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Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase.

Biotechnology and bioengineering

Hartman J, Daram P, Frizzell RA, Rado T, Benos DJ, Sorscher EJ.
PMID: 18601017
Biotechnol Bioeng. 1992 Apr 05;39(8):828-32. doi: 10.1002/bit.260390805.

Prokaryotic expression of polypeptides as fusion proteins with glutathione-S-transferase has recently been reported as a one-step means of purifying recombinant protein. The usefulness of the glutathione-S-transferase/glutathione-agarose system, however, is significantly limited by the frequent synthesis of recombinant proteins in...

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Hartman J, Daram P, Frizzell RA, et al. Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase. Biotechnol Bioeng. 1992;39(8):828-32doi: 10.1002/bit.260390805.
Hartman, J., Daram, P., Frizzell, R. A., Rado, T., Benos, D. J., & Sorscher, E. J. (1992). Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase. Biotechnology and bioengineering, 39(8), 828-32. https://doi.org/10.1002/bit.260390805
Hartman, J, et al. "Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase." Biotechnology and bioengineering vol. 39,8 (1992): 828-32. doi: https://doi.org/10.1002/bit.260390805
Hartman J, Daram P, Frizzell RA, Rado T, Benos DJ, Sorscher EJ. Affinity purification of insoluble recombinant fusion proteins containing glutathione-S-transferase. Biotechnol Bioeng. 1992 Apr 05;39(8):828-32. doi: 10.1002/bit.260390805. PMID: 18601017.
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CD123 as a Biomarker in Hematolymphoid Malignancies: Principles of Detection and Targeted Therapies.

Cancers

El Achi H, Dupont E, Paul S, Khoury JD.
PMID: 33113953
Cancers (Basel). 2020 Oct 23;12(11). doi: 10.3390/cancers12113087.

CD123, the α chain of the interleukin 3 receptor, is a cytokine receptor that is overexpressed in multiple hematolymphoid neoplasms, including acute myeloid leukemia, blastic plasmacytoid dendritic cell neoplasm, acute lymphoblastic leukemia, hairy cell leukemia, and systemic mastocytosis. Importantly,...

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El Achi H, Dupont E, Paul S, et al. CD123 as a Biomarker in Hematolymphoid Malignancies: Principles of Detection and Targeted Therapies. Cancers (Basel). 2020;12(11)doi: 10.3390/cancers12113087.
El Achi, H., Dupont, E., Paul, S., & Khoury, J. D. (2020). CD123 as a Biomarker in Hematolymphoid Malignancies: Principles of Detection and Targeted Therapies. Cancers, 12(11), . https://doi.org/10.3390/cancers12113087
El Achi, Hanadi, et al. "CD123 as a Biomarker in Hematolymphoid Malignancies: Principles of Detection and Targeted Therapies." Cancers vol. 12,11 (2020). doi: https://doi.org/10.3390/cancers12113087
El Achi H, Dupont E, Paul S, Khoury JD. CD123 as a Biomarker in Hematolymphoid Malignancies: Principles of Detection and Targeted Therapies. Cancers (Basel). 2020 Oct 23;12(11). doi: 10.3390/cancers12113087. PMID: 33113953; PMCID: PMC7690688.
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Human granulocyte-colony stimulating factor (G-CSF)/stem cell factor (SCF) fusion proteins: design, characterization and activity.

PeerJ

Mickiene G, Dalgėdienė I, Zvirblis G, Dapkunas Z, Plikusiene I, Buzavaite-Verteliene E, Balevičius Z, Rukšėnaitė A, Pleckaityte M.
PMID: 32884863
PeerJ. 2020 Aug 21;8:e9788. doi: 10.7717/peerj.9788. eCollection 2020.

BACKGROUND: Stem cell factor (SCF) and granulocyte-colony stimulating factor (G-CSF) are well-characterized vital hematopoietic growth factors that regulate hematopoiesis. G-CSF and SCF synergistically exhibit a stimulatory effect on hematopoietic progenitors. The combination of G-CSF and SCF has been used...

