- Untargeted Metabolomics
- Lipidomics
- Targeted Metabolomics
- Functional Metabolomics
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Proteomics
- Nanoparticle proteomics
- iTRAQ/TMT-based Proteomics Analysis
- Label free Quantitative Proteomics
- Protein Identification
- DIA proteomics
- Peptidomics
- Parallel Reaction Monitoring (PRM) Targeted Proteome
- Metpro -Ⅱ Protein-Metabolite Interactions
- Phosphoproteomics
- Acetylation Analysis
- Protein Ubiquitination Analysis
Covalent attachment of ubiquitin to proteins governs a wide array of cellular processes, including cell division, DNA repair, endocytosis, cellular signaling, and protein quality control. The sequential action of three enzymes — E1 ubiquitin-activating enzyme, E2 ubiquitin-conjugating enzyme, and E3 ubiquitin ligase results in attachment of ubiquitin to a substrate protein, usually via an amide (isopeptide) bond that links the C-terminal carboxyl group of ubiquitin with a lysine side chain(s) of the protein substrate . Ubiquitin itself possesses seven lysine residues (Lys6, 11, 27, 29, 33, 48, and 63), enabling it to form ubiquitin polymers; chains with different linkages signal different functional outcomes for the tagged proteins . All seven lysines are used for chain formation in vivo, as is the N-terminal α-amino group, the latter leading to ‘linear’ ubiquitin chains. Chains can be homopolymeric or, less commonly, of mixed linkage. Branched ubiquitin chains, which use different lysines of a single ubiquitin for chain extension, can also form.
Advantages
Instrument: Orbitrap high resolution mass spectrometry, realizing ultra-high sensitivity detection.
Enrichment Kit: ultra high enrichment efficiency and coverage.
Qualitative and quantitative: internationally recognized data search software.
Application
Disease biomarkers
Plant stress
Molecular mechanism of occurrence and development of diseases
Target of chemical or biological drugs
