Resources

Proteomics Databases



Metabolomics Databases

• • Mass Spectrometry Flow Cytometry Technology

  Flow Cytometry is the most classic single-cell analysis technique, which can detect multiple parameters in single cells, thus conducting subgroup and functional analysis of samples. Traditional flow cytometry is generally based on the detection of fluorescence emission spectra. Since the emission spectra of fluorescent groups are relatively short, overlap often occurs between the emissions of different fluorophores during multi-parameter detection.

• • Detecting Glycosylation

  Glycosylation of protein is a widespread, structurally complex and varied post-translational modification of proteins, playing important roles in cells and organisms, such as participating in the regulation of cell recognition, adhesion, signal transduction, etc.

• • Extracellular Vesicle Proteomics

  Exosomes are small vesicles with a lipid bilayer membrane, with diameters ranging from 30 to 150 nm. They are secreted by living cells and are widely present in various body fluids, including blood, saliva, urine, synovial fluid, milk, cerebrospinal fluid, etc. Exosomes are rich in a large number of bioactive molecules, such as nucleic acids, proteins, lipids, and sugars.

• • Acetylation Detection Methods

  Protein acetylation is a critical protein post-translational modification, which involves the covalent binding of an acetyl group to a lysine residue by an acetyl donor (such as acetyl coenzyme A) through enzymatic or non-enzymatic means. Currently, two forms of acetylation are known - Nα acetylation and Nε acetylation.

• • Protein Modification Prediction Software

  Protein modification is a crucial biochemical process in living organisms. To boost the efficiency of protein modification research, scientists have developed various protein modification prediction software. These tools are primarily used to predict potential modification sites on proteins and possible functional changes post-modification.

• • Peptide Identification Process

  Peptide identification is a core process in proteomics, involving the analysis of proteins in biological samples to identify specific peptide segments. This process is not only crucial for basic biological research, but it also plays a key role in disease diagnosis, drug discovery, and biomarker identification. A complete peptide identification process can be approximately divided into the following stages.

• • Is Prokaryotic Expression Used Before MS Protein Modification?

  In biological research, mass spectrometry analysis is a widely used technique for the quantitative and qualitative analysis of proteins and their modifications. Understanding protein modifications is crucial to reveal their functions. However, the study of protein modifications often faces challenges in preparing suitable protein samples.

• • Proteomics and 2-Hydroxyisobutyrylation MS Analysis

  Proteomics is a discipline that studies all protein expression, structure, and function. It involves describing protein sequences, protein structures, protein interaction networks, and the biological functions and functional dynamics of proteins. Research in proteomics helps to understand the occurrence and development of diseases, reveal the molecular mechanisms of diseases, and provide new drug targets and biomarkers.

• • Circular Dichroism for Determining Absolute Configuration

  The absolute configuration is a way of describing stereochemical molecules, defined according to the spatial configuration of stereoisomers. This is a method of categorizing based on the actual three-dimensional distribution of the structure, unrelated to optical activity or flocculation activity. The most commonly used description method is the Cahn-Ingold-Prelog (CIP) rules.

• • Protein Quantification via Coomassie Brilliant Blue Assay

  The Coomassie Brilliant Blue method for determining protein content is a commonly used method in biology and chemistry experiments. The basic principle is to use Coomassie Brilliant Blue under acidic conditions to stain the structure of proteins, and then determine the protein content in the sample through the ultraviolet spectrophotometric method.