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Mickiene G, Dalgėdienė I, Zvirblis G, et al. Human granulocyte-colony stimulating factor (G-CSF)/stem cell factor (SCF) fusion proteins: design, characterization and activity. PeerJ. 2020;8:e9788doi: 10.7717/peerj.9788.
Mickiene, G., Dalgėdienė, I., Zvirblis, G., Dapkunas, Z., Plikusiene, I., Buzavaite-Verteliene, E., Balevičius, Z., Rukšėnaitė, A., & Pleckaityte, M. (2020). Human granulocyte-colony stimulating factor (G-CSF)/stem cell factor (SCF) fusion proteins: design, characterization and activity. PeerJ, 8e9788. https://doi.org/10.7717/peerj.9788
Mickiene, Gitana, et al. "Human granulocyte-colony stimulating factor (G-CSF)/stem cell factor (SCF) fusion proteins: design, characterization and activity." PeerJ vol. 8 (2020): e9788. doi: https://doi.org/10.7717/peerj.9788
Mickiene G, Dalgėdienė I, Zvirblis G, Dapkunas Z, Plikusiene I, Buzavaite-Verteliene E, Balevičius Z, Rukšėnaitė A, Pleckaityte M. Human granulocyte-colony stimulating factor (G-CSF)/stem cell factor (SCF) fusion proteins: design, characterization and activity. PeerJ. 2020 Aug 21;8:e9788. doi: 10.7717/peerj.9788. eCollection 2020. PMID: 32884863; PMCID: PMC7444511.
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A validated, sensitive electrophoretic method for the detection of activin receptor type II-Fc fusion proteins in human blood.

Drug testing and analysis

Martin L, Zouhiri N, Audran M, Marchand A.
PMID: 29499588
Drug Test Anal. 2018 Mar 02; doi: 10.1002/dta.2376. Epub 2018 Mar 02.

New therapeutic proteins that trap circulating members of the transforming growth factor (TGF) beta superfamily (activins and growth differentiation factors) show promising effects on erythropoiesis and muscular growth. They are dimeric recombinant fusion proteins composed of the extracellular domain...

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Martin L, Zouhiri N, Audran M, et al. A validated, sensitive electrophoretic method for the detection of activin receptor type II-Fc fusion proteins in human blood. Drug Test Anal. 2018;doi: 10.1002/dta.2376.
Martin, L., Zouhiri, N., Audran, M., & Marchand, A. (2018). A validated, sensitive electrophoretic method for the detection of activin receptor type II-Fc fusion proteins in human blood. Drug testing and analysis, . https://doi.org/10.1002/dta.2376
Martin, L, et al. "A validated, sensitive electrophoretic method for the detection of activin receptor type II-Fc fusion proteins in human blood." Drug testing and analysis vol. (2018). doi: https://doi.org/10.1002/dta.2376
Martin L, Zouhiri N, Audran M, Marchand A. A validated, sensitive electrophoretic method for the detection of activin receptor type II-Fc fusion proteins in human blood. Drug Test Anal. 2018 Mar 02; doi: 10.1002/dta.2376. Epub 2018 Mar 02. PMID: 29499588.
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Reprint of: A new tagged-TEV protease: Construction, optimisation of production, purification and test activity.

Protein expression and purification

Miladi B, Bouallagui H, Dridi C, El Marjou A, Boeuf G, Di Martino P, Dufour F, Elm'selmi A.
PMID: 21889987
Protein Expr Purif. 2011 Sep 02; doi: 10.1016/j.pep.2011.08.018. Epub 2011 Sep 02.

The Tobacco Etch Virus (TEV) protease is frequently used in the cleavage of recombinant fusion proteins because of its efficiency and high specificity. In this work, we present a new recombinant form of TEV termed Streptag II-TEV for high-level...

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Miladi B, Bouallagui H, Dridi C, et al. Reprint of: A new tagged-TEV protease: Construction, optimisation of production, purification and test activity. Protein Expr Purif. 2011;doi: 10.1016/j.pep.2011.08.018.
Miladi, B., Bouallagui, H., Dridi, C., El Marjou, A., Boeuf, G., Di Martino, P., Dufour, F., & Elm'selmi, A. (2011). Reprint of: A new tagged-TEV protease: Construction, optimisation of production, purification and test activity. Protein expression and purification, . https://doi.org/10.1016/j.pep.2011.08.018
Miladi, Baligh, et al. "Reprint of: A new tagged-TEV protease: Construction, optimisation of production, purification and test activity." Protein expression and purification vol. (2011). doi: https://doi.org/10.1016/j.pep.2011.08.018
Miladi B, Bouallagui H, Dridi C, El Marjou A, Boeuf G, Di Martino P, Dufour F, Elm'selmi A. Reprint of: A new tagged-TEV protease: Construction, optimisation of production, purification and test activity. Protein Expr Purif. 2011 Sep 02; doi: 10.1016/j.pep.2011.08.018. Epub 2011 Sep 02. PMID: 21889987.
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Eradication of c-erbB-2-Positive Ovarian Cancer Cells Mediated by Intracellular Expression of Anti-c-erbB-2 Antibody.

