Resources

Proteomics Databases



Metabolomics Databases

• • Low Protein Yield? Microscale Sequencing Solutions for Critical Samples

  With the rapid development of single-cell omics, tumor microenvironment studies, and novel protein therapeutics, researchers are increasingly confronted with a specific sequencing challenge: sample quantities are extremely limited—often at nanogram or even picomole levels—while background complexity and low signal-to-noise ratios severely hinder protein full-length sequencing. This limitation is particularly pronounced in contexts such as antibody sequencing, analysis of clinical biopsy fluids, or .........

• • What Are the N-Terminus and C-Terminus of an Antibody? Accurate Sequencing Resolves Structural Challenges

  Antibodies serve as core effectors of the immune system and have become increasingly central to disease diagnostics, drug development, and targeted therapeutics. With the rapid expansion of the antibody-based therapeutics market, there is a growing demand for comprehensive structural characterization. This article focuses on the N-terminus and C-terminus of antibody molecules and explores how accurate protein sequencing technologies address key challenges in antibody structure elucidation. What Are the.....

• • Irreplaceability of Full-Length Sequencing:Why Traditional Mass Spectrometry Cannot Achieve Complete Protein Coverage

  In modern proteomics research, mass spectrometry has undoubtedly become a critical tool for advancing the discovery and functional characterization of proteins. From large-scale protein identification to the analysis of post-translational modifications (PTMs), traditional database-dependent mass spectrometry strategies—such as data-dependent acquisition (DDA) and data-independent acquisition (DIA)—offer broad expression profiling capabilities. However, when the focus shifts to deciphering the complete .....

• • Edman Degradation vs Protein Full-Length Sequencing: A Complete Analysis Strategy from N-Terminus to C-Terminus

  In the investigation of protein functionality, validation of recombinant proteins, and development of antibody-based therapeutics, the accurate determination of the primary structure—namely, the linear sequence of amino acids—represents a fundamental and indispensable step. To accomplish this, researchers commonly employ two primary methodologies: Edman Degradation: A well-established chemical technique that enables sequential identification of amino acids from the N-terminus; Protein full-length ..........

• • Struggling with Complex Isoforms? A Step-by-Step Guide to Protein Full-Length Sequencing Characterization

  In protein expression systems, even proteins derived from the same gene may result in multiple protein isoforms that are structurally similar yet functionally distinct. These differences can arise from alternative splicing, variation in translation initiation, post-translational modifications, or divergent degradation pathways. Such isoforms are commonly found in natural proteins and are especially relevant during the development of biopharmaceuticals—including antibody drugs, fusion proteins, and .........

• • Current State, Challenges, and Development Trends in Targeted Proteomics

  With ongoing advances in proteomic technologies, research priorities are shifting progressively from discovery-driven approaches to targeted strategies. Targeted proteomics, particularly techniques such as Multiple Reaction Monitoring (MRM/SRM) and Parallel Reaction Monitoring (PRM), has emerged as a pivotal tool for biomarker validation, drug target confirmation, and the evaluation of responses to biological therapies. This review provides a systematic overview of the current progress, major technical.....

• • Unlocking Cancer Biomarkers: The Role of Protein Full-Length Sequencing in Precision Oncology

  With the rapid advancement of precision medicine and personalized therapeutic strategies, the identification of cancer biomarkers has become a cornerstone of early detection, prognostic evaluation, and therapeutic decision-making in oncology. However, conventional proteomics approaches predominantly target localized protein fragments or peptide segments, which hampers the comprehensive characterization of protein structural variations—such as splice isoforms, post-translational modifications (PTMs), and....

• • PRM vs. MRM: Comparative Analysis in Quantitative Proteomics

  In proteomics research, targeted quantification techniques play an increasingly critical role, spanning the workflow from target discovery to result validation. Compared to traditional approaches such as labeled quantification and data-dependent acquisition (DDA), Multiple Reaction Monitoring (MRM) and Parallel Reaction Monitoring (PRM) offer superior specificity, sensitivity, and reproducibility—making them especially advantageous for the precise detection of low-abundance proteins. With the advancement...

• • PRM and MRM in Targeted Proteomics: Advantages and Limitations

  Targeted proteomics, recognized for its high quantitative accuracy and reproducibility, has emerged as a pivotal approach in biomarker validation, translational clinical research, and the investigation of drug mechanisms. At present, two primary mass spectrometry-based targeted strategies—Multiple Reaction Monitoring (MRM) and Parallel Reaction Monitoring (PRM)—have demonstrated distinct technical characteristics and application-specific strengths. This article provides an in-depth comparison of PRM and....

• • Immunogenicity Testing of Therapeutic Proteins

  Immunogenicity Testing of Therapeutic Proteins involves the assessment of the likelihood and extent to which exogenous proteins—such as recombinant proteins, monoclonal antibodies, and fusion proteins—elicit immune responses in the human body, using a combination of biological, immunological, and molecular techniques. With advances in biopharmaceutical technology, therapeutic proteins have become integral to the treatment of cancers, autoimmune diseases, metabolic disorders, and other conditions.