Protein carbonylation is an irreversible, non-enzymatic post-translational modification (PTM) commonly used as a marker of oxidative stress. Research has shown that protein carbonyls are involved in the etiology and progression of disease and age-related changes in the body. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein carbonylation service to accelerate your project.

Protein carbonylation is a post-translational modification involving reactive oxygen species. It generally refers to the formation of reactive ketones or aldehydes that can react with 2,4-dinitrophenylhydrazine (DNPH) to form hydrazones. This occurs especially on lysine, arginine, threonine and proline. Numerous studies have shown that protein carbonylation increases with age in cells, organelles and tissues of different species. Furthermore, protein carbonylation is associated with various age-related or metabolic diseases, such as Alzheimer's disease, Parkinson's disease, diabetes, chronic lung disease, etc. The current development of antibodies against DNPH-derived proteins has revolutionized the study of carbonylated proteins by allowing the use of immunological techniques. A variety of advanced methods allow the identification of carbonylated proteins in various diseases in humans, animal models, and cellular models.

Fig 1. Analytical flowchart of the identification of protein carbonylation sites. (Weng SL, et al., 2017)

Services

Mass spectrometry-based proteomics has been used for site-specific identification of carbonylated peptides. However, due to the labile nature of ROS bonds and the low abundance of endogenous carbonylated proteins in vivo, the unambiguous identification of carbonylated proteins and modification sites by commonly used proteomic techniques remains challenging. Creative BioMart has successfully performed reliable studies of protein carbonylation using a variety of techniques to fully understand the carbonylation status of proteins. In addition, our scientists are commmitted to developing computational analysis tools to comprehensively study the efficiency of protein carbonylation sites. Here, we consider a variety of sequence-based features, including amino acid sequence, amino acid composition (AAC), amino acid pair composition (AAPC), position-weighted matrix (PWM), position-specific scoring matrix (PSSM), solvent accessible surface area (ASA) and physicochemical properties (AAindex) were evaluated for the best predictive model.

Protein carbonylation mediates redox signaling processes, which may contribute to pathogenesis. Therefore, the development of drugs that can control the carbonylation status of cellular proteins should facilitate the development of therapeutic strategies for various diseases. We provide the following services for protein carbonylation, including but not limited to:

• Detecting and quantifying protein carbonylation: we used a mass spectrometry-based large-scale proteomic approach to uncover the potential of novel protein targets susceptible to carbonylation modifications to quantitatively characterize how these modifications change in disease states or aging.
• Identification of carbonylated proteins: we used methods based on two-dimensional gel-based approaches and gel-free proteomic approaches to enrich carbonylation from complex mixtures, including analysis of membrane and low-abundance proteins.
• Predicted carbonyl modification sites and types: we determined the exact amino acid sites and types of carbonylation modifications by mass spectrometry/mass spectrometry analysis and sequence database searches. Furthermore, three classifiers, namely Support Vector Machines (SVM), Decision Trees (DT) and Random Forests (RF), were used to build a predictive model using each type of feature.

Approaches for Analyzing Protein Carbonylation

• Spectrophotometry.
• ELISA.
• Slot blot.
• Two-dimensional gel electrophoresis.
• Proteomics.
• Mass spectrometry.
• Computer-based method.

Our mission is to provide global customers with the most comprehensive and professional customized protein carbonylation service. If you have any special requirements about our services, please feel free to contact us. We are looking forward to working together with your attractive projects.

Reference

1. Weng SL, Huang KY, Kaunang FJ, et al.. (2017) Investigation and identification of protein carbonylation sites based on position-specific amino acid composition and physicochemical features. BMC Bioinformatics. 18(Suppl 3):66.

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