a human chorionic gonadotropin (HCG) ? subunit, for increasing an in vivo half-life activity of EPO. The in vivo half-life can be greatly elongated while retaining the intrinsic activity of the EPO, without increasing the sugar chain content.

Abstract: The present invention relates to a fusion protein having enhanced in vivo activity of erythropoietin wherein a carboxy terminal peptide fragment of thrombopoietin is fused with the carboxy terminal of human erythropoietin. This fusion protein has highly enhanced in vivo half-life due to increased carbohydrate content without loss of the inherent activity of erythropoietin, and does not cause any antigenicity when applied to the human body.

Abstract: Provided is a fusion protein comprising, at its carboxy terminal of human erythropoietin (EPO), a mutant having one to four amino acid substitutions in the carboxy terminal peptide (CTP) fragment of a human chorionic gonadotropin (HCG) &bgr; subunit, for increasing an in vivo half-life activity of EPO. The in vivo half-life can be greatly elongated while retaining the intrinsic activity of the EPO, without increasing the sugar chain content.

Abstract: The present invention relates to a vaccine prepared from an attenuated Pseudomonas aeruginosa strains which are obtained by isolating Pseudomonas aeruginosa in a pure state according to the Fisher-Devlin immunotype and then repeatedly purifying the isolated strain, particularly CFCPA 10142 (KCCM 10029), CFCPA 20215 (KCCM 10030), CFCPA 30720 (KCCM 10031), CFCPA 40057 (KCCM 10032), CFCPA 50243 (KCCM 10033), CFCPA 60534 (KCCM 10034) and CFCPA 70018 (KCCM 10035) strains. In addition, the present invention relates to a process for preparing the vaccine for immunization against Pseudomonas aeruginosa infection which contains cell wall proteins having molecular weights ranging from 10,000 to 100,000. The cell wall protein component of the attenuated strain is non-pathogenic and safe, and exhibits excellent antibody formation capacity and is useful for preparation of a vaccine and therapeutic agent.