这是一篇来自已证抗体库的有关
人类 SUMO2的综述,是根据14篇发表使用所有方法的文章归纳的。这综述旨在帮助来邦网的访客找到最适合SUMO2 抗体。
SUMO2 同义词: HSMT3; SMT3B; SMT3H2; SUMO3; Smt3A
艾博抗(上海)贸易有限公司
domestic rabbit 多克隆 | | 艾博抗(上海)贸易有限公司 SUMO2抗体(Abcam, ab233222)被用于被用于免疫印迹在人类样本上 (图 4d). J Clin Invest (2022) ncbi |
domestic rabbit 单克隆(EPR4602) | | 艾博抗(上海)贸易有限公司 SUMO2抗体(Abcam, EPR4602)被用于被用于免疫印迹在人类样本上 (图 1a). PLoS Pathog (2019) ncbi |
domestic rabbit 多克隆 | | 艾博抗(上海)贸易有限公司 SUMO2抗体(Abcam, ab233222)被用于被用于免疫印迹在人类样本上 (图 1a). PLoS ONE (2019) ncbi |
domestic rabbit 单克隆(EPR4602) | - 免疫组化-石蜡切片; 大鼠; 1:100; 图 2a
- 免疫印迹; 大鼠; 1:3000; 图 6c
| 艾博抗(上海)贸易有限公司 SUMO2抗体(Abcam, ab109005)被用于被用于免疫组化-石蜡切片在大鼠样本上浓度为1:100 (图 2a) 和 被用于免疫印迹在大鼠样本上浓度为1:3000 (图 6c). Biosci Rep (2018) ncbi |
domestic rabbit 单克隆(EPR4602) | - 免疫组化; 人类; 图 5b
- 免疫印迹; 人类; 1:1000; 图 2c
| 艾博抗(上海)贸易有限公司 SUMO2抗体(AbCam, EPR4602)被用于被用于免疫组化在人类样本上 (图 5b) 和 被用于免疫印迹在人类样本上浓度为1:1000 (图 2c). Oncotarget (2017) ncbi |
domestic rabbit 多克隆 | | 艾博抗(上海)贸易有限公司 SUMO2抗体(Abcam, Ab22654)被用于被用于免疫印迹在人类样本上 (图 3). Methods Mol Biol (2017) ncbi |
MBL International
单克隆(10000000) | | MBL International SUMO2抗体(MBL international, M114-3)被用于被用于免疫印迹在人类样本上 (图 4a). Cell Chem Biol (2019) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL, 1E7)被用于被用于免疫印迹在人类样本上 (图 2a, 3a). Toxicol Appl Pharmacol (2018) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL, 1E7)被用于被用于免疫细胞化学在小鼠样本上 (图 4a). PLoS Pathog (2016) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL, M114-3)被用于被用于免疫印迹在人类样本上浓度为1:500 (图 1). Nat Commun (2016) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL, M114-3)被用于被用于免疫印迹在人类样本上浓度为1:500 (图 4a). Nat Commun (2015) ncbi |
单克隆(10000000) | - 免疫沉淀; 人类; 图 1a
- 免疫印迹; 人类; 图 1a
| MBL International SUMO2抗体(MBL, M114-3)被用于被用于免疫沉淀在人类样本上 (图 1a) 和 被用于免疫印迹在人类样本上 (图 1a). Genome Biol (2015) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL, 114-3)被用于被用于ChIP-Seq在人类样本上 (图 7). Nucleic Acids Res (2015) ncbi |
单克隆(10000000) | | MBL International SUMO2抗体(MBL International Corporation, M114-3)被用于被用于免疫印迹在人类样本上. Nucleic Acids Res (2014) ncbi |
Luo Y, Li Z, Kong Y, He W, Zheng H, An M,
et al. KRAS mutant-driven SUMOylation controls extracellular vesicle transmission to trigger lymphangiogenesis in pancreatic cancer. J Clin Invest. 2022;132:
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Ding L, Zhu Q, Zhou F, Tan H, Xu W, Pan C,
et al. Identification of viral SIM-SUMO2-interaction inhibitors for treating primary effusion lymphoma. PLoS Pathog. 2019;15:e1008174
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Bentz G, Lowrey A, Horne D, Nguyen V, Satterfield A, Ross T,
et al. Using glycyrrhizic acid to target sumoylation processes during Epstein-Barr virus latency. PLoS ONE. 2019;14:e0217578
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LI Y, Du L, Wang J, Vega R, Lee T, Miao Y,
et al. Allosteric Inhibition of Ubiquitin-like Modifications by a Class of Inhibitor of SUMO-Activating Enzyme. Cell Chem Biol. 2019;26:278-288.e6
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Hirano S, Udagawa O, Kobayashi Y, Kato A. Solubility changes of promyelocytic leukemia (PML) and SUMO monomers and dynamics of PML nuclear body proteins in arsenite-treated cells. Toxicol Appl Pharmacol. 2018;360:150-159
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Jin L, Lu J, Gao J. Silencing SUMO2 promotes protection against degradation and apoptosis of nucleus pulposus cells through p53 signaling pathway in intervertebral disc degeneration. Biosci Rep. 2018;38:
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Sallais J, Alahari S, Tagliaferro A, Bhattacharjee J, Post M, Caniggia I. Factor inhibiting HIF1-A novel target of SUMOylation in the human placenta. Oncotarget. 2017;8:114002-114018
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Citro S, Chiocca S. Assessing the Role of Paralog-Specific Sumoylation of HDAC1. Methods Mol Biol. 2017;1510:329-337
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Maroui M, Callé A, Cohen C, Streichenberger N, Texier P, Takissian J,
et al. Latency Entry of Herpes Simplex Virus 1 Is Determined by the Interaction of Its Genome with the Nuclear Environment. PLoS Pathog. 2016;12:e1005834
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Du L, LI Y, Fakih M, Wiatrek R, Duldulao M, Chen Z,
et al. Role of SUMO activating enzyme in cancer stem cell maintenance and self-renewal. Nat Commun. 2016;7:12326
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Yan Y, Ollila S, Wong I, Vallenius T, Palvimo J, Vaahtomeri K,
et al. SUMOylation of AMPKα1 by PIAS4 specifically regulates mTORC1 signalling. Nat Commun. 2015;6:8979
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Niskanen E, Malinen M, Sutinen P, Toropainen S, Paakinaho V, Vihervaara A,
et al. Global SUMOylation on active chromatin is an acute heat stress response restricting transcription. Genome Biol. 2015;16:153
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Toropainen S, Malinen M, Kaikkonen S, Rytinki M, Jääskeläinen T, Sahu B,
et al. SUMO ligase PIAS1 functions as a target gene selective androgen receptor coregulator on prostate cancer cell chromatin. Nucleic Acids Res. 2015;43:848-61
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Paakinaho V, Kaikkonen S, Makkonen H, Benes V, Palvimo J. SUMOylation regulates the chromatin occupancy and anti-proliferative gene programs of glucocorticoid receptor. Nucleic Acids Res. 2014;42:1575-92
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