Indirect detection of protein S-Nitrosothiol modification using existing kits is limited by poor selectivity
Nitric oxide (NO) is a key biological molecule in many aspects of health and disease. Certain thiol groups of amino acid are reversibly modified by nitric oxide and form S-Nitrosothiol modifications. Some of these modifications have been shown to alter in several pathological conditions, such as Alzheimer’s disease, Parkinson’s disease, stroke, heart disease, pulmonary and musculoskeletal dysfunction as well as cancer. Despite the widely recognized importance of S-Nitrosylation, the detection methods are limited. The only commercial kits for detecting the modification utilize Biotin Switch Technique, which is indirect and non-selective. The poor selectivity of existing kits can lead to false identification of modification, which is likely to compromise the quality of research.
A novel direct assay to detect protein S-Nitrosylation with high selectivity
The researchers at University of Michigan have demonstrated a novel method to detect protein S-Nitrosylation. Unlike current methods, this approach enables the one-step enrichment of S-Nitrosylation with no cross-reactivity towards other cysteine post-translational modifications. This method has the potential to replace current commercial kits for monitoring protein oxidation, and provide a simplified route for quantifying select S-Nitrosylation modifications from biological samples or materials.
- Detection of nitrosothiols in clinical biopsies.
- Detection of nitrosothiols in materials.
- Detection of nitrosothiols biological specimens for basic research.
- Mapping sites of nitrosothiols in proteins for profiling drug dependent oxidative responses.
- Improve the accuracy of S-Nitrosylation detection
- Allow a simplified procedure for quantifying S-Nitrosylation modification
- Can be used in modification detection as well as site mapping