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Workflow Kits

HRM Calibration Kit

Next generation targeted proteomics technology

Calibration peptides for HRM-MS™ (SWATH, DIA) for fully automated high-throughput data processing with Spectronaut™ software.
 

Product number: Ki-3003

USD

595.00

In stock

Hyper Reaction Monitoring Mass Spectrometry (HRM-MS™) is the next generation targeted proteomics technology invented at Biognosys that enables reproducible and precise quantification of 1000s of proteins in a single instrument run with data independent acquisition (DIA, SWATH). Spectronaut™ software in combination with the HRM Calibration Kit enables fully automated and accurate signal processing of HRM-MS™ data sets.

The HRM Calibration Kit, containing non-naturally occurring synthetic peptides in a pooled mix, serves to calibrate retention time and other parameters for the Spectronaut™ software enabling peak detection, scoring, mass calibration, noise reduction and other data analysis steps. 

The use of the HRM Calibration Kit translates into better results:

  • Smart in-run parameter calibration guarantees quick and robust analysis
  • Increased sensitivity and specificity by iRT normalization and advanced handling of interfering signals
  • High quantitative accuracy by supporting optimized ion current extraction
  • Automated quality control by monitoring LC and MS performance

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The HRM Calibration Kit contains

  • HRM Peptide Mix (2x 2.0 ml tube)
  • Dissolution Buffer (2x 2.0 ml tube)

The kit components are sufficient for approximately 1000 injections (or 100 samples) depending on sample volume and injection amount.

Using the HRM Calibration Kit requires just one step: Pipet the HRM Peptide Mix into your sample directly before measurement – everything else is handled by Spectronaut™ software. Spectronaut™  automatically detects the HRM peptides and reports successful calibration only if the HRM peptides are detected in the sample.
 

Supported instruments

  • Thermo Scientific™ Q Exactive™ Series
  • Thermo Scientific™ Orbitrap Fusion™ Series
  • AB SCIEX TripleTOF® Series (5600, 5600+, 6600)

If your instrument is not on the list please contact us to get detailed information on the instruments we support.

See the Quick Reference Card for detailed information on how to use the HRM Calibration Kit.

Please contact us for support.

Please contact us for support.

Visit Science Hub to access all scientific and technical content (publications, videos, application notes, posters and more) related to Biognosys technology, products and services.

