Protein Cysteine

"Protein cysteine redox status, two types of proteomic methods have been frequently used: gel-based and MS- based methods. The gel-based method has been widely applied in distinguishing the differentially post-translation modified proteins, such as redox modification of cysteines. One example is the non- reducing/reducing diagonal 2D-PAGE, which analyzes the global disulfide proteome before the thiol-reactive reagents were introduced into the study of the thiol redox status. Other improved gel-based methods are dependent on the cysteine alkylation reagent-mediated radioactive 14 -labeling, the fluorescence-labeling and the biotin- PDP-labeling, which were combined with the two-dimensional differential gel electrophoresis to develop the method of Redox-DIGE. OMICS Group International is one of the leading Open Access Publishers which is publishing 700+ peer-reviewed journals with the support of 50,000+ editorial board members as editorial team and aimed to disseminate the scholarly knowledge to the scientific society. OMICS Group also organizing 3000+ International Scientific Conferences and events yearly all over the world with the support of 1000+ Scientific associations worldwide. Citation: Hu Q, Guo G, Yang Z, Li Y, Xia Y (2014) Stable Isotope Metabolic Labeling-Based Quantitative Thiol Redox Proteomic Analysis of Hydrogen Peroxide-treated Arabidopsis plant. J Proteomics Bioinform 7: 121-133."

• Share this page
• 
• 
• 
• 
• 
• 

Last date updated on April, 2024