Resources

Proteomics Databases



Metabolomics Databases

• • How to Choose the Right Method for Host Cell Protein Detection?

  In the research, development, and manufacturing of biopharmaceuticals, recombinant protein expression systems represent a fundamental enabling technology. A consequential challenge is the presence of host cell proteins (HCPs), a category of process-related impurities that must be stringently controlled. HCPs are endogenous proteins released from production host cells during expression, cell lysis, and cultivation. Although typically present only at trace levels in the final product, their potential ........

• • Challenges and Innovations in Membrane Protein Structure Determination

  Membrane proteins act as the communication hubs and molecular conduits between cells and their external environment, playing pivotal roles in signal transduction, ion transport, and molecular exchange. They account for over 60% of known drug targets and represent central subjects in drug discovery, bioengineering, and vaccine design. With recent advancements, membrane proteins are no longer considered inaccessible to structural biology. Breakthroughs in cryo-electron microscopy (Cryo-EM), coupled with .....

• • How to Perform High-Throughput Proteomics Analysis of Lactylation Modifications?

  Protein lactylation represents a novel mechanistic link between lactate metabolism and epigenetic regulation. With growing interest in its roles in immunometabolism, stem cell differentiation, and the tumor microenvironment, there is an urgent need to establish a systematic, high-throughput platform for detecting lactylation modifications, enabling precise characterization of their modification landscapes and dynamic changes. However, inherent technical challenges, such as low abundance, weak specificity...

• • What Is Phosphoproteomics?

  Phosphoproteomics is a critical subdiscipline of proteomics dedicated to the systematic investigation of protein phosphorylation within cells or tissues. Phosphorylation, one of the most prevalent and significant post-translational modifications (PTMs), involves the covalent attachment of a phosphate group to specific amino acid residues, typically serine (Ser), threonine (Thr), or tyrosine (Tyr), catalyzed by kinases. This modification regulates protein activity, structural conformation, subcellular ......

• • What Is A Disulfide Bond in Proteins?

  In the realm of protein science, the disulfide bond, although formed simply by a linkage between two sulfur atoms, plays a critical role in maintaining both the structural integrity and the functional activity of proteins. This article provides an in-depth scientific examination of disulfide bonds in proteins, aiming to elucidate the nature of this subtle yet essential covalent structure. Definition of a Disulfide Bond A disulfide bond is a covalent linkage formed between the sulfur atoms (–SH groups) of...

• • How to Efficiently Conduct Olink Proteomics?

  In biomarker discovery, clinical cohort investigations, and pharmaceutical development, the Olink proteomics platform, based on Proximity Extension Assay (PEA) technology, offers reliable data support with minimal sample input, high sensitivity, and substantial high-throughput capacity. To ensure both research efficiency and data reliability, research teams must make informed decisions at multiple stages, including study design, experimental execution, and data analysis. This article systematically ........

• • How to Choose the Appropriate Strategies for Ubiquitinated Protein Enrichment?

  Ubiquitination, a key reversible post-translational modification of proteins, plays a central role in various biological processes, including cell cycle regulation, protein degradation, DNA damage repair, and signal transduction. The comprehensiveness and precision of ubiquitination research are often contingent upon the use of efficient and highly selective ubiquitinated protein enrichment strategies. Requirements for these strategies vary considerably depending on the experimental objectives, sample .....

• • What Is CUT&Tag? Principles, Workflow, and Advantages Explained

  In recent years, the exploration of chromatin states has transitioned from ChIP-seq to more sensitive and efficient approaches. Among these, Cleavage Under Targets and Tagmentation (CUT&Tag) has gained significant prominence due to its high sensitivity, low background noise, and compatibility with high-throughput applications, making it a preferred technique in the field of chromatin epigenetics. This review provides a comprehensive examination of the principles, experimental workflow, and advantages of....

• • What Is Non‑Degradative Ubiquitination?

  In eukaryotic cells, ubiquitination represents a pivotal post-translational modification whereby the small protein ubiquitin is covalently conjugated to substrate proteins, thereby modulating their stability, activity, subcellular localization, and interaction networks. While the canonical and most extensively characterized role of ubiquitination is to direct proteins toward proteasomal degradation, typically via K48-linked polyubiquitin chains in the 26S proteasome pathway, accumulating evidence has ......

• • How Different Enrichment Strategies Impact Acetylated Protein Detection: A Comparative Review

  Protein acetylation, a crucial post-translational modification in eukaryotes, plays a pivotal role in regulating diverse biological processes, including gene expression, metabolic homeostasis, and cell cycle progression. In recent years, advances in mass spectrometry have significantly deepened acetylome research. However, because acetylation events often occur at low abundance, direct detection by mass spectrometry is frequently hindered by signal suppression from high-abundance proteins. Consequently.....