1. What platform do you use for MS-based quantitative proteomics?
Our quantitative proteomics workflows are powered by the Bruker timsTOF HT platform, which combines TIMS (Trapped Ion Mobility Spectrometry) with PASEF (Parallel Accumulation Serial Fragmentation) to achieve ultra-high sensitivity, resolution, and throughput. It enables 4D proteome analysis with excellent depth and precision.
2. What’s the difference between DIA and DDA in quantitative proteomics?
DIA (Data-Independent Acquisition) fragments all detectable precursor ions in a systematic, unbiased manner, resulting in higher reproducibility, improved quantitation accuracy, and greater coverage across samples. It is ideal for comparative and large-scale studies.
DDA (Data-Dependent Acquisition) selectively fragments the most intense precursor ions, making it effective for exploratory research but more prone to missing low-abundance proteins and variability between runs.
3. DDA vs DIA proteomics: which acquisition mode is better for quantitative proteomics?
DDA (data-dependent acquisition) is ideal for discovery-oriented studies that prioritize broad protein identification and deep proteome coverage, making it a strong option for pilot projects and hypothesis generation. DIA (data-independent acquisition) consistently fragments all peptides within defined m/z windows, delivering higher quantitative completeness, fewer missing values, and better reproducibility across large cohorts. In practice, DDA is often selected for exploratory profiling, while DIA is preferred for robust label-free quantification (LFQ) in large-scale or clinically oriented studies where cross-sample comparability is critical.
4. Do you offer TMT or iTRAQ labeled proteomics?
Currently, we do not offer TMT-labeled or iTRAQ-labeled proteomics. Instead, we specialize in label-free quantitative proteomics, which avoids issues like ratio compression, sample mixing artifacts, and labeling cost. Label-free methods are more flexible for handling large sample sizes and diverse sample types without requiring chemical labeling, while still delivering high-quality quantitative results using advanced mass spectrometry and statistical normalization.
5. Do you remove high-abundance proteins in blood proteomics (plasma/serum)?
Yes. Plasma and serum are dominated by a small set of high-abundance proteins that can mask low-abundance biomarkers and limit LC–MS/MS proteome depth. To improve sensitivity and coverage, Blood DIA includes high-abundance protein reduction using a robust magnetic bead-based workflow that enriches low-abundance proteins with strong reproducibility across cohorts. With this strategy, Blood DIA typically enables identification of 4,000+ proteins from plasma or serum while maintaining consistent label-free quantification.
6. What is the minimum sample amount required for low-input proteomics?
Our Low-Input DIA proteomics workflow is highly optimized for trace samples. We can perform reliable quantitative analysis from as little as 1 mg of tissue, 1 µL of blood, 10 oocytes, or 10,000 mammalian cells, enabling protein profiling even in highly limited experimental scenarios.
7. Do your quantitative proteomics services accept IP-enriched samples or gel-based samples?
Yes. Quantitative proteomics can be performed on IP-enriched eluates as well as gel bands, gel spots, and gel slices. To maximize compatibility and recovery, workflows support on-bead digestion for magnetic bead and in-gel digestion for gel-separated proteins, enabling reliable LC–MS/MS-based proteome profiling from non-standard sample formats.
8. How do you ensure data quality and reproducibility in proteomics analysis?
We implement comprehensive quality control (QC) measures at every stage of the workflow. This includes internal standards such as iRT peptides, reference samples like HeLa cell lysate, and mixed peptide/protein QC pools. These controls help monitor system performance, retention time alignment, and quantification consistency to ensure reliable, reproducible results across batches and projects.
9. How should proteomics samples be prepared, stored, and shipped for quantitative LC–MS/MS analysis?
For best quantitative proteomics performance, samples should be collected using clean, protein-compatible reagents and processed quickly to minimize degradation. Snap-freeze tissues or cell pellets whenever possible and store at −80°C, avoiding repeated freeze–thaw cycles. For biofluids (plasma/serum), clarify by centrifugation, aliquot, and freeze promptly. Avoid detergents and additives that interfere with LC–MS/MS (e.g., SDS, high salt, excessive glycerol, and nucleic acids); if lysis buffers are used, choose MS-compatible formulations or discuss buffer exchange/cleanup options in advance. Ship samples on dry ice with sealed, clearly labeled tubes to maintain sample integrity.
10. What is the typical turnaround time?
Turnaround time varies depending on the project scope, but standard proteomics services typically require 4–6 weeks from sample receipt to data delivery. Express options may be available upon request.