Resources
Proteomics Databases
Metabolomics Databases

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• Can mass spectrometry be used in proteomics?
Learn whether mass spectrometry can be used in proteomics, why it is the standard measurement platform, how it compares with antibody methods, and when an MS workflow is the right choice.
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• Bottom-Up Proteomics Guide: Principles, Workflows, and LC–MS/MS Applications
A bottom-up proteomics guide covering core principles, standard workflow steps, LC-MS/MS acquisition modes, quantitation strategies, and key applications in protein analysis.
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• A Beginner's Guide to Mass Spectrometry-Based Proteomics
A beginner guide to mass spectrometry-based proteomics with project planning tips, workflow basics, report reading, and common mistakes to avoid.
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• Is Histone Acetylation Analysis Suitable for Clinical Samples?
Histone acetylation, an important epigenetic modification, plays a key role in gene expression regulation, cell proliferation and differentiation, and disease initiation and progression. With the rapid development of precision medicine and clinical biomarker research, an increasing number of research groups aim to apply histone acetylation analysis to clinical samples to explore its potential value in cancer, immune diseases, and neurodegenerative diseases. However, clinical samples are often characte......
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In eukaryotic chromatin, histones serve not only as structural proteins that package DNA but also as critical regulators of gene expression. H2B ubiquitination, an important epigenetic modification, exerts profound effects on chromatin architecture and transcriptional regulation through the covalent attachment of the small protein ubiquitin to lysine residues on histone H2B. This modification participates in transcription initiation and elongation while also influencing DNA damage repair, chromosomal ......
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• What Is Histone Lysine Succinylation?
Histone lysine succinylation is an emerging epigenetic modification that significantly influences chromatin architecture and gene transcription by introducing a negatively charged succinyl group onto histone lysine residues. This modification is closely linked to cellular metabolism and also plays critical roles in cancer, metabolic disorders, and immune regulation. With advances in mass spectrometry and immunoenrichment technologies, scientists can now detect Ksucc modification sites with high sensit......
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• Phage Immunoprecipitation Sequencing Service: How PhIP-Seq Profiles Antibody-Peptide Binding
A phage immunoprecipitation sequencing (PhIP-Seq) service profiles antibody-peptide binding by capturing antibody-bound, phage-displayed peptides and measuring which library members become enriched by sequencing.
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Multiple reaction monitoring (MRM), also called selected reaction monitoring (SRM) on some triple-quadrupole platforms, answers that question by measuring predefined precursor-to- product ion transitions for target peptides. The mass spectrometer selects a specific peptide ion in the first quadrupole (Q1), fragments it in the collision cell (Q2), and monitors one or more product ions in the third quadrupole (Q3).
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• What Determines N-Terminal Sequencing Cost? Sample Purity, Method Choice, and Sequence Length
Researchers planning N-terminal sequencing often ask for a single price before the sample and reporting goal are defined. That question is understandable. Grant budgets, vendor comparisons, and QC timelines all depend on cost predictability. However, terminal analysis is rarely sold as a fixed-price assay.
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• N-Terminal Sequencing Methods Compared: Edman Degradation vs Mass Spectrometry
Researchers who need N-terminal evidence often begin with a simple assumption: one assay should read the first residues and answer the question. In practice, the main N-terminal sequencing methods split into two major routes. Sequential Edman chemistry reads the protein terminus directly, one residue per cycle. MS-based approaches infer terminal sequence through intact mass measurement, terminal peptide identification, or LC-MS/MS analysis of selected fragments.
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