Alteogen, Inc.

Cj Healthcare Corporation

Lucky Corporation Co., Ltd.

Samsung Electronics Co., Ltd.

Soon Jae Park

So-Young Lee

Hye-Shin Chung

Sunbae Lee

Minsoo Byun

Sang Hyun Lee

Sunghyun Kim

Ji-Sun Kim

Sang Hoon Yun

Jeong Soo Cho

Seung Joon Lee

Hojung Lee

Sang Mee Lee

Jin Hwan Kim

Hyung-Nam Song

Yong Mo Kim

Sun-Ah You

Hye Shin Chung

Bum Joon Kim

Jung Hee Kim

Young Joon Park

Chang Woo Lee

Jee Won Ahn

Dong Eok Lee

Ki Wan Kim

Seong-Kyu Kim

Soon Chang Kwon

Ji Hyun Moon

Ji Sun Kim

Chi Hye Park

Jeong Kyun Woo

Hyoung Taek Lim

Seung Joo Lee

Won Jeong Lee

Young Mee Lee

Yoon Jung Lee

Hoo Keun Oh

Chung Min Lee

Chang Bong Jun

Jun Young Kim

Ji Hyeon Yeon

Sung Yoo Cho

Seonhun Kwon

Sun-ah Yoo

Teug Y Won

Sun Ah You

Kyuwan Kim

Ki Seok Nam

Kibum Park

Jaehyeong Ko

Gil Bu Kang

The present invention is related to the field of protein engineering technology which increases the enzymatic activity and thermal stability of human hyaluronidase which is an enzyme that hydrolyzes hyaluronic acid; and more particularly to hyaluronidase PH20 variants or fragments thereof, which comprise one or more amino acid residue substitutions in the region corresponding to the alpha-helix region and its linker region in the amino acid sequence of wild-type PH20 of SEQ ID NO: 1 and in which one or more amino acid residues at the N-terminus and/or the C-terminus are selectively cleaved additionally. Specifically, the present invention relates to PH20 variants or fragments thereof, which comprise one or more amino acid residue substitutions selected from the group consisting of T341A, T341C, T341G, S343E, M345T, K349E, L353A, L354I, N356E and I361T in wild-type PH20 having the amino acid sequence of SEQ ID NO: 1, and additionally comprise the substitution of amino acids located in the alpha-helix 8 region and/or a linker region between alpha-helix 7 and alpha-helix 8 in the amino acid sequence of wild-type PH20, and in which one or more amino acids located at the N-terminal and C-terminal regions are deleted.

Hyaluronidase variants and pharmaceutical composition comprising the same

Disclosed is a method for producing hyaluronidase or a variant thereof. Specifically, the method is capable of changing the N-glycan levels under culture conditions including a controlled concentration of glucose in the culture medium and a decreased culture temperature for a specific culture time period, thereby increasing the specific activity by 10% or more and improving the quality and production yield.

Method for producing recombinant hyaluronidase

The present disclosure relates to an antibody-drug conjugate in which a modified antibody comprising a motif having a specific structure at the end of the antibody is conjugated to a drug via a linker, and a composition comprising the same, and more particularly to a modified antibody-drug conjugate (mADC) comprising a modified antibody that has a significantly increased conjugation yield of drug due to a motif bound to the heavy chain or light chain C-terminus of the antibody, and to a composition comprising the same.

Antibody-drug conjugate comprising modified antibody

The present invention relates to a growth hormone receptor antagonist comprising a growth hormone variant which is modified by substitution of one or more amino acids of growth hormone. Further, the growth hormone receptor antagonist of the present invention may further comprise a long-acting carrier which is fused to the growth hormone variant. The growth hormone receptor antagonist may have strong binding potency to growth hormone receptor and may exhibit a long-lasting antagonistic action.

Growth hormone receptor antagonists and fusion proteins thereof

A modified antibody that binds specifically to folate receptor alpha (FOLR1) and blocks the activity of FOLR1 with an increased binding affinity, an antigen-binding fragment thereof, a composition containing the antibody or fragment, and their uses are disclosed. The modified antibody or antigen-binding fragment thereof may be used for the prevention or treatment of cancer proliferative disorder associated with an increased FOR1 expression, and may also be used for diagnosis of the disease. The proliferative disorder may be cancer.

Antibody specifically binding to FOLR1 and uses thereof

The present invention relates to a method for preparing a fusion protein having an IgG Fc domain and, specifically, to a method for preparing a fusion protein having an IgG Fc domain, the method additionally comprising a step of culturing cells, which produce the fusion protein, at a decreased culture temperature, thereby increasing cell growth and cell viability so as to increase fusion protein productivity and inhibiting aggregate generation so as to improve quality and production yield.

