Siheung, South Korea
Siheung, South Korea

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Sinha N.D.,Boxborough | Jung K.E.,ST Pharm Co.
Current Protocols in Nucleic Acid Chemistry | Year: 2015

Chromatographic methods have been essential tools for analysis and purification of synthetic oligonucleotides since the 1970s. Significant developments in terms of instruments and stationary phases (media) have been made during the past several decades; among the latest are sub-micron to micron particles for the media, as well as ultra performance liquid chromatography (UPLC). Micron and sub-micron particles have increased product resolution. Applications of recently developed methods such as IP-RP-HPLC and LC-MS have been discussed for analysis, along with use of various methods for purification. Utilization of UPLC has decreased analysis time, increasing the throughput for analysis. Commonly used methods for analysis and purification of synthetic oligonucleotides have been described in this unit. © 2015 by John Wiley & Sons, Inc.


Patent
MEDIPLEX Corporation, Snu R&Db Foundation and St Pharm Co. | Date: 2012-11-29

The present invention relates to a method for preparing an end site-specific macromolecule-bile acid oligomer conjugate, comprising conjugating a bile acid oligomer which is prepared by oligomerization of two or more bile acid monomers to the terminal site of a macromolecule; a method for body absorption of an end site-specific macromolecule-bile acid oligomer conjugate, comprising administering the macromolecule-bile acid oligomer conjugate prepared by the above method to a subject orally; an end site-specific macromolecule-bile acid oligomer conjugate wherein the bile acid oligomer is conjugated to the terminal site of macromolecule; a composition comprising the conjugate; an oral formulation for macromolecule comprising the conjugate, a solubilizer, an excipient, a disintegrant, a binder, and a lubricant; a pharmaceutical composition comprising a heparin-bile acid oligomer conjugate wherein the bile acid oligomer is conjugated to the terminal site of heparin; and a method for treating thrombosis using said composition.


Patent
St Pharm Co. | Date: 2014-10-27

The present invention provides a novel method for preparing lacosamide with high chiral purity from D-serine. The method of the present invention can obtain lacosamide with high chiral purity in a high yield through a simple and environmentally-friendly process and thus can be easily applied to mass production.


Patent
Hyosung Corporation and St Pharm Co. | Date: 2014-07-16

Provided are a novel polyketone polymerization catalyst and a method of preparing a ligand, which can reduce production costs and can enable commercial mass synthesis by using ((2,2-dimethyl-1,3-dioxane-5,5-diyl)bis(methylene))bis(bis(2-methoxyphenyl)phosphine) as a ligand constituting the polykeytone polymerization catalyst, the ligand having a simple structure and a small molecular weight while having high activity.


Patent
Hyosung Corporation and ST Pharm Co. | Date: 2016-05-25

Provided are a novel polyketone polymerization catalyst and a method of preparing a ligand, which can reduce production costs and can enable commercial mass synthesis by using ((2,2-dimethyl-1,3-dioxane-5,5-diyl)bis(methylene))bis(bis(2-methoxyphenyl)phosphine) as a ligand constituting the polykeytone polymerization catalyst, the ligand having a simple structure and a small molecular weight while having high activity.


Patent
St Pharm Co. | Date: 2012-01-18

The present invention provides a method which enables the simple, economical and high-yield production which is a key intermediate of antidiabetic drug Januvia.


Patent
ST Pharm Co. | Date: 2016-09-14

The present invention provides a novel method for preparing lacosamide with high chiral purity from D-serine. The method of the present invention can obtain lacosamide with high chiral purity in a high yield through a simple and environmentally-friendly process and thus can be easily applied to mass production.