Peer-Reviewed Papers

  1. Bruderer R, Sondermann J, Tsou CC, Barrantes-Freer A, Stadelmann C, et al. New targeted approaches for the quantification of data-independent acquisition mass spectrometry. Proteomics. 2017 Mar 20.
  2. Fabre B, Korona D, Nightingale DJ, Russell S, Lilley KS. SWATH-MS data of Drosophila melanogaster proteome dynamics during embryogenesis. Data Brief. 2016; 9:771-775. 
  3. Fabre B, Korona D, Nightingale DJ, Russell S, Lilley KS. SWATH-MS dataset of heat-shock treated Drosophila melanogaster embryos. Data Brief. 2016; 9:991-995.
  4. Boominathan A, Vanhoozer S, Basisty N, Powers K, Crampton AL, Wang X, et al. Stable nuclear expression of ATP8 and ATP6 genes rescues a mtDNA Complex V null mutant. Nucleic Acids Res. 2016; 44(19):9342-9357.
  5. H TV, Cuauhtemoc LC, Nidia MC, Alba RR, Sara CL, Esteban M, et al. Deletion of the hypothetical protein SCO2127 of Streptomyces coelicolor allowed identification of a new regulator of actinorhodin production. Appl Microbiol Biotechnol. 2016;100(21):9229-9237.
  6. Vowinckel J, Zelezniak A, Kibler A, Bruderer R, Muelleder M, Reiter L, Ralser M. Precise label-free quantitative proteomes in high-throughput by microLC and data-independent SWATH acquisition. bioRxiv Sep 5.
  7. Bruderer R, Bernhardt OM, Gandhi T, Reiter L. High-precision iRT prediction in the targeted analysis of data-independent acquisition and its impact on identification and quantitation. Proteomics. 2016; 16(15-16): 2246-56.
  8. Rouwette T, Sondermann J, Avenali L, Gomez-Varela D, Schmidt M. Standardized Profiling of The Membrane-Enriched Proteome of Mouse Dorsal Root Ganglia (DRG) Provides Novel Insights Into Chronic Pain. Mol Cell Proteomics. 2016; 15(6):2152-68.
  9. Fabre B, Korona D, Groen A, Vowinckel J, Gatto L, Deery MJ, Ralser M, Russell S, Lilley KS. Analysis of the Drosophila melanogaster proteome dynamics during the embryo early development by a combination of label-free proteomics approaches. Proteomics. 2016 Mar 31.
  10. Bongers M, Chrysanthopoulos PK, Behrendorff JB, Hodson MP, Vickers CE, Nielsen LK. Systems analysis of methylerythritol-phosphate pathway flux in E. coli: insights into the role of oxidative stress and the validity of lycopene as an isoprenoid reporter metabolite. Microb Cell Fact. 2015; 14(1):193.
  11. Villeneuve LM, Purnell PR, Stauch KL, Fox HS. Neonatal mitochondrial abnormalities due to PINK1 deficiency: Proteomics reveals early changes relevant to Parkinson׳s disease. Data Brief. 2015; 6:428-342.
  12. Villeneuve LM, Purnell PR, Boska MD, Fox HS. Early Expression of Parkinson's Disease-Related Mitochondrial Abnormalities in PINK1 Knockout Rats. Mol Neurobiol. 2016; 53(1):171-186.
  13. Haverland NA, Villeneuve LM, Ciborowski P, Fox HS. The Proteomic Characterization of Plasma or Serum from HIV-Infected Patients. Methods Mol Biol. 2016; 1354:293-310.
  14. Campbell K, Vowinckel J, Keller MA, Ralser M. Methionine metabolism alters oxidative stress resistance via the pentose phosphate pathway. Antioxid Redox Signal. 2015 Nov 23.
  15. Muntel J, Xuan Y, Berger ST, Reiter L, Bachur R, Kentsis A, Steen H. Advancing Urinary Protein Biomarker Discovery by Data-Independent Acquisition on a Quadrupole-Orbitrap Mass Spectrometer. J Proteome Res. 2015 Oct 22. 
  16. Bilbao A, Zhang Y, Varesio E, Luban J, Strambio-De-Castillia C, Lisacek F, Hopfgartner G.Ranking Fragment Ions Based on Outlier Detection for Improved Label-Free Quantification in Data-Independent Acquisition LC-MS/MS. J Proteome Res. 2015 Oct 14. 
  17. Krautkramer KA, Reiter L, Denu JM, Dowell JA. Quantification of SAHA-Dependent Changes in Histone Modifications Using Data-Independent Acquisition Mass Spectrometry. J Proteome Res. 2015; 14(8):3252-62. 
  18. Bilbao A, Varesio E, Luban J, Strambio-De-Castillia C, Hopfgartner G, Müller M, Lisacek F. Processing strategies and software solutions for data-independent acquisition in mass spectrometry. Proteomics. 2015; 15(5-6):964-80.
  19. Bruderer R, Bernhardt OM, Gandhi T, Miladinovic SM, Cheng LY, Messner S, et al. Extending the limits of quantitative proteome profiling with data-independent acquisition and application to acetaminophen treated 3D liver microtissues. Mol Cell Proteomics. 2015 May;14(5):1400-10.
  20. Selevsek N, Chang CY, Gillet LC, Navarro P, Bernhardt OM, Reiter L, et al. Reproducible and consistent quantification of the Saccharomyces cerevisiae proteome by SWATH-MS. Mol Cell Proteomics. 2015.
  21. Orellana CA, Marcellin E, Schulz BL, Nouwens AS, Gray PP, Nielsen LK. High-Antibody-Producing Chinese Hamster Ovary Cells Up-Regulate Intracellular Protein Transport and Glutathione Synthesis. J Proteome Res. 2015.
  22. Westman J, Smeds E, Johansson L, Mörgelin M, Olin AI, Malmström E, Linder A, Herwald H. Treatment with p33 Curtails Morbidity and Mortality in a Histone-Induced Murine Shock Model. J Innate Immun. 2014.
  23. Liu Y, Hüttenhain R, Collins B, Aebersold R. Mass spectrometric protein maps for biomarker discovery and clinical research. Expert Rev Mol Diagn. 2013;13(8):811-25.
  24. Vowinckel J, Capuano F, Campbell K, Deery MJ, Lilley KS, Ralser M. The beauty of being (label)-free: sample preparation methods for SWATH-MS and next-generation targeted proteomics. F1000Research 2013, 2:272.
If we forgot to include your publication that uses our technology, please don’t hesitate to let us know at info@biognosys.com.

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What does iRT stand for?

iRT is stands for indexed retention time. It is a dimensionless value that allows the transferring of retention time information of a peptide to different chromatographic set ups. 

What are iRT peptides?

iRT peptides are 11 non-naturally occurring chemically synthesized peptides that are used in the next generation proteomics workflows to accurately calculate the indexed retention time of peptides on a chromatographic set up. 

Why is it beneficial to add the iRT peptides to all my samples?

Apart from predicting the retention time the iRT peptides are used for mass calibration and QC monitoring of the LC-MS set up. In an HRM-MS experiment the iRT or HRM peptides are further used as anchor points for the data analysis. 

What is the difference between the iRT peptides and the HRM calibration peptides?

On top of the 11 peptides in the iRT kit the HRM calibration kit contains additional peptides. These are used in the older versions of Spectronaut. With the new algorithm of SN 9 the HRM peptides are no longer a requirement and can be replaced with the iRT peptides if desired. This has the advantage that only one set of peptides are required for customers using all three next-generation proteomics workflows offered by Biognosys. 

Do I really need to add the iRT peptides to all my runs because they make the per sample costs higher?

As of Spectronaut 9 the iRT peptides are not required in all cases for the samples used for spectral library generation. Yet, we strongly advise using them as in seldom cases spectral library generation can fail without them. For all DIA runs the peptides are required by the software. Adding the iRT peptides to the sample increase the per sample costs by less than 1% (~30cents/sample). Further, the dilution can be optimized on the newest generation of mass spectrometers to further reduce the per run cost additions.

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