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Introduction
S‑Nitrosylation involves the reversible attachment of nitric oxide (NO) to cysteine thiols, forming S‑nitrosothiols (SNOs). As a key mechanism of NO signaling, it dynamically regulates protein activity, localization, and interactions. Dysregulated S‑nitrosylation has been linked to altered redox homeostasis and diverse pathological processes, particularly in cardiovascular and neurological diseases.
Products Solutions
Our human protein S‑nitrosylation arrays enable high‑throughput profiling of S‑nitrosylated proteins across hundreds of targets. Using selective labeling of S‑nitrosylated cysteines combined with antibody‑based detection, the platform facilitates comparative analysis of protein S‑nitrosylation across biological samples.
- High‑throughput S‑nitrosylation profiling
- Multiplex analysis of hundreds of protein targets
- Selective detection of S‑nitrosylated cysteines
- Comparative analysis across biological samples
Research Areas
- Cancer Research
- Cardiovascular Biology
- Neuroscience & Neurodegeneration
References
- Su, Q., Qin, JQ., Huang, Y. et al. USP16 S‑nitrosylation aggravates coronary microembolization‑induced myocardial injury via repressing KDM1A‑mediated glutathione homeostasis. Nat Commun 17, 255 (2026).
- Cheng A, Wang J, Li J, et al. S‑Nitrosylation of p39 promotes its degradation and contributes to synaptic dysfunction induced by β‑amyloid peptide. Commun Biol. 2024;7(1):1113.
- Okuda, K., Nakahara, K., Ito, A. et al. Pivotal role for S‑nitrosylation of DNA methyltransferase 3B in epigenetic regulation of tumorigenesis. Nat Commun 14, 621 (2023).
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