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Protein ubiquitination modifications are often accompanied by ubiquitin-proteasome degradation, causing changes in protein stability and participating in various bioregulatory processes such as proliferation and apoptosis, endocytosis and immunity. It occurs through a triple enzyme cascade (E1-E2-E3) that allows single or multiple ubiquitin molecules to be attached to the amino acid (Lys) side chain of a protein, often accompanied by proteasomal degradation, and regulates changes in protein expression levels. The ubiquitination-modified lysine covalently links the ubiquitin molecule, two glycine K-ε-GG residues, resulting in a mass shift of 114.1 Da in molecular weight. The mass shift of 114.1 Da can be accurately determined by mass spectrometry to detect the ubiquitinated modified peptide and its site.
The process of protein ubiquitination modification plays a key role in the regulation of the insect body's immune system. Like the phosphorylation modification process, the ubiquitination modification process is a reversible, covalent modification process. It regulates the stability, functional activity state and intracellular localisation of the modified protein. It is involved in the regulation of many cellular activities including cell cycle, apoptosis, transcriptional regulation, DNA damage repair and immune response. Lifeasible provides services of ubiquitination analysis for insect proteins to detect the large throughput of ubiquitinated modified proteins in insect samples based on mass spectrometry and enrichment processing.
| Analysis content | Detail |
| Ubiquitinated modified proteins in insect samples |
Statistics of protein identification and quantification results, Venn diagram analysis, statistics of difference results, volcano map, cluster heat map.
Subcellular localization, domain analysis, motif analysis, GO function analysis, KEGG pathway analysis, interaction network analysis.
Peptide relative molecular mass distribution, peptide sequence length distribution. |
Lifeasible performs ubiquitinated differential proteomics analysis by data-dependent acquisition-synchronous cumulative sequential fragmentation scanning mode based on mass spectrometry. Using ion flow separation, we can effectively differentiate modified isomeric peptides based on the shape and cross-sectional properties of the molecule, greatly improving the depth of identification of the modification and achieving a comprehensive improvement in the depth of coverage, sensitivity and throughput of proteomics with less loading volume and faster scanning speed.
Fig 1. Service flow for ubiquitination analysis of insect proteins.
| Sample | Requirements |
| Fresh tissue dry weight | >120 mg, transport using dry ice |
| Protein solution | >2 mg, transport using dry ice |
| Number of freshly cultured cells | >108, transport using dry ice |
Lifeasible provides services of ubiquitination analysis for insect proteins using mass spectrometry and enrichment processing to detect the large throughput of ubiquitinated modified proteins in insect samples. If you are interested in our services or if you have any questions, please click online inquiry for more detailed information.
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