Methods in molecular medicine

Deshane J, Alvarez RD, Siegal GP.
PMID: 21340837
Methods Mol Med. 2001;39:757-68. doi: 10.1385/1-59259-071-3:757.

Overexpression of erbB-2 is important in the pathogenesis of a variety of human neoplasms. Overexpression of the erbB-2 gene product has been associated with poor clinical prognosis with respect to malignancies originating in the ovary, breast, gastrointestinal tract, salivary...

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Deshane J, Alvarez RD, Siegal GP. Eradication of c-erbB-2-Positive Ovarian Cancer Cells Mediated by Intracellular Expression of Anti-c-erbB-2 Antibody. Methods Mol Med. 2001;39:757-68doi: 10.1385/1-59259-071-3:757.
Deshane, J., Alvarez, R. D., & Siegal, G. P. (2001). Eradication of c-erbB-2-Positive Ovarian Cancer Cells Mediated by Intracellular Expression of Anti-c-erbB-2 Antibody. Methods in molecular medicine, 39757-68. https://doi.org/10.1385/1-59259-071-3:757
Deshane, J, et al. "Eradication of c-erbB-2-Positive Ovarian Cancer Cells Mediated by Intracellular Expression of Anti-c-erbB-2 Antibody." Methods in molecular medicine vol. 39 (2001): 757-68. doi: https://doi.org/10.1385/1-59259-071-3:757
Deshane J, Alvarez RD, Siegal GP. Eradication of c-erbB-2-Positive Ovarian Cancer Cells Mediated by Intracellular Expression of Anti-c-erbB-2 Antibody. Methods Mol Med. 2001;39:757-68. doi: 10.1385/1-59259-071-3:757. PMID: 21340837.
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Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein.

Frontiers in microbiology

Kim D, Kim J, Park S, Kim M, Baek K, Kang M, Choi JK, Maharjan S, Akauliya M, Lee Y, Kwon HJ.
PMID: 34950112
Front Microbiol. 2021 Dec 07;12:726231. doi: 10.3389/fmicb.2021.726231. eCollection 2021.

SARS-CoV-2 infections continue to spread quickly by human-to-human transmission around the world. Therefore, developing methods to rapidly detect SARS-CoV-2 with high sensitivity are still urgently needed. We produced a monoclonal antibody that specifically detects the N protein of SARS-CoV-2...

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Kim D, Kim J, Park S, et al. Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Front Microbiol. 2021;12:726231doi: 10.3389/fmicb.2021.726231.
Kim, D., Kim, J., Park, S., Kim, M., Baek, K., Kang, M., Choi, J. K., Maharjan, S., Akauliya, M., Lee, Y., & Kwon, H. J. (2021). Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Frontiers in microbiology, 12726231. https://doi.org/10.3389/fmicb.2021.726231
Kim, Dongbum, et al. "Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein." Frontiers in microbiology vol. 12 (2021): 726231. doi: https://doi.org/10.3389/fmicb.2021.726231
Kim D, Kim J, Park S, Kim M, Baek K, Kang M, Choi JK, Maharjan S, Akauliya M, Lee Y, Kwon HJ. Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Front Microbiol. 2021 Dec 07;12:726231. doi: 10.3389/fmicb.2021.726231. eCollection 2021. PMID: 34950112; PMCID: PMC8688357.
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Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein.

Frontiers in microbiology

Kim D, Kim J, Park S, Kim M, Baek K, Kang M, Choi JK, Maharjan S, Akauliya M, Lee Y, Kwon HJ.
PMID: 34950112
Front Microbiol. 2021 Dec 07;12:726231. doi: 10.3389/fmicb.2021.726231. eCollection 2021.

SARS-CoV-2 infections continue to spread quickly by human-to-human transmission around the world. Therefore, developing methods to rapidly detect SARS-CoV-2 with high sensitivity are still urgently needed. We produced a monoclonal antibody that specifically detects the N protein of SARS-CoV-2...

