Enhanced Diagnostic Tools
Mass spectrometry can be used for analysis of small molecules, oligonucleotides, lipids, glycans, proteins, peptides and determining the location of post translational modifications. It offers accuracy of measurement over a wide molecular weight range, as small as sub-picomole, sample consumption. Furthermore, any difference between theoretical and measured mass may provide important information about the primary structure and post-translational modifications of a therapeutic protein product.
Mass spectrometery is used for the analysis of macromolecules originating from biological sources, such as proteins, peptides, DNA or RNA oligomers. Instrumentation of mass analysis has experienced tremendous improvements in recent years. Electrospray-ionization mass spectrometry (ESI-MS) and matrix assisted laser desorption time-of-flight mass spectrometry (MALDI-TOF MS) have become the methods of choice for the analysis of pharmaceuticals and biosimilars. Both techniques are powerful analytical tools by themselves, but are most powerful if used in combination with techniques such as gel electrophoresis, electro-blotting, liquid chromatography (LC), capillary electrophoresis (CE) and/or protein sequencing. These two techniques are now the major technologies used in metabolomics and proteomics.
Bio-Synthesis' mass spectrometry services uses industry-leading technologies—instruments, chemistry, software, and quantification tools -- that are specifically optimized for exceptional, application-focused performance. This end-to-end system is designed to deliver the fast and reliable quality control methods for your proteins and peptides.
Please contact us to discuss your specific project in more detail. We will provide you with a full project proposal within 2 days that includes analysis protocols, timelines, and costs.
Identify and QA your protein/peptide by MS starting at $250
Price subject to change based on project specifications. Contact us for services and fees not listed below.
Data quality is ensured through the use of appropriate internal and external standards. The MALDI-TOF mass spectrometers are calibrated with external standards that vary depending on the analyte molecular weight. This results in the best calibration for the most accurate mass assignments. Samples that have been trypsin digested are internally recalibrated from observed trypsin autolysis fragments. The electrospray mass spectrometers are calibrated using polyalanine which allows for even distribution of multiple mass peaks. A variety of search engines, for protein identification from mass fingerprinting and for interpretation of MS/MS spectra, are available each of which generates its own statistics. The choice of database searching software to be applied is optional to investigators and discussion of this matter is encouraged with our technical support team.
Prior to sending samples, investigators are recommended to contact the facility to discuss the required analysis. This is necessary to ensure that the most efficient and cost-effective analytical methods are employed. Samples are normally analyzed in the order of their receipt, but special arrangements can be made for unstable samples. A sample submission form and guidelines should accompany each set of samples.
When preparing samples for mass spectrometric analysis, it is best to limit sample manipulations. When dealing with solution samples, never bring the sample to complete dryness. Salts and detergents will interfere with MS analysis of solution samples. Based on extensive studies, we have found that SDS-PAGE or 2D IEF-SDS-PAGE is the best method for recovery of low quantities of protein.
Please provide amounts of 1 to 3 µgs and higher per oligonucletide, peptide or protein in lyophylized as a dry powder form. If possible ship sample frozen in aqueous solution containing volatile buffers. If this is not possible an additional sample handling step may be needed.
Protein/peptide solutions in 10 μM volatile buffers can sometimes be analyzed directly while samples with higher salt concentrations require prior C18 or C4 ZipTip desalting.