Protein Identification

Protein Identification

Proteomics

Product Overview

Protein identification is a one-stop scientific research service based on high-throughput liquid chromatography-tandem mass spectrometry (LC-MS/MS), following the classic bottom-up proteomics strategy, to accurately identify proteins in biological samples, perform sequence matching, post-translational modification analysis, species annotation, and functional analysis.

By enzymatically digesting complex protein mixtures into small molecule peptides, and acquiring precise mass-to-charge ratio and secondary fragment information via high-resolution mass spectrometry, combined with professional database retrieval and comparison, global qualitative and quantitative analysis of proteins is achieved, from single pure proteins, gel-separated proteins, and immunoprecipitation products to complex biological samples such as cells, tissues, and body fluids. This provides core data support for life science research, disease mechanism exploration, drug target discovery, and quality control of biological products.

This service enables precise identification of proteins, comparison of abundance differences, localization of modification sites, screening of interacting proteins, and structural and functional annotation. It is an indispensable basic supporting technology for fields such as proteomics, molecular biology, clinical medicine, agriculture, and food science.

Technical Process


Technical Process

High-resolution LC-MS/MS protein identification across multiple sample typesTechnical Workflowdiagram

Identifiable Sample Types

Gel dot/strip identification: Single protein identification of target protein bands/spots on SDS-PAGE gels, compatible with IP, Co-IP, and pull-down purification products.

Solution protein identification: Qualitative analysis of protein solutions, lyophilized powders, and crude protein extracts.

Target protein modification site identification: Identification and quantification of post-translational modification sites such as phosphorylation, glycosylation, acetylation, ubiquitination, and methylation.

Full-spectrum proteomics identification: Global protein identification in complex samples such as cells, tissues, and body fluids.

Technological Advantages

Ultra-high precision platform: High-resolution mass spectrometry such as TIMSTOF HT/ORBITRAP FUSION LUMOS, with resolution >10⁵, mass accuracy <1ppm, and result accuracy >99%.

No species restrictions: Compatible with all species including humans, animals, plants, microorganisms, and viruses.

Strong sample compatibility: Accepts various sample types such as gel strips, solutions, lyophilized powders, tissues, cells, body fluids, and FFPE sections.

Stable turnaround time: Basic identification takes 5-7 working days, and editing takes 7-10 working days.

Reliable results: Strict quality control, false positive rate <1%, providing complete raw data and reproducible analysis procedures.

After-sales support: Provides result interpretation, paper figure optimization, and experimental design consultation.

Sample Submission Requirements

Sample
Glue Strips/Dots
Specification
Codon staining/silver staining/fluorescent staining strips
Notes
clearly visible bands, avoid contamination
Sample
Protein Solutions
Specification
Total volume ≥ 2ug
Notes
please specify solution composition
Sample
Cells/Tissues
Specification
Cells ≥ 10^5,tissues ≥ 10mg
Notes
flash-frozen in liquid nitrogen or stored at -80℃

References

1. After IP treatment, silver staining is performed, and samples of the differential bands are cut and sent for testing.

IP, @2x.jpg

Reference Articles: W.-S. Wei, et al. TRIM65 supports bladder urothelial carcinoma cell aggressiveness by promoting ANXA2 ubiquitination and degradation, Cancer Letters (2018), doi: 10.1016/j.canlet.2018.07.036.

Reference: W.-S. Wei, et al. TRIM65 supports bladder urothelial carcinoma cell aggressiveness by promoting ANXA2 ubiquitination and degradation, Cancer Letters (2018), doi: 10.1016/j.canlet.2018.07.036.

2. After TAP staining, silver staining is performed, and the strip is cut and sent as a sample.

IP, 2@2x.jpg

Reference Articles: Zhang H-J, et al. (2018) Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation. PLoS Pathog 14(7): e1007208. https:// doi.org /10.1371 /journal.ppat. 1007208.

Reference : Zhang H-J, et al. (2018) Epstein-Barr virus activates F-box protein FBXO2 to limit viral infectivity by targeting glycoprotein B for degradation. PLoS Pathog 14(7): e1007208. https:// doi.org /10.1371 /journal.ppat. 1007208.

IP, 3@2x.jpg

Reference Articles: Teng, Kai et al. “KIFC1 is activated by TCF-4 and promotes hepatocellular carcinoma pathogenesis by regulating HMGA1 transcriptional activity.” Journal of experimental & clinical cancer research : CR vol. 38,1 329. 24 Jul. 2019, doi:10.1186/s13046-019-1331-8

Reference: Teng, Kai et al. "KIFC1 is activated by TCF-4 and promotes hepatocellular carcinoma pathogenesis by regulating HMGA1 transcriptional activity." Journal of experimental & clinical cancer research : CR vol. 38,1 329. 24 Jul. 2019, doi:10.1186/s13046-019-1331-8

IP, 4@2x.jpg

Reference Articles: Yang, Min-Hui et al. “Nuclear lncRNA HOXD-AS1 suppresses colorectal carcinoma growth and metastasis via inhibiting HOXD3-induced integrin β3 transcriptional activating and MAPK/AKT signalling.” Molecular cancer vol. 18,1 31. 1 Mar. 2019, doi:10.1186/s12943-019-0955-9

Reference: Yang, Min-Hui et al. "Nuclear lncRNA HOXD-AS1 suppresses colorectal carcinoma growth and metastasis via inhibiting HOXD3-induced integrin β3 transcriptional activating and MAPK/AKT signaling." Molecular cancer vol. 18,1 31. 1 Mar. 2019, doi:10.1186/s12943-019-0955-9

Shenzhen Wininnovate Bio Co., Ltd.

Innovative mass spectrometry and AI technologies provide protein and metabolite mass spectrometry multi-omics solutions for life science research, empowering the growth of the biotechnology, pharmaceutical, and healthcare industries.

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