Cite
Kim D, Kim J, Park S, et al. Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Front Microbiol. 2021;12:726231doi: 10.3389/fmicb.2021.726231.
Kim, D., Kim, J., Park, S., Kim, M., Baek, K., Kang, M., Choi, J. K., Maharjan, S., Akauliya, M., Lee, Y., & Kwon, H. J. (2021). Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Frontiers in microbiology, 12726231. https://doi.org/10.3389/fmicb.2021.726231
Kim, Dongbum, et al. "Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein." Frontiers in microbiology vol. 12 (2021): 726231. doi: https://doi.org/10.3389/fmicb.2021.726231
Kim D, Kim J, Park S, Kim M, Baek K, Kang M, Choi JK, Maharjan S, Akauliya M, Lee Y, Kwon HJ. Production of SARS-CoV-2 N Protein-Specific Monoclonal Antibody and Its Application in an ELISA-Based Detection System and Targeting the Interaction Between the Spike C-Terminal Domain and N Protein. Front Microbiol. 2021 Dec 07;12:726231. doi: 10.3389/fmicb.2021.726231. eCollection 2021. PMID: 34950112; PMCID: PMC8688357.
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PTD-mediated delivery of α-globin chain into Κ-562 erythroleukemia cells and α-thalassemic (HBH) patients' RBCs ex vivo in the frame of Protein Replacement Therapy.

Journal of biological research (Thessalonike, Greece)

Miliotou AN, Papagiannopoulou D, Vlachaki E, Samiotaki M, Laspa D, Theodoridou S, Tsiftsoglou AS, Papadopoulou LC.
PMID: 34284828
J Biol Res (Thessalon). 2021 Jul 20;28(1):16. doi: 10.1186/s40709-021-00148-3.

BACKGROUND: α-Thalassemia, a congenital hemoglobinopathy, is characterized by deficiency and/or reduced levels of α-globin chains in serious forms of α-thalassemia (HbH disease/Hb Bart's). This research work deals with a Protein Replacement Therapy approach in order to manage α-thalassemia manifestations,...

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Miliotou AN, Papagiannopoulou D, Vlachaki E, et al. PTD-mediated delivery of α-globin chain into Κ-562 erythroleukemia cells and α-thalassemic (HBH) patients' RBCs ex vivo in the frame of Protein Replacement Therapy. J Biol Res (Thessalon). 2021;28(1):16doi: 10.1186/s40709-021-00148-3.
Miliotou, A. N., Papagiannopoulou, D., Vlachaki, E., Samiotaki, M., Laspa, D., Theodoridou, S., Tsiftsoglou, A. S., & Papadopoulou, L. C. (2021). PTD-mediated delivery of α-globin chain into Κ-562 erythroleukemia cells and α-thalassemic (HBH) patients' RBCs ex vivo in the frame of Protein Replacement Therapy. Journal of biological research (Thessalonike, Greece), 28(1), 16. https://doi.org/10.1186/s40709-021-00148-3
Miliotou, Androulla N, et al. "PTD-mediated delivery of α-globin chain into Κ-562 erythroleukemia cells and α-thalassemic (HBH) patients' RBCs ex vivo in the frame of Protein Replacement Therapy." Journal of biological research (Thessalonike, Greece) vol. 28,1 (2021): 16. doi: https://doi.org/10.1186/s40709-021-00148-3
Miliotou AN, Papagiannopoulou D, Vlachaki E, Samiotaki M, Laspa D, Theodoridou S, Tsiftsoglou AS, Papadopoulou LC. PTD-mediated delivery of α-globin chain into Κ-562 erythroleukemia cells and α-thalassemic (HBH) patients' RBCs ex vivo in the frame of Protein Replacement Therapy. J Biol Res (Thessalon). 2021 Jul 20;28(1):16. doi: 10.1186/s40709-021-00148-3. PMID: 34284828; PMCID: PMC8290593.
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Analysis insights for three FRET pairs of chemically unlinked two-molecule FRET cytometry.

Cytometry. Part A : the journal of the International Society for Analytical Cytology

Ni Z, Gale A, Johnson MS, Sedger LM.
PMID: 34935263
Cytometry A. 2021 Dec 21; doi: 10.1002/cyto.a.24527. Epub 2021 Dec 21.

Förster resonance energy transfer (FRET) is the direct energy exchange between two-component fluorescent molecules. FRET methods utilize chemically linked molecules or unlinked fluorescence protein-protein interactions. FRET is therefore a powerful indicator of molecular proximity, but standardized determination of FRET...

