Resources

    Proteomics Databases

    resources1

    Metabolomics Databases

    resources2
  • • How to Analyze CD Spectra Using Deconvolution Algorithms

    Circular Dichroism (CD) spectroscopy is an important technique for investigating the secondary structures of proteins. However, a CD spectrum essentially represents the superposition of multiple structural components (such as α-helices, β-sheets, and random coils), and thus cannot directly reveal the proportion of each constituent. In such cases, the deconvolution algorithm serves as a crucial analytical approach. This study systematically presents the principles, workflow, and considerations for appl......

  • • Circular Dichroism Analysis of Antibody Drugs

    In antibody drug development, structural characterization is a critical step to ensure both safety and therapeutic efficacy. Circular dichroism (CD) is an optical technique that relies on the differential absorption of left- and right-circularly polarized light by chiral molecules. Owing to its operational simplicity, high sensitivity, and minimal sample requirement, Circular Dichroism analysis has become a widely employed method for investigating protein secondary structures.   Introduction to Circul......

  • • DIA-MS Analysis Solutions for Diverse Sample Types: Plasma, Tissue, and More

    In proteomics research, achieving high reproducibility across biologically diverse and complex sample types remains a persistent challenge. A central focus of mass spectrometry development is how to enable high-throughput, low-bias quantitative analysis for a wide range of biological specimens, including plasma, tissue, cells, and body fluids. Data-Independent Acquisition Mass Spectrometry (DIA-MS), with its high proteome coverage, superior reproducibility, and minimal missing values, is emerging as a .....

  • • Far UV Circular Dichroism (CD) Spectroscopy Analysis

    In structural biology, the precise determination of protein secondary structures is fundamental to elucidating their functions. Far-UV Circular Dichroism (CD) spectroscopy, a highly sensitive and non-destructive technique, is widely employed for investigating protein conformations, assessing structural stability, and analyzing drug–protein interactions across diverse research fields. What is Far-UV Circular Dichroism (CD) Spectroscopy? Circular Dichroism (CD) refers to the differential absorption of l......

  • • CD Spectroscopy vs FTIR: Which Technique is Better for Analyzing Protein Secondary Structure?

    The structural organization of a protein dictates its biological function, with secondary structure representing a pivotal level in this hierarchy. Alterations in α-helices, β-sheets, and random coils are frequently associated with functional transitions of proteins, including partial or complete inactivation. Consequently, accurate characterization of protein secondary structure is essential not only for fundamental research but also for applications such as drug development, evaluation of biopharmac......

  • • How to Use CD Spectroscopy for Protein Secondary Structure Analysis: A Complete Guide

    Circular Dichroism (CD) spectroscopy is a technique that measures the differential absorption of circularly polarized light by chiral molecules, and it is widely employed for rapid qualitative and quantitative assessment of protein secondary structures. In contrast to high-resolution approaches such as X-ray crystallography or nuclear magnetic resonance (NMR), CD spectroscopy offers distinct advantages, including rapid data acquisition, no requirement for crystallization, and minimal sample consumptio......

  • • Current Status and Future Trends in Single Cell Proteomics

    In contemporary life science research, the ability to resolve molecular features at the single-cell level has become crucial for overcoming the challenges associated with studying cellular heterogeneity. Single-cell RNA sequencing (scRNA-seq) has been widely adopted in fields such as developmental biology, immunology, and oncology, revealing extensive intercellular transcriptional differences. However, mRNA levels cannot directly represent a cell’s functional state, as proteins serve as the primary ........

  • • Sample Preparation Protocol for Single Cell Protein Analysis

    With the rapid advancement of single-cell omics, single-cell proteomics (SCP) has transitioned from method validation to large-scale applications, emerging as a core technology for elucidating cellular functional states, population heterogeneity, and microenvironmental interactions. SCP enables direct interrogation of cell states at the functional level, and its research significance has become increasingly evident in fields such as oncology, immunology, stem cell biology, and neuroscience. However, SCP....

  • • Advances in Single Cell Proteomics for Cancer Research

    In the field of cancer research, molecular profiling technologies at the single-cell level are rapidly emerging as pivotal tools for advancing precision medicine. With the widespread adoption of single-cell RNA sequencing (scRNA-seq), our understanding of cellular heterogeneity and interactions within the tumor microenvironment has significantly deepened. However, proteins, as the primary effectors of cellular functions, exhibit intricate interdependencies among their expression levels, post-translational..

  • • Data Analysis Strategies and Toolkits for Single Cell Proteomics

    Single Cell Proteomics (SCP) enables the investigation of protein expression, post-translational modifications, and functional states at the resolution of individual cells. With advances in mass spectrometry technologies, Single Cell Proteomics has emerged as a critical approach for elucidating cellular heterogeneity, molecular mechanisms, and potential disease biomarkers. Nevertheless, the intrinsic high dimensionality, sparsity, and heterogeneity of Single Cell Proteomics data pose significant .......

Submit Inquiry
Name *
Email Address *
Phone Number
Inquiry Project
Project Description *

 

How to order?


/assets/images/icon/icon-message.png

Submit Inquiry

/assets/images/icon/icon-return.png