Resources

• • Detection of Protein Methylation Based on LC-MS/MS

  Protein methylation is one of the critical post-translational modifications that regulate various biological processes, including gene expression, signal transduction, and protein-protein interactions. This modification primarily occurs on lysine and arginine residues through the transfer of methyl groups by methyltransferases, resulting in mono-, di-, or trimethylation.

• • Quantitative Analysis of Protein Acetylation Using Acetylomics

  Acetylation is a key post-translational modification that plays a significant role in regulating various biological processes, including gene expression, cell cycle control, metabolism, and stress responses. Typically occurring on lysine residues, acetylation modifies protein structure and function through the addition of an acetyl group, which in turn influences cellular physiology.

• • Analysis of Acetylation Sites Using Acetyl-proteomics

  Protein acetylation is a critical post-translational modification that plays a pivotal role in cellular processes such as metabolism, signal transduction, and gene expression regulation. The analysis of acetylation sites provides insights into the regulatory mechanisms of protein functions and uncovers molecular pathways involved in various diseases.

• • Quantitative Analysis of Glycoproteins Using Nano-LC and Orbitrap Fusion

  Glycoproteins are proteins that play crucial roles in biological processes, with glycosylation modifications affecting protein structure, stability, and function. Aberrant glycosylation is associated with various diseases, including cancer, diabetes, and neurodegenerative disorders, making glycoprotein analysis important in both basic research and clinical diagnostics. Due to the structural complexity and heterogeneity of glycoproteins, traditional analytical methods often fall short in accurately character

• • High-Throughput Identification and Quantification of Ubiquitinated Proteins

  Ubiquitin is a small, highly conserved protein found in all eukaryotes, playing pivotal roles in a range of biological processes including protein degradation, regulation of the cell cycle, DNA repair, and signal transduction. Ubiquitination involves the covalent attachment of ubiquitin to substrate proteins, which can tag them for degradation via the proteasome or alter their activity, localization, or interactions.

• • Detection and Analysis of Glycoproteins Based on HCD/ETD Mass Spectrometry

  Glycoproteins play crucial roles in various physiological functions, including cell communication, immune response, and protein stability regulation. Given their structural complexity and key roles in biological functions, the detection and analysis of glycoproteins have become a significant focus in biological research.

• • Quantitative Analysis of Phosphoproteins Using iTRAQ/TMT Labeling

  Protein phosphorylation is a critical post-translational modification involved in numerous physiological processes, including cellular signal transduction and regulation. Accurately quantifying the phosphorylation status of proteins is essential for understanding their functional roles within biological systems.

• • Detection of Low Abundance Phosphoproteins Using TiO2 and IMAC

  Protein phosphorylation is a critical post-translational modification widely present in cells, influencing various biological processes such as signal transduction, cell cycle regulation, and metabolism. The study of phosphorylated proteins is essential for understanding the regulatory mechanisms behind these processes.

• • Procedure of Membrane Protein Purification with Detergent Optimization

  Membrane proteins play a critical role in cellular processes, including signal transduction, transport of molecules, and energy transduction. Despite their significance, purifying these proteins in a functional state remains a challenging endeavor. The delicate balance between maintaining protein stability and functionality during extraction and purification processes is paramount.

• • MALDI-TOF Analysis of Peptide Mass Fingerprinting

  Peptide Mass Fingerprinting (PMF) is a widely used analytical method for protein identification based on mass spectrometry. Among the various techniques employed, Matrix-Assisted Laser Desorption/Ionization-Time of Flight Mass Spectrometry (MALDI-TOF MS) has emerged as a prominent tool. This technique enables the rapid identification of proteins by measuring the masses of peptide fragments and comparing them with reference databases.