• Proceedings of the PSK Conference
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• 2003.04a
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• pp.207.3-208
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• 2003

Peroxisome proliferator-activated receptor (PPAR), a member of the nuclear hormone receptor superfamily, is a transcription factor activated by specific natural or synthetic ligands. It is involved in various cellular processes including adipogenesis, inflammation, cell cycle progression and carcinogenesis. Here, we report the production and characterization of a PPARgamma subtype-specific monoclonal antibody P${\gamma}$ 48.34A, which was raised against full-length human PPARgamma protein. (omitted)

• KSBB Journal
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• v.5 no.4
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• pp.365-371
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• 1990

To improve the growth of mouse hybridoma 2c3.1 secreting anti-Hepatitis B surface antigen monoclonal antibody (anti-HBsAg MAb), we had constructed an enriched medium and observed the effects of fetal bovine serum and serum-free supplements including human serum albumin, 'insulin and transferrin', and monoethanolamine. For further enhancement of growth, the concentrations of two major energy sources, glucose and glutamine, were strengthened with various ratios in the enriched medium. Maximum cell growth and monoclonal antibody production obtained in various ratios of glucose/glutamine with an inoculation concentration of 2$\times$105 cells/ml were 0.73$\times$106-4.62$\times$106 cells/ml and 65.1-422.6 $\mu\textrm{g}$/ml, respectively. Glutamine was round to be a major energy source and a limiting nutrient in comparison to glucose for 2c3.1 cell cultivation in enriched media with low serum.

• Parasites, Hosts and Diseases
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• v.57 no.3
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• pp.283-290
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• 2019

A rapid diagnostic test (RDT) kit was developed to detect non-structural protein 1 (NS1) of yellow fever virus (YFV) using monoclonal antibody. NS1 protein was purified from the cultured YFV and used to immunize mice. Monoclonal antibody to NS1 was selected and conjugated with colloidal gold to produce the YFV NS1 RDT kit. The YFV RDTs were evaluated for sensitivity and specificity using positive and negative samples of monkeys from Brazil and negative human blood samples from Korea. Among monoclonal antibodies, clones 3A11 and 3B7 proved most sensitive, and used for YFV RDT kit. Diagnostic accuracy of YFV RDT was fairly high; Sensitivity was 0.0% and specificity was 100% against Dengue viruses type 2 and 3, Zika, Chikungunya and Mayaro viruses. This YFV RDT kit could be employed as a test of choice for point-of-care diagnosis and large scale surveys of YFV infection under clinical or field conditions in endemic areas and on the globe.

• Korean Journal of Veterinary Research
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• v.40 no.1
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• pp.81-85
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• 2000

Coxiella burnetii (C burnetii) is the causative agent of Q fever in animal and human. The distribution of the disease has been documented around world. In this study we developed the competitive enzyme linked immunosorbent assay(cELISA) and compared it with indirect immunofluorescent assay(IFA). A monoclonal antibody(Mab) against C burnetii and a peroxidase-conjugated anti-mouse IgM were used as an indicator system competing against antibody in animal serum or as an indicater of the absence of antibody. Sera were considered antibody positive when the percentage inhibition index(PI index) is upper than 30. PI index is calculated as 100-[sample OD/Mab OD)${\times}100$]. Among 162 bovine serum samples, 23 samples were antibody positive both in cELISA and IFA. And 156 samples showed same results. From goat with experimentally induced infection with C burnetii the antibody was detected 20 days early in cELISA compared to IFA. On the basis of present findings, it was demonstrated that cELISA is a reliable diagnostic method for The detection of specific antibodies against C burnetii infection.

• Proceedings of the Korean Society of Applied Pharmacology
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• 1998.11a
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• pp.198-198
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• 1998

Muc1 mucin is found in a variety of epithelial tissue and is overexpressed in several epithelial cancer. Recently it is alsol reported that primary Hamster tracheal surface epithelial(HTSE) cells express Muc1 protein and cDNA encoding HTSE muc1 protein has been cloned. Although numerous monoclonal antibodies (mAbs) to human muncins, particularly Muc1 have been produced, no such antibodies to murine Muc1 have been described. We now describe monoclonal antibody, called mAb M1CT, produced to C-terminal region of HTSE Muc1 protein by immunising mice with a glutathion-s-transferase linked fusion protein. In this study, using this antibody(mAb M1CT) we investigated the effect of RA on the expression of Muc1 in HTSE cells. Retinoic acid(RA) plays an essential role in maintaining normal differentiation of tracheal epithelial cells. With RA-deficiency tracheocytes undergo squamous metaplasia, an abnormal differentiation that can be reversed by RA. We had primary culture of HTSE cells under different concentrations of RA. Culture was maintained until the direction of differentiation was determined. Then Western blot analysis with mAb M1CT was performed with the cell lysates from the culture. The expression of Muc1 protein was decreased in dose-dependent manner as the concentration of retinoic acid was decreased. Our result indicates that the expression of Muc1 protein is coordinately regulated with airway mucous cell differentiation by RA pathway. And the antibody, mAb M1CT, produced in this study should provide useful tool to study the expression of Muc1 mucin in differentiation process or disease.

