A new epitope tag from hepatitis B virus preS1 for immunodetection, localization and affinity purification of recombinant proteins

Oh, Mee Sook; Kim, Keun Soo; Jang, Young Kug; Maeng, Cheol Young; Min, Soon; Jang, Myeong Hee; Yoon, Sun Woo; Kim, Jung Hee; Hong, Hyo Jeong

doi:10.1016/j.jim.2003.08.010

Cited by 13 publications

(11 citation statements)

References 18 publications

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“…The DNA encoding PA was prepared by digestion of pT7-PA (kindly provided by W. K. Seong at the Korea Center for Disease Control and Prevention) with BamHI and SalI and was ligated into the BamHI-SalI sites of pBS1-1 (Aprogen, Korea), which contains an S1 tag at the 5Ј end of the fused gene (16), to construct pBS1-1-PA. The DNA encoding LF was synthesized by PCR from pXO1 DNA (kindly provided by W. K. Seong.…”

Section: Methodsmentioning

confidence: 99%

An Anthrax Lethal Factor-Neutralizing Monoclonal Antibody Protects Rats before and after Challenge with Anthrax Toxin

Lim

Kim

et al. 2005

Infect Immun

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Lethal factor (LF) is a component of anthrax lethal toxin (LeTx).was approximately one-third that of 3C16C3 (0.63 g/ml) in the in vitro LeTx-neutralization assay. The 5B13B1 antibody, which had the highest neutralizing activity, provided perfect protection against LeTx challenge in an in vivo LeTx neutralization assay using Fisher 344 rats. In addition, the antibody showed pre-and postexposure prophylactic effects in the animal experiments. This is the first report that an MAb binding to domain III of LF has neutralizing activity against LeTx. The 5B13B1 antibody may be useful in prophylaxis against anthrax poisoning.

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Section: Methodsmentioning

confidence: 99%

An Anthrax Lethal Factor-Neutralizing Monoclonal Antibody Protects Rats before and after Challenge with Anthrax Toxin

Lim

Kim

et al. 2005

Infect Immun

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“…9. These spectra exhibited two negative bands at 208 and 222 nm, characteristic of a predominantly a-helical structure of BSA [24]. With the increase in OB concentration, band intensity of curves (a-c) decreased regularly.…”

Section: Spectramentioning

confidence: 98%

The investigation of the interaction between oxybutynin hydrochloride and bovine serum albumin by spectroscopic methods

Guo

Jing

Guo

et al. 2010

Journal of Luminescence

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“…(15,18) The PCR product was subcloned into the EcoRV-XhoI sites of pMS2-1 (Aprogen, Daejon, South Korea) to construct the hTPO expression plasmid pMS2-1-TPO. A plasmid expressing mGM-CSF and mIL-4 was constructed using pdCMV-dhfr (Aprogen), (18) a plasmid designed for antibody production in mammalian cells that contains two multiple cloning sites for protein expression. Coding sequences for mIL-4 and mGM-CSF (Cytokine Bank, Jeonju, Korea) were inserted into the EcoRI-NotI and HindIII-XbaI sites of pdCMVdhfr, respectively.…”

Section: Plasmid Constructionmentioning

confidence: 99%

“…The ability of the constructed pMS2-1-TPO plasmid to mediate expression of hTPO was confirmed by transient expression in COS-7 cells as described previously. (18) …”

Section: Plasmid Constructionmentioning

confidence: 99%

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Monoclonal Anti-Thrombopoietin Antibodies Generated by Genetic Immunization

Lim

Kim²,

Kim³

et al. 2006

Hybridoma

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Thrombopoietin (TPO) is a megakaryocyte growth and differentiation factor that is currently being investigated as a therapeutic for cancer patients undergoing myelosuppressive chemotherapy. We generated monoclonal antibodies (MAbs) specific for human thrombopoietin (hTPO) by genetic immunization using an hTPO expression plasmid and an adjuvant plasmid that encodes mouse granulocyte-macrophage colony-stimulating factor (GM-CSF) and interleukin-4 (IL-4). All genetically immunized mice exhibited a high humoral immune response. Splenocytes from these mice were used to generate hybridomas. Two MAbs, designated 2B9A10 and 4C16B15 (of IgG1 and IgG3 isotypes, respectively), were subsequently selected and produced. They specifically recognized and precipitated recombinant hTPO produced by mammalian cells and were effective in sandwich enzyme-linked immunosorbent assays (ELISAs) for hTPO quantitation. Our results demonstrate that these MAbs should be useful for purification and quantitation of hTPO in clinical and laboratory settings.

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A new epitope tag from hepatitis B virus preS1 for immunodetection, localization and affinity purification of recombinant proteins

Cited by 13 publications

References 18 publications

An Anthrax Lethal Factor-Neutralizing Monoclonal Antibody Protects Rats before and after Challenge with Anthrax Toxin

An Anthrax Lethal Factor-Neutralizing Monoclonal Antibody Protects Rats before and after Challenge with Anthrax Toxin

The investigation of the interaction between oxybutynin hydrochloride and bovine serum albumin by spectroscopic methods

Monoclonal Anti-Thrombopoietin Antibodies Generated by Genetic Immunization

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