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4D proteomics for deeper protein analysis (CAT#: STEM-MB-0100-WXH)

Introduction

The basic principle of mass spectrometry proteomics is to analyze the physical and chemical properties of the measured sample ions, and obtain qualitative and quantitative results based on the mass spectrum and related information of the sample. At present, mass spectrometry analysis of proteomics generally identifies and quantifies peptide proteins based on three dimensions: retention time, mass-to-charge ratio (m/z), and ionic intensity (intensity), that is, 3D proteomics. On the basis of 3D proteomics, 4D proteomics adds the fourth dimension, ion mobility, which mainly separates ions according to their shape and cross-section, and can distinguish peptides with very small m/z differences, enabling low-abundance protein signals to be differentiated and identified. 4D has greatly improved the identification accuracy, identification depth, quantitative accuracy, and detection cycle, and the sample size requirement has been greatly reduced.




Applications

• Protein expression profiling for drug response, gene knockout/overexpression
• Physiological research on growth and development of plants and microorganisms and stress and adversity
• High-throughput analysis of disease biomarkers and drug targets
• Mechanism of protein action and screening of proteins with special functions
• Construction of draft proteomes in various species

Procedure

1. Sampling: tissues, cells, body fluids, etc.
2. Quality inspection of protein extraction, enzymatic hydrolysis and fragmentation
3. 4D proteomics technology detection
4. Bioinformatics analysis

Notes

Customer provides protein or tissue samples.

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