Method for producing fusion protein having IgG Fc domain

A stable liquid formulation includes a fusion protein having an Fc domain of a human immunoglobulin G (IgG), in particular, a protein in which an Fc domain of a human immunoglobulin G (IgG) and a soluble extracellular domain of a vascular endothelial growth factor (VEGF) receptor are fused (e.g., aflibercept)). A composition for stabilizing a protein and a method for stabilizing a protein in which an Fc domain of an IgG and a soluble extracellular domain of a VEGF receptor are fused are disclosed. The present invention improves therapeutic effects on various ophthalmic diseases (e.g., retinal vein occlusion, diabetic macular edema, choroidal neovascularization and wet age-related macular degeneration, etc.) caused by abnormal angiogenesis, while pursuing stabilization of bioactivity through a stable liquid formulation suitable for intravitreal injection of an anti-VEGF-Fc fusion protein including aflibercept.

Stable liquid formulation of fusion protein with IgG Fc domain

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. The present invention also relates to a high-purity purification method for NexP-hGH, which includes the steps of: (a) carrying out anion-exchange resin chromatography on a biological emulsion comprising NexP-hGH in which human growth hormone is fused with an alpha-1 antitrypsin mutant; (b) carrying out hydrophobic resin chromatography on the biological emulsion comprising NexP-hGH, or on the eluate produced in step (a); and (c) carrying out affinity chromatography, entailing packing with a resin to which anti-alpha-1 antitrypsin antibody fragments are attached, on the biological emulsion comprising NexP-hGH and on the eluate produced in step (a) or step (b).

Method of purifying a long-acting human growth hormone

The present invention relates to a composition for stabilizing TNF&#x3b1;-binding protein exhibiting physiological activity, and more specifically, to a composition for stabilizing protein including basic amino acid and sugar and/or ammonium salt, a pharmaceutical formulation including the same, and a method for stabilizing TNF&#x3b1;-binding protein. The formulation including basic amino acid; and sugar and/or ammonium salt according to the present invention effectively inhibits aggregation, denaturation and oxidation of TNF&#x3b1;-binding protein used for treating various diseases, for example, an anti-TNF-alpha antibody, such that the protein is capable of being preserved and stored for a long time, which is widely usable and effective in a medical field using TNF&#x3b1;-binding protein, for example, an anti-TNF-alpha antibody.

Composition for stabilizing protein and pharmaceutical formulation comprising the same

The present invention relates to an antibody in which a motif composed of an amino acid or peptide sequence including one or more cysteine residues is bound to the terminus of a parent antibody, particularly the terminus of the heavy chain of the parent antibody. Also, the present invention relates to a modified antibody-drug conjugate (mADC) comprising a drug bound to the antibody, and a method for producing the antibody or the modified antibody-drug conjugate. The modified antibody-drug conjugate according to the invention can accurately deliver the drug to a target cell due its high specificity to antigen, and thus can increase the therapeutic effect of the drug. Also, it can increase the usability of drugs, particularly anticancer drugs, the use of which is restricted due to their toxicity, despite their high efficacy. Moreover, the invention relates to a composition for treatment of diseases, particularly cancers, which comprise the modified antibody-drug conjugate.

Modified antibody in which motif comprising cysteine residue is bound, modified antibody-drug conjugate comprising the modified antibody, and production method for same

The present invention relates to a composition for stabilizing a fusion protein of a physiologically active protein and an Fc domain, and more particularly to a method of stabilizing a fusion protein of a protein and an Fc domain using a composition containing an ammonium salt or a combination of an ammonium salt and succinate. The composition containing an ammonium salt or a combination of an ammonium salt and succinate according to the present invention can effectively inhibit the aggregation of the protein-Fc domain fusion protein, and thus enables the fusion protein to be stored for a long period of time. Accordingly, the composition can be widely used in the medical field that uses the protein-Fc domain fusion protein.

Composition for stabilizing fusion protein in which protein and FC domain are fused

A novel alpha-1 antitrypsin variant, a method of preparing the same, and use thereof are provided. The alpha-1 antitrypsin variant has excellent stability in the body and maintains an inhibitory effect on elastase activities because the blood half-life (t) and the area under blood drug concentration vs. time curve (AUC) are remarkably increased by adding an N-glycosylation site in animal cells through amino acid mutation between 1and 25positions of the N-terminus of alpha-1 antitrypsin. Therefore, the alpha-1 antitrypsin variant can be useful in preventing or treating alpha-1 antitrypsin deficiency.

Alpha-1 antitrypsin variant, preparation method thereof and use thereof

An extracellular leucine aminopeptidase was isolated from the culture medium of Streptomyces therrnonitrificans which is a Zn.sup.2+ -dependent metalloenzyme which comprises an amino acid sequence Lys-Phe-Ser-Lys-Lys-Phe-Asn-Glu (SEQ ID NO: 3) at the N-terminal thereof, and amino acid sequences of Glu-Pro-Gly-Thr-Gly-Ala-Leu-Glu-Pro (SEQ ID NO: 4) and Asn-Pro-Asp-Ile-Val-Tyr (SEQ ID NO: 5) at other regions thereof. The aminopeptidase has a pH optimum of 7.5 to 9.0, a temperature optimum of 30.degree. to 50.degree. C., and an apparent molecular weight as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis under reducing conditions of 41 to 45 kDa, and as determined by gel filtration under native state conditions of 36 to 40 kDa.

Extracellular aminopeptidase isolated from Streptococcus

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Daejeon, South Korea

Soon Jae Park