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Ni Z, Gale A, Johnson MS, et al. Analysis insights for three FRET pairs of chemically unlinked two-molecule FRET cytometry. Cytometry A. 2021;doi: 10.1002/cyto.a.24527.
Ni, Z., Gale, A., Johnson, M. S., & Sedger, L. M. (2021). Analysis insights for three FRET pairs of chemically unlinked two-molecule FRET cytometry. Cytometry. Part A : the journal of the International Society for Analytical Cytology, . https://doi.org/10.1002/cyto.a.24527
Ni, Zhongran, et al. "Analysis insights for three FRET pairs of chemically unlinked two-molecule FRET cytometry." Cytometry. Part A : the journal of the International Society for Analytical Cytology vol. (2021). doi: https://doi.org/10.1002/cyto.a.24527
Ni Z, Gale A, Johnson MS, Sedger LM. Analysis insights for three FRET pairs of chemically unlinked two-molecule FRET cytometry. Cytometry A. 2021 Dec 21; doi: 10.1002/cyto.a.24527. Epub 2021 Dec 21. PMID: 34935263.
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Analysis of two major anti-M2 antibodies (anti-PDC-E2/anti-BCOADC-E2) in primary biliary cirrhosis: relationship to titers of immunofluorescent anti-mitochondrial antibody.

Hepatology research : the official journal of the Japan Society of Hepatology

Miyakawa H, Kitazawa E, Fujikawa H, Kikuchi K, Abe K, Kawaguchi N, Kako M.
PMID: 10838031
Hepatol Res. 2000 Jul;18(1):1-9. doi: 10.1016/s1386-6346(99)00079-0.

To analyze anti-M2 components in primary biliary cirrhosis (PBC) we measured two major anti-M2 antibodies (anti-PDC-E2 and anti-BCOADC-E2) by immunoblotting and ELISA, and compared the results between 38 immunofluorescent anti-mitochondrial antibody (AMA)-negative PBC patients (group A) and 39 strongly...

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Miyakawa H, Kitazawa E, Fujikawa H, et al. Analysis of two major anti-M2 antibodies (anti-PDC-E2/anti-BCOADC-E2) in primary biliary cirrhosis: relationship to titers of immunofluorescent anti-mitochondrial antibody. Hepatol Res. 2000;18(1):1-9doi: 10.1016/s1386-6346(99)00079-0.
Miyakawa, H., Kitazawa, E., Fujikawa, H., Kikuchi, K., Abe, K., Kawaguchi, N., & Kako, M. (2000). Analysis of two major anti-M2 antibodies (anti-PDC-E2/anti-BCOADC-E2) in primary biliary cirrhosis: relationship to titers of immunofluorescent anti-mitochondrial antibody. Hepatology research : the official journal of the Japan Society of Hepatology, 18(1), 1-9. https://doi.org/10.1016/s1386-6346(99)00079-0
Miyakawa, et al. "Analysis of two major anti-M2 antibodies (anti-PDC-E2/anti-BCOADC-E2) in primary biliary cirrhosis: relationship to titers of immunofluorescent anti-mitochondrial antibody." Hepatology research : the official journal of the Japan Society of Hepatology vol. 18,1 (2000): 1-9. doi: https://doi.org/10.1016/s1386-6346(99)00079-0
Miyakawa H, Kitazawa E, Fujikawa H, Kikuchi K, Abe K, Kawaguchi N, Kako M. Analysis of two major anti-M2 antibodies (anti-PDC-E2/anti-BCOADC-E2) in primary biliary cirrhosis: relationship to titers of immunofluorescent anti-mitochondrial antibody. Hepatol Res. 2000 Jul;18(1):1-9. doi: 10.1016/s1386-6346(99)00079-0. PMID: 10838031.
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Application of TEV Protease in Protein Production.

Methods in molecular medicine

Polayes DA, Parks TD, Johnston SA, Dougherty WG.
PMID: 21390844
Methods Mol Med. 1998;13:169-83. doi: 10.1385/0-89603-485-2:169.

In many cases, the analysis of a specific protein is impeded by the inability to purify large amounts of it from a native source. Proteins of interest may be present in minute quantities and/or purification may be plagued with...

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Polayes DA, Parks TD, Johnston SA, et al. Application of TEV Protease in Protein Production. Methods Mol Med. 1998;13:169-83doi: 10.1385/0-89603-485-2:169.
Polayes, D. A., Parks, T. D., Johnston, S. A., & Dougherty, W. G. (1998). Application of TEV Protease in Protein Production. Methods in molecular medicine, 13169-83. https://doi.org/10.1385/0-89603-485-2:169
Polayes, D A, et al. "Application of TEV Protease in Protein Production." Methods in molecular medicine vol. 13 (1998): 169-83. doi: https://doi.org/10.1385/0-89603-485-2:169
Polayes DA, Parks TD, Johnston SA, Dougherty WG. Application of TEV Protease in Protein Production. Methods Mol Med. 1998;13:169-83. doi: 10.1385/0-89603-485-2:169. PMID: 21390844.
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