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Seongnam, South Korea

Trademark
ATGen Co. | Date: 2013-11-28

(Based on Intent to Use) diagnostic preparations for clinical laboratory use and medical laboratory use; diagnostic preparations for clinical research use other than for medical use; diagnostic reagents for clinical laboratory use, medical laboratory use, medical research use and clinical research use. (Based on Intent to Use) diagnostic activators in the nature of a protein that activates immune cells for use in diagnostic kits that tests NK Cell activity; diagnostic preparations for medical diagnostic use; (Based on Intent to Use) (Based on 44(e)) diagnostic reagents for medical diagnostic use.


Provided are a method for diagnosing cancer, a diagnosis kit and compositions useful for measurement of NK cell activity. The incidence of cancer may be diagnosed by monitoring changes in the in vivo immune system through measurement of NK cell activity in blood. Thus, the incidence of cancer may be readily predicted as described herein using a blood sample from a subject.


Trademark
ATGen Co. | Date: 2014-06-04

proteins, neuroproteins, recombinant proteins, heat shock proteins, enzymes, ubiquitins, cancer related proteins, viral antigens, antibodies and hormones; diagnostic kits for clinical laboratory use, medical laboratory use, medical diagnostic use, medical research use and clinical research use; diagnostic activators for use in diagnostic kits; diagnostic preparations for clinical laboratory use, medical laboratory use, medical diagnostic use, medical research use and clinical research use; diagnostic reagents for clinical laboratory use, medical laboratory use, medical diagnostic use, medical research use and clinical research use. manufacture and supply of proteins, neuroproteins, recombinant proteins, heat shock proteins, enzymes, ubiquitins, cancer related proteins, viral antigens, antibodies and hormones; online sale of proteins, neuroproteins, recombinant proteins, heat shock proteins, enzymes, ubiquitins, cancer related proteins, viral antigens, antibodies and hormones; medical research services; clinical research services; research and development of medicines based on protein and peptide therapeutic applications; medical diagnostic services; manufacture and supply of in vitro diagnostic devices and antibody detection kits; custom medical services, namely, DNA cloning services, protein expression and purification services, monoclonal antibody services.


Yang E.,Korean International Vaccine Institute | Cho Y.,Yonsei University | Choi J.-A.,Korean International Vaccine Institute | Choi Y.,Korean International Vaccine Institute | And 7 more authors.
Journal of Microbiology and Biotechnology | Year: 2015

Current influenza vaccines are produced in embryonated chicken eggs. However, egg-based vaccines have various problems. To address these problems, recombinant protein vaccines have been developed as new vaccine candidates. Unfortunately, recombinant proteins frequently encounter aggregation and low stability during their biogenesis. It has been previously demonstrated that recombinantly expressed proteins can be greatly stabilized with high solubility by fusing stabilizing peptide (SP) derived from the C-terminal acidic tail of human synuclein (ATS). To investigate whether SP fusion proteins can induce protective immunity in mice, we produced influenza HA and SP fusion protein using a baculovirus expression system. In in vitro tests, SP-fused recombinant HA1 (SP-rHA1) was shown to be more stable than recombinant HA1 (rHA1). Mice were immunized intramuscularly with baculovirus-expressed rHA1 protein or SP-rHA1 protein (2 μg/mouse) formulated with aluminum hydroxide. Antibody responses were determined by ELISA and hemagglutination inhibition assay. We observed that SP-rHA1 immunization elicited HA-specific antibody responses that were comparable to rHA1 immunization. These results indicate that fusion of SP to rHA1 does not negatively affect the immunogenicity of the vaccine candidate. Therefore, it is possible to apply SP fusion technology to develop stable recombinant protein vaccines with high solubility. © 2015 by The Korean Society for Microbiology and Biotechnology. Source


Bak E.J.,Yonsei University | Park H.G.,ATGC Biotechnology Co. | Lee C.,ATGen Co. | Lee T.-I.,ATGen Co. | And 4 more authors.
BMB Reports | Year: 2011

Chana series are new chalcone derivatives. To evaluate the possibility of Chana series as therapeutic agents of type 2 diabetes, the inhibitory effects of Chana series on the activities of α-glucosidase and DPP-4 were investigated using in vitro enzyme assays, and their effects on adipocyte differentiation were investigated in C3H10T1/2 cells. Chana 1 and Chana 7 among the Chana series showed significant inhibition of α-glucosidase activity. In DPP-4 enzyme assay, Chana 1 exhibited the highest inhibitory activity while Chana 7 did not. In MTT assay, Chana 1 did not show significant cytotoxicity up to a concentration of 250 μM, whereas cytotoxicity was observed with Chana 7 at a concentration of 300 μM. In addition, Chana 1 induced adipocyte differentiation. Therefore, Chana 1 showed inhibitory effects on α-glucosidase and DPP-4 as well as a stimulatory effect on adipocyte differentiation, suggesting that Chana 1 may be a potential beneficial agent for the treatment of type 2 diabetes. Source

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