中文背景介绍
蛋白质的氧化还原代谢和氧化还原调节改变了生物医学研究,并正在快速推进临床实施1。这些概念的核心是蛋白质半胱氨酸硫醇与亲电试剂的反应或其氧化,这会影响蛋白质的稳定性、结构和/或功能(例如,对药物的抗性)。因此,半胱氨酸和其他氧化还原敏感位点的蛋白质修饰研究至关重要,需要以高精度进行。
xoder(靶点科技)的化学试剂产品组合包括一系列化合物,适用于与成像、流式细胞术、蛋白质印迹和质谱等最常见下游分析技术兼容的应用。包括用于研究蛋白质磺酰化、反应型半胱氨酸中的关键蛋白质氧化还原修饰以及典型工作流程的试剂示例。 系列用于其他氧化还原修饰和氧化还原改性剂(例如,ros发生器和淬灭剂)的试剂。
英文背景介绍
redox metabolism and redox regulation of proteins have revolutionized biomedical research and are fast advancing towards clinical implementation 1. at the core of these concepts is the reaction of protein cysteine thiols with electrophiles or their oxidation, which influence the stability, structure and/or function of proteins (e.g., resistance to drugs) 2,3. therefore, the study of protein modifications at cysteine and other redox sensitive sites is critical and needs to be conducted with a high level of precision.
our portfolio of chemical reagents includes a series of compounds for applications compatible with most common downstream analytical technologies such as imaging, flow cytometry, western blot, and mass spectrometry. examples of reagents for studying protein sulfenylation, a key protein redox modification at reactive cysteines, and typical workflows are included below 4-11. these can be found here along with reagents for other redox modifications and redox modifiers (e.g., ros generators and quenchers).
试剂选择表格
实验处理流程
精选参考文献
1 chen x, lee j, wu h, tsang aw, furdui cm. mass spectrometry in advancement of redox precision medicine. adv exp med biol. 2019;1140:327-358. pmid: 31347057.
2 poole lb, furdui cm, king sb. introduction to approaches and tools for the evaluation of protein cysteine oxidation. essays biochem. 2020 feb 17;64(1):1-17. pmid: 32031597; pmcid: pmc7477960.
3 baez no, reisz ja, furdui cm. mass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveats. free radic biol med. 2015 mar;80:191-211. epub 2014 sep 28. pmid: 25261734; pmcid: pmc4355329.
4 poole lb, klomsiri c, knaggs sa, furdui cm, nelson kj, thomas mj, fetrow js, daniel lw, king sb. fluorescent and affinity-based tools to detect cysteine sulfenic acid formation in proteins. bioconjug chem. 2007 nov-dec;18(6):2004-17. epub 2007 nov 21. pmid: 18030992; pmcid: pmc2526167.
5 klomsiri c, nelson kj, bechtold e, soito l, johnson lc, lowther wt, ryu se, king sb, furdui cm, poole lb. use of dimedone-based chemical probes for sulfenic acid detection evaluation of conditions affecting probe incorporation into redox-sensitive proteins. methods enzymol. 2010;473:77-94. pmid: 20513472; pmcid: pmc3795394.
6 furdui cm, poole lb. chemical approaches to detect and analyze protein sulfenic acids. mass spectrom rev. 2014 mar-apr;33(2):126-46. epub 2013 sep 17. pmid: 24105931; pmcid: pmc3946320.
7 qian j, klomsiri c, wright mw, king sb, tsang aw, poole lb, furdui cm. simple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteins. chem commun (camb). 2011 aug 28;47(32):9203-5. epub 2011 jul 8. pmid: 21738918; pmcid: pmc3587177.
8 qian j, klomsiri c, wright mw, king sb, tsang aw, poole lb, furdui cm. simple synthesis of 1,3-cyclopentanedione derived probes for labeling sulfenic acid proteins. chem commun (camb). 2011 aug 28;47(32):9203-5. epub 2011 jul 8. pmid: 21738918; pmcid: pmc3587177.
9 poole th, reisz ja, zhao w, poole lb, furdui cm, king sb. strained cycloalkynes as new protein sulfenic acid traps. j am chem soc. 2014 apr 30;136(17):6167-70. epub 2014 apr 16. pmid: 24724926; pmcid: pmc4017607.
10 li z, forshaw te, holmila rj, vance sa, wu h, poole lb, furdui cm, king sb. triphenylphosphonium-derived protein sulfenic acid trapping agents: synthesis, reactivity, and effect on mitochondrial function. chem res toxicol. 2019 mar 18;32(3):526-534. epub 2019 mar 4. pmid: 30784263; pmcid: pmc6719313.
11 holmila rj, vance sa, chen x, wu h, shukla k, bharadwaj ms, mims j, wary z, marrs g, singh r, molina aj, poole lb, king sb, furdui cm. mitochondria-targeted probes for imaging protein sulfenylation. sci rep. 2018 apr 27;8(1):6635. pmid: 29703899; pmcid: pmc5923234.
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