• IMMUNE NETWORK
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• v.1 no.1
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• pp.14-25
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• 2001

Background: Bone marrow stromal cells (BMSCs) express many cell surface molecules, which regulate the proliferation and differentiation of immune cells within the bone marrow. Methods: To identify cell surface molecules, which can regulate cell proliferation through cell interaction, monoclonal antibodies (MoAbs) against BMSCs were produced. Among them, 1H8 MoAb, which recognized distinctly an 80 kDa protein, abolished myeloma cell proliferation that was induced by co-culturing with BMSCs. Results: IL-6 gene expression was increased when myeloma or stromal cells were treated with 1H8 MoAb. In addition, the expression of IL-6 receptor and CD40 was up-regulated by 1H8 treatment, suggesting that the molecule recognized by 1H8 MoAb is involved in cell proliferation by modulating the expression of cell growth-related genes. Myeloma cells contain high levels of reactive oxygen species (ROS), which are related to gene expression and tumorigenesis. Treatment with 1H8 decreased the intracellular ROS level and increased PAG antioxidant gene concomitantly. Finally, 1H8 induced the tyrosine phosphorylation of several proteins in U266. Conclusion: Taken together, 1H8 MoAb recognized the cell surface molecule and triggered the intracellular signals, which led to modulate gene expression and cell proliferation.

• Biomolecules & Therapeutics
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• v.3 no.4
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• pp.245-250
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• 1995

The carbon tetrachloride($CCl_4$) has been demonstrated to have a hepatotoxic effect in human or many other species. To investigate the enzyme induction of mixed function oxygenases in liver of male Sprague-Dawley rats a single 0.1, 0.5 mι/kg dose of carbon tetrachloride were given. At 24 hr after a single dose of 0.1 mι CC1$_4$/kg weight, methanol extract of Hedera rhombea leaves was administered with 100, 500 mg/kg weight. Assays of 7-ethoxyresorufin-Ο-deethylation(EROD),7-benzyloxyresorufin-Ο-deathylation(BROD),4-nitro-phenol-UDP-glucuronosyltransferase(UDPGT), Western blot and RNA slot blot were used as representatives of the activities of cytochrome P-450 enzymes. The change of the activity of CYP1A1 form measured by EROD assay and Western analysis using 1-7-1 monoclonal antibody was not observed. The activity CYP2B1 form by BROD assay and using 2-66-3 monoclonal antibody was remarkably increased. Elevated level of CYP2B1 mRNA was shown by slot hybridization with 2B1-specific probe. Administration of methanol extract of Hedera rhombea leaves reversed the enzyme activity and the level of mRNA, which suggest the chemoprotective effect of methanol extracts of Hedera rhombea leaves to carbon tetrachloride hepatotoxlcity.

• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.361.2-361
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• 1998

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
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• 1996.10a
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• pp.263.2-263
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• 1996

No Abstract, See Full Text

• Journal of Microbiology and Biotechnology
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• v.12 no.6
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• pp.916-920
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• 2002

This report describes a high-level expression of human alpha-2a interferon ($IFN{\alpha}-2a$) in Escherichia coli and its pilot scale purification by using a monoclonal antibody-independent chromatographic procedure that is based on anion-exchange, cation-exchange, hydrophobic interaction, and gel filtration. The recombinant E. coli produced much more $IFN{\alpha}-2a$ in a soluble form, when cultivated at low temperatures than at high-temperature fermentation. However, if the bacterial growth was taken into consideration, fermentation at $30^{\circ}C$ seemed optimal for the interferon production. By using our new protocol, we recovered approximately 160 mg of $IFN{\alpha}-2a$ with a specific activity of $3.59{\times}10^8$ IU/mg from 201 of the broth. The gel permeation chromatographic and SDS-PAGE indicated that the interferon preparation was purified to homogeneity and was of the correctly folded fast-migrating monomer.