Abstract: The present invention relates to an ophthalmic liquid composition comprising: a therapeutically effective amount of aflibercept; a buffer containing sodium acetate or histidine; a sugar including sucrose, trehalose or a combination thereof; and a surfactant that is polysorbate or poloxamer, and a composition for stabilizing aflibercept. The ophthalmic liquid composition of the present invention is characterized by the excellent effect of imparting stability against stresses upon agitation, repeated freezing and thawing, ultraviolet (UV) exposure, and storage at a high temperature.

Abstract: The present invention relates to an antibody specifically bound to a coagulation factor VIII or an antigen binding fragment thereof, and a use thereof. More specifically, the present invention relates to: an antibody which is specifically bound to a coagulation factor VIII including specific sequences of heavy chain CDR and light chain CDR, or an antigen binding fragment thereof; a column in which the antibody or the antigen binding fragment thereof is coupled to a column stationary phase as a ligand for isolating or purifying a recombinant coagulation factor VIII; and a method for purifying a recombinant coagulation factor VIII using the same.

Abstract: The present invention provides an antibody having cross-linking ability against human Sema3A and mouse Sema3A. The antibody of the present invention can be used as therapeutic antibody drugs for inhibiting Sema3A in various cancers in which Sema3A expression is high, such as glioblastoma, pancreatic cancer and liver cancer. Since Sema3A is considered to be a therapeutic target of diabetic retinopathy, autoimmune arthritis, neuropathic pain and osteoporosis, the antibody of the present invention or an antigen binding fragment thereof can be used as a therapeutic agent for associated diseases in addition to an anti-cancer drug. The antibody of the present invention inhibits the growth of cancer cells derived from various carcinomas through inhibition of Sema3A function due to high anti-Sema3A binding, and inhibits the movement of cancer cells through inhibition of phosphorylation of ERK among Sema3A lower signaling substances.

Abstract: The present invention provides an antibody having cross-linking ability against human Sema3A and mouse Sema3A. The antibody of the present invention can be used as therapeutic antibody drugs for inhibiting Sema3A in various cancers in which Sema3A expression is high, such as glioblastoma, pancreatic cancer and liver cancer. Since Sema3A is considered to be a therapeutic target of diabetic retinopathy, autoimmune arthritis, neuropathic pain and osteoporosis, the antibody of the present invention or an antigen binding fragment thereof can be used as a therapeutic agent for associated diseases in addition to an anti-cancer drug. The antibody of the present invention inhibits the growth of cancer cells derived from various carcinomas through inhibition of Sema3A function due to high anti-Sema3A binding, and inhibits the movement of cancer cells through inhibition of phosphorylation of ERK among Sema3A lower signaling substances.

Abstract: The present invention provides an antibody having cross-linking ability against human Sema3A and mouse Sema3A. The antibody of the present invention can be used as therapeutic antibody drugs for inhibiting Sema3A in various cancers in which Sema3A expression is high, such as glioblastoma, pancreatic cancer and liver cancer. Since Sema3A is considered to be a therapeutic target of diabetic retinopathy, autoimmune arthritis, neuropathic pain and osteoporosis, the antibody of the present invention or an antigen binding fragment thereof can be used as a therapeutic agent for associated diseases in addition to an anti-cancer drug. The antibody of the present invention inhibits the growth of cancer cells derived from various carcinomas through inhibition of Sema3A function due to high anti-Sema3A binding, and inhibits the movement of cancer cells through inhibition of phosphorylation of ERK among Sema3A lower signaling substances.

Abstract: There is provided an expression vector for animal cell having an increased gene expression efficiency, and particularly, an expression vector for animal cells including a MAR element and a SAR element, which are gene expression increasing factors, at a 5? end of a promoter, a 3? end of a transcription termination site, or at both of the 5? end of the promoter and the 3? end of the transcription termination site. The expression vector for animal cells according to the present invention exhibits remarkably increased gene expression efficiency as compared to conventional expression vectors for animal cells, such that protein expression of foreign genes may be significantly increased using this expression vector for animal cells. Particularly, the expression vector for animal cells according to the present invention may be useful in that a high-expression cell line may be secured even without MTX amplification.

Abstract: There is provided an expression vector for animal cell having an increased gene expression efficiency, and particularly, an expression vector for animal cells including a MAR element and a SAR element, which are gene expression increasing factors, at a 5? end of a promoter, a 3? end of a transcription termination site, or at both of the 5? end of the promoter and the 3? end of the transcription termination site. The expression vector for animal cells according to the present invention exhibits remarkably increased gene expression efficiency as compared to conventional expression vectors for animal cells, such that protein expression of foreign genes may be significantly increased using this expression vector for animal cells. Particularly, the expression vector for animal cells according to the present invention may be useful in that a high-expression cell line may be secured even without MTX amplification.

Abstract: The present invention relates to mammalian expression vectors including nuclear matrix attachment region of human interferon ?, and more particularly to pPGM-1, pPGM-2 and pPGM-3 including nuclear matrix attachment region of interferon ? gene. Those expression vectors confer position independent expression of the introduced foreign gene, thus increasing the frequency of colonies which efficiently express the recombinant protein.