OX133, a monoclonal antibody recognizing protein-bound N-ethylmaleimide for the identification of reduced disulfide bonds in proteins.
OX133, a monoclonal antibody recognizing protein-bound N-ethylmaleimide for the identification of reduced disulfide bonds in proteins.
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DOI：
10.1080/19420862.2016.1152443
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发表时间：
2016-05
期刊：
影响因子：
5.3
通讯作者：
Barclay AN
中科院分区：
文献类型：
--
作者：
Holbrook LM;Kwong LS;Metcalfe CL;Fenouillet E;Jones IM;Barclay AN
在体内，一些蛋白质二硫键（变构二硫键）的酶促还原提供了重要的结构和功能调节水平。产生的游离半胱氨酸残基可以通过马来酰亚胺试剂（包括生物素衍生物）标记，从而允许检测或纯化还原的蛋白质。在筛选特异于还原型蛋白的单克隆抗体的过程中，我们分离出OX 133，这是一种独特的抗体，它以序列独立的方式识别多肽居民、N-乙基马来酰亚胺（NEM）修饰的半胱氨酸残基。OX 133为标记还原/烷基化抗原和捕获还原/烷基化蛋白质提供了生物素-马来酰亚胺试剂的替代方案，其优点是NEM修饰的蛋白质在质谱法中更容易检测，并且比用基于生物素的试剂捕获后的情况更容易回收。
In vivo, enzymatic reduction of some protein disulfide bonds, allosteric disulfide bonds, provides an important level of structural and functional regulation. The free cysteine residues generated can be labeled by maleimide reagents, including biotin derivatives, allowing the reduced protein to be detected or purified. During the screening of monoclonal antibodies for those specific for the reduced forms of proteins, we isolated OX133, a unique antibody that recognizes polypeptide resident, N-ethylmaleimide (NEM)-modified cysteine residues in a sequence-independent manner. OX133 offers an alternative to biotin-maleimide reagents for labeling reduced/alkylated antigens and capturing reduced/alkylated proteins with the advantage that NEM-modified proteins are more easily detected in mass spectrometry, and may be more easily recovered than is the case following capture with biotin based reagents.
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影响因子：
4.8
作者：
Papandreou, Marie-Jeanne;Barbouche, Rym;Fenouillet, Emmanuel
通讯作者：
Fenouillet, Emmanuel
影响因子：
5.8
作者：
Metcalfe C;Cresswell P;Barclay AN
通讯作者：
Barclay AN
影响因子：
--
作者：
Schmidt B;Hogg PJ
通讯作者：
Hogg PJ
影响因子：
4.8
作者：
Barbouche, R;Miquelis, R;Fenouillet, E
通讯作者：
Fenouillet, E
影响因子：
10.4
作者：
Hogg, P. J.
通讯作者：
Hogg, P. J.