Biomarker Research
Our fast, antibody-free and scalable services and can be applied at all research stages, from biomarker discovery and validation to routine measurements.
PolyQuant’s experienced professionals assist at every stage of the project, starting from the identification of biomarker candidate proteins through discovery proteomics to quantitative validation of the biomarker panel using our QconCAT reference standards.
Background
Disease-related biomarkers allow diagnosis, monitoring of disease progression in response to treatment and prediction of disease occurence. Thousands of disease associated proteins have already been described. It is also acknowledged that no single molecule characterizes malignant state but protein profiles, also named biomarker panels.
These biomarker panels usually consist of 5 to 50 protein candidates and multiplexing tests are essential for their validation.
The Challenge
Development of antibody-based biomarker assays still remains expensive and time consuming and most of them are generated to measure 1-5 proteins. Additionally, the target proteins need to be known and the resulting antibodies need to be thoroughly tested to exclude cross-reactivity. Genetic tests are fast but do not provide quantitative information or information about post-translational modifications, isoforms generated by alternative splicing….
The Solution
Proteomics employing mass spectrometry facilitates much faster identification and validation of new biomarker candidates, even at low levels. Furthermore, it is possible to identify post-translational modifications, to quantitatively evaluate protein expression and even to distinguish between isoforms.
From discovery to validation
Mass spectrometry enables highly specific biomarker detection and validation. We offer consulting and support and full services performed by experienced professionals.
Individual service
Receive customized proteomics services with clear timelines, milestones, deliverables and detailed reporting.
Support
Our experienced team provides consulting and support at every stage of the project.
Scalable
From exploratory studies to routine measurements and high throughput analyses.
High sensitivity
Stable, accurate and sensitive protein analysis with high-end instruments
Antibody-free
Fast method setup by unbiased, antibody-independent protein detection.
Reliable
Validate identified biomarkers using targeted LC-MS/MS, supported by our proprietary QconCAT technology
Contact us now:
Discuss your requirements with our experienced professionals.
E-Mail: info[at]polyquant.com
Phone: +49 (0)9405 96999 10
Fax: +49 (0)9405 96999 28
References
Targeted LC-MS/MS for the evaluation of proteomics biomarkers in the blood of neonates with necrotizing enterocolitis and late-onset sepsis
Chatziioannou AC, et al.,
Anal Bioanal Chem. 2018 Nov;410(27):7163-7175. [Pubmed]
Chatziioannou et al. used QconCATs and synthetic peptides belonging to 47 protein markers for a prospective case-control study evaluating serum proteomics profiles. They were able to define two panels of three proteins each that allow highly sensitive diagnosis of late-onset sepsis (LOS) and differential diagnosis between LOS and necrotizing enterocolitis.
A family of QconCATs (Quantification conCATemers) for the quantification of human pharmacological target proteins
Vasilogianni AM, et al.,
J Proteomics. 2022 Jun 15;261:104572. [Pubmed]
In this report, the authors describe the development and characterization of two QconCAT constructs for quantification of 24 enzymes and 21 receptor tyrosine kinases (RTKs), complementing two previously reported QconCATs for the quantification of key enzymes and drug transporters. The QconCATs were successfully applied in quantification of target proteins in human liver.
Stoichiometry, Absolute Abundance, and Localization of Proteins in the Bacillus cereus Spore Coat Insoluble Fraction Determined Using a QconCAT Approach
Stelder SK, et al.,
J Proteome Res. 2018 Feb 2;17(2):903-917 [Pubmed]
Stelder et al. quantified crucial spore proteins using a QconCAT reference standard, determining the absolute abundance of 21 proteins, covering approx. 5.66% of the total spore weight in wild type and approx. 4.13% in the ΔCotE mutant.
Rigorous determination of the stoichiometry of protein phosphorylation using mass spectrometry
Johnson H, et al.,
Journal of the American Society for Mass Spectrometry 2009 Dec;20(12):2211-20. [PubMed]
Johnson et al. use QconCATs to determine absolute protein concentrations and the stoichiometry of phosphorylation at predefined sites.