Protein S-nitrosylation (SNO) is one of the most important and common post-translational modifications (PTMs) that regulate a variety of physiological and pathological processes, such as immune responses, cellular senescence, and transcriptional and post-translational regulation. Creative BioMart's extensive experience in post-translational modification of proteins based on computational and experimental methods enables us to provide protein nitrosylation service to accelerate your project.

Protein S-nitrosylation (SNO) is a process of covalent modification of nitric oxide (NO) and its derivatives and cysteine residues. Protein S-nitrosylation has been reported to play a role in the in vitro/in vivo regulation of various metabolic enzymes, oxidoreductases, proteases, protein kinases, and protein phosphatases, as well as the function of regulatory factors, including G proteins. In addition, abnormalities in protein S-nitrosylation and other post-translational modifications contribute to many diseases, such as Alzheimer's disease and breast cancer. Therefore, regulating protein S-nitrosylation modification may be a new and effective way of health protection. There is a current need for improved analytical methods to identify and quantify S-nitrosylated proteins under various physiological and pathophysiological conditions for investigational studies and clinical diagnosis. Accurate prediction of SNO sites is crucial for revealing a certain biological mechanism of NO regulation and related drug development.

Fig 1. A schematic diagram of protein S-nitrosylation sites. (Zhao Q, et al., 2021)

Services

Proteomic analysis of S-nitrosothiols produced in vivo has been challenging due to the low-level, dynamic, and unstable nature of S-nitrosylation. To address these challenges, Creative BioMart has successfully employed a variety of techniques to reliably study protein nitrosylation to fully understand the S-nitrosylation status of proteins. Combining traditional mass spectrometry-based proteomics, biotin conversion technology (BST) and advanced computational methods, we offer a variety of services for S-nitrosylated (SNO) proteins, including but not limited to:

• Detection and identification of S-nitrosylated proteins: relying on exogenous treatment with NO or NO donors, increases the total amount of intracellular RSNO to enhance the effects of NO. We performed SNO-site identification and SNO-site quantification using various new techniques for S-nitrosylated protein enrichment and identification.
• Structural features of cysteine S-nitrosylation sites: most proteins have cysteine residues, but the affinity of this amino acid residue for NO can vary widely. Consensus motifs were first found by analyzing the linear sequences of S-nitrosylated proteins. Second, we employ a variety of different methods and proteomic approaches to detect and identify S-nitrosylation sites, and the growing number of identified SNO sites allows analysis of the precise environment of modified cysteines.
• Computational prediction of protein S-nitrosylation sites: we developed various computational methods to predict protein S-nitrosylation sites, especially when the proportion of S-nitrosylation sites is less than 1%. Here, we can provide useful and experimentally testable information about potential protein S-nitrosylation sites.

Approaches for Analyzing Protein Nitrosylation

We use traditional methods combined with computational methods to predict SNO. Our services are dedicated to accelerating research on SNO and facilitating the prediction of SNO sites, paving the way for accelerated related drug development.

• Biotin switch assay (BSA) technology.
• Biotin conversion technology (BST).
• Computational biology methods.

Our mission is to provide global customers with the most comprehensive and professional customized protein nitrosylation 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. Zhao Q, Ma J, Xie F, et al.. (2021) Recent Advances in Predicting Protein S-Nitrosylation Sites. Biomed Res Int. 2021: 5542224.

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