Resources

Proteomics Databases



Metabolomics Databases

• • TMT vs Label Free

  TMT is a chemical labeling method used for quantitative proteomics. Peptides from different samples are chemically labeled with different isotopic labels. These labels are designed to have the same mass, but when broken down in a mass spectrometer they will release different reporter ions. The relative abundance of peptides in different samples can be determined by comparing the intensities of these reporter ions.

• • Targeted Proteomics

  Targeted proteomics is a mass spectrometry method that focuses on studying a specific set of proteins or peptides, in contrast to traditional global proteomics analysis. Targeted proteomics typically uses selected reaction monitoring (SRM) or multiple reaction monitoring (MRM) techniques to specifically detect and quantify specific peptide segments.

• • Protein Amino Acid Composition Analysis

  Protein amino acid composition analysis is to understand the basic composition of proteins by determining the types of amino acids they contain and their relative molar ratios. This analysis method is commonly used to identify, quantify and study the chemical properties and structure of proteins and peptides. Below are some techniques commonly used for protein amino acid composition analysis:

• • TMT Quantitative Mass Spectrometry

  TMT (Tandem Mass Tag) is a widely used technique in quantitative proteomics. TMT is a chemical labeling method used for quantitative proteomics. Peptides from different samples are labeled with different isotopic tags. These tags have the same mass in the mass spectrometer, but when they are fragmented in the mass spectrometer, they release different reporter ions. By comparing the intensities of these reporter ions, the relative abundance of peptides in different samples can be determined.

• • Fundamentals of Infrared Spectroscopy and Spectrum Analysis

  Infrared spectroscopy (IR) is an experimental technique widely used in the fields of chemistry, biology, and materials science. Its basic principle is that chemical bonds in molecules absorb infrared radiation at specific frequencies, resulting in vibrational motion of the bonds. Infrared spectra display the specific frequencies at which a material absorbs infrared radiation.

• • Number of Replicate Samples in Epigenomics Experiments

  In epigenomic experiments, parallel samples are used to ensure the reliability and reproducibility of experimental results. The choice of the number of parallel samples depends on various factors, including experimental design, expected variability, and data analysis methods.

• • Analysis of mRNA 5' Capping Rate in Brain Tissue

  The 5' cap of mRNA in brain tissue is a crucial biological process that is essential for regulating gene expression and cellular function. The 5' cap structure of mRNA not only protects mRNA from degradation by exogenous nucleases, but also facilitates its nuclear export, localization, and translation. This regulation is particularly important in the nervous system as it affects neuronal signaling, neuronal cell survival, and overall brain function.

• • Sample Preparation and Submission Guide for Proteomics Research

  Proteomics research requires following certain guidelines and steps for sample submission to ensure sample quality and accuracy of analysis results. The following are general guidelines for sample preparation and submission: Sample Preparation: Ensure sample representativeness and sufficient quantity. Use appropriate buffer and inhibitors to extract proteins, avoiding protein degradation and modifications. Remove cell debris and insoluble material through centrifugation or filtration.

• • Overview of Label-Free Proteomics Experimental Workflow

  Label-free proteomics is a method for analyzing protein expression without the need for pre-labeling samples. The advantages of this method include its simplicity, cost-effectiveness, and applicability to a wide range of sample types.

• • Dia Proteomics

  DIA (Data-Independent Acquisition Proteomics) proteomics is an advanced mass spectrometry technique used for in-depth protein analysis. Compared to the traditional Data-Dependent Acquisition (DDA) method, DIA technology provides higher coverage and quantification accuracy in proteomic research, allowing researchers to analyze proteins in samples more comprehensively. The core of DIA proteomics lies in its mass spectrometry acquisition mode.