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Your search keyword '"Daigo, Kenji"' showing total 12 results
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12 results on '"Daigo, Kenji"'

4. Frequent Germline and Somatic Single Nucleotide Variants in the Promoter Region of the Ribosomal RNA Gene in Japanese Lung Adenocarcinoma Patients

Author

Ohashi, Riuko, primary, Umezu, Hajime, additional, Sato, Ayako, additional, Abé, Tatsuya, additional, Kondo, Shuhei, additional, Daigo, Kenji, additional, Sato, Seijiro, additional, Hara, Norikazu, additional, Miyashita, Akinori, additional, Ikeuchi, Takeshi, additional, Motoyama, Teiichi, additional, Kishi, Masashi, additional, Nagaoka, Tadahiro, additional, Horiuchi, Keiko, additional, Shiga, Atsushi, additional, Okuda, Shujiro, additional, Sekiya, Tomoki, additional, Ohtsubo, Aya, additional, Ichikawa, Kosuke, additional, Kagamu, Hiroshi, additional, Kikuchi, Toshiaki, additional, Watanabe, Satoshi, additional, Tanuma, Jun-Ichi, additional, Schraml, Peter, additional, Hamakubo, Takao, additional, Tsuchida, Masanori, additional, and Ajioka, Yoichi, additional

Published
2020
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5. Lineage-Specific Epigenomic and Genomic Activation of Oncogene HNF4A Promotes Gastrointestinal Adenocarcinomas

Author

Pan, Jian, primary, Silva, Tiago C., additional, Gull, Nicole, additional, Yang, Qian, additional, Plummer, Jasmine T., additional, Chen, Stephanie, additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Gery, Sigal, additional, Ding, Ling-Wen, additional, Jiang, Yan-Yi, additional, Hu, Shaoyan, additional, Xu, Li-Yan, additional, Li, En-Min, additional, Ding, Yanbing, additional, Klempner, Samuel J., additional, Gayther, Simon A., additional, Berman, Benjamin P., additional, Koeffler, H. Phillip, additional, and Lin, De-Chen, additional

Published
2020
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6. Lineage-Specific Epigenomic and Genomic Activation of the Oncogene HNF4A Promotes Gastrointestinal Adenocarcinomas

Author

Pan, Jian, primary, Silva, Tiago C., additional, Gull, Nicole, additional, Yang, Qian, additional, Plummer, Jasmine, additional, Chen, Stephanie, additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Gery, Sigal, additional, Ding, Ling-Wen, additional, Jiang, Yan-Yi, additional, Hu, Shao-Yan, additional, Xu, Li-Yan, additional, Li, En-Min, additional, Ding, Yanbing, additional, Klempner, Samuel J., additional, Berman, Benjamin P., additional, Phillip Koeffler, H., additional, and Lin, De-Chen, additional

Published
2019
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11. Factor H–Related Protein 5 Interacts with Pentraxin 3 and the Extracellular Matrix and Modulates Complement Activation

Author

Csincsi, Ádám I., primary, Kopp, Anne, additional, Zöldi, Miklós, additional, Bánlaki, Zsófia, additional, Uzonyi, Barbara, additional, Hebecker, Mario, additional, Caesar, Joseph J. E., additional, Pickering, Matthew C., additional, Daigo, Kenji, additional, Hamakubo, Takao, additional, Lea, Susan M., additional, Goicoechea de Jorge, Elena, additional, and Józsi, Mihály, additional

Published
2015
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12. Expression and Purification of Full-Length and Domain-Fragment Recombinant Pentraxin 3 (PTX3) Proteins from Mammalian and Bacterial Cells.

Author

Daigo K and Hamakubo T

Subjects
Animals, Arginine chemistry, Buffers, C-Reactive Protein metabolism, CHO Cells, Cricetulus, Escherichia coli genetics, Humans, Protein Domains, Serum Amyloid P-Component metabolism, C-Reactive Protein genetics, Escherichia coli growth & development, Protein Engineering methods, Recombinant Proteins isolation & purification, Serum Amyloid P-Component genetics
Abstract

Although cell-based protein expression systems enable us a certain amount of protein suitable for subsequent biological experiments to be obtained, aggregates of the protein of interest are sometimes encountered during the purification procedure. Pentraxin 3 (PTX3), a member of the pentraxin family that is classified as a carbohydrate-binding protein based on its structure, comprises one of the humoral arms of the pattern recognition receptors that play an important role in the innate immune response. PTX3 comprises two domains; an N-terminal domain and a C-terminal domain. The C-terminal domain containing pentraxin signature has similar biological functions as other pentraxins such as C-reactive protein (CRP) and serum amyloid-P component (SAP). On the other side, the N-terminal domain is specific to PTX3. A supply of the PTX3 protein in full length or partial fragments is thus essential for the elucidation of its biological functions. Here we describe the expression and purification of recombinant PTX3. An arginine-containing buffer is essential for the elution of bacterially expressed PTX3 N-terminal domain to minimize aggregation. This method allows high-yield purification of full-length or domain-fragment recombinant PTX3 proteins for biological study.

Published
2020
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