PubMed | ST Pharm. Co. and Korea Research Institute of Bioscience and Biotechnology
Type: Journal Article | Journal: Cell death & disease | Year: 2017

DNA damage-induced apoptosis suppressor (DDIAS) rescues lung cancer cells from apoptosis in response to DNA damage. DDIAS is transcriptionally activated by NFATc1 and EGF-mediated ERK5/MEF2B, leading to cisplatin resistance and cell invasion. Therefore, DDIAS is suggested as a therapeutic target for lung cancer. Here, we report that DDIAS stability is regulated by E3 U-box ubiquitin ligase carboxyl terminus of HSP70-interacting protein (CHIP)-mediated proteasomal degradation. We first isolated CHIP as an interacting partner of DDIAS by yeast two-hybrid screening. CHIP physically associated with both the N- and C-terminal regions of DDIAS, targeting it for proteasomal degradation and reducing the DDIAS half-life. CHIP overexpression analyses indicated that the tetratrico peptide repeat (TPR) domain and the U-box are required for DDIAS ubiquitination. It is likely that HSP70-bound DDIAS is recruited to the CHIP E3 ligase via the TPR domain, suggesting DDIAS as a client protein of HSP70. In addition, CHIP overexpression in lung cancer cells expressing high DDIAS levels induced significant growth inhibition by enhancing DDIAS degradation. Furthermore, simultaneous CHIP overexpression and DNA damage agent treatment caused a substantial increase in the apoptosis of lung cancer cells. Taken together, these findings indicate that the stability of the DDIAS protein is regulated by CHIP/HSP70-mediated proteasomal degradation and that CHIP overexpression stimulates the apoptosis of lung cancer cells in response to DNA-damaging agents.


PubMed | ST Pharm. Co., Korea Research Institute of Bioscience and Biotechnology and Korean University of Science and Technology
Type: Journal Article | Journal: Biochimica et biophysica acta | Year: 2016

DNA damage induced apoptosis suppressor (DDIAS) is an anti-apoptotic protein that promotes cancer cell survival. We previously reported that DDIAS is transcriptionally activated by nuclear factor of activated T cells 2 (NFATc1). However, the upstream regulation of DDIAS expression by growth factors has not been studied. Here, we demonstrate that DDIAS expression is induced by extracellular signal-regulated kinase 5 (ERK5) and myocyte enhancer factor 2B (MEF2B) in response to epidermal growth factor (EGF) and that it positively regulates -catenin signaling in HeLa cells. The genetic or pharmacological inhibition of ERK5 suppressed DDIAS induction following EGF exposure and the overexpression of constitutively active MEK5 (CA-MEK5) enhanced DDIAS expression. In chromatin immunoprecipitation assays, MEF2B, a downstream target of ERK5, exhibited sequence-specific binding to a MEF2 binding site in the DDIAS promoter following treatment with EGF. The overexpression of MEF2B increased the EGF-mediated induction of DDIAS expression, whereas the knockdown of MEF2B impaired this effect. Furthermore, DDIAS promoted invasion by increasing -catenin expression at the post-translational level in response to EGF, suggesting that DDIAS plays a crucial role in the metastasis of cancer cells by regulating -catenin expression. It is unlikely that MEF2B and NFATc1 cooperatively regulate DDIAS transcription in response to EGF. Collectively, EGF activates the ERK5/MEF2 pathway, which in turn induces DDIAS expression to promote cancer cell invasion by activating -catenin target genes.


PubMed | ST Pharm. Co., Korea Research Institute of Bioscience and Biotechnology and Korean University of Science and Technology
Type: | Journal: Data in brief | Year: 2016

The data included in this article are associated with the article entitled DNA-damage-induced apoptosis suppressor (DDIAS) is upregulated via ERK5/MEF2B signaling and promotes -catenin-mediated invasion (J.Y. Im, S.H. Yoon, B.K. Kim, H.S. Ban, K.J. Won, K.S. Chung, K.E. Jung, M. Won) [1]. Quantitative RT-PCR data revealed that genetic or pharmacological inhibition of extracellular signal-regulated kinase 5 (ERK5) suppresses DDIAS transcription in response to epidermal growth factor (EGF) in Hela cells. p300 did not interact with myocyte enhancer factor 2B (MEF2B), a downstream target of ERK5 and affect transcription of DDIAS. Moreover, DDIAS transcription is activated by ERK5/MEF2B signaling on EGF exposure in the non-small cell lung cancer cells (NSCLC) NCI-H1703 and NCI-H1299. DDIAS knockdown suppresses lung cancer cell invasion by decreasing -catenin protein level on EGF exposure.

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