The new edition of our “Analytical Sciences, Synthesis & Purification” catalog is available now! Offering a full suite of innovative products and technologies from Advion Interchim Scientific, this catalog features over 20,000 products ranging from consumables and reagents to instrumentation.
Not only a product resource, the catalog features in-depth scientific information to improve your daily workflow, including sample preparation tips and tricks, analysis technologies such as GC and LC/MS, and help selecting the best consumables for your workflow or purification.
Take advantage of this extensive guide to boost your lab with:
The Advion Interchim Scientific suite of systems and consumables allows users to harness the power of mass spectrometry, flash chromatography, prep LC and more. Simple and robust, download our brochure to learn more about:
The Advion Interchim Scientific expression® compact mass spectrometer (CMS): A fast and easy analytical tool for the organic chemist. Ideal for fast reaction monitoring, the expression® CMS features a single quadrupole that can adapt to multiple ionization sources in seconds, including both ESI and APCI. The expression® CMS offers a variety of novel sampling techniques, including fast assay methods for liquids, solids, gases, and even air-sensitive compounds.
Direct mass analysis of TLC plates in 30 seconds at the push of a button with Plate Express™
One-touch analysis of solids and liquid samples with the ASAP® probe
puriFlash® ultra performance flash purification: Ideal for method development and purification of rare and high added value compounds, the Interchim family of puriFlash® systems offer users a wide range of throughput options and the highest recovery rates at >95%.
Mass-Guided Purification: the Interchim puriFlash® + Advion CMS offers the ideal solution for Flash-MS, and can provide fraction identification in <30 seconds.
Fill out the form to download the full Advion Interchim Scientific brochure now.
The TriVersa NanoMate® LESA® is the latest in chip-based electrospray ionization technology from Advion Interchim Scientific®. It combines the benefits of liquid chromatography, mass spectrometry, chip-based infusion, fraction collection and direct surface analysis into one integrated ion source platform. It allows scientists to obtain more information from complex samples than LC/MS alone.
One of the benefits of nanoelecrtospray ionization (nanoESI) is the reported optimal ionization efficiency (equalized response) of chemically different analyses despite the presence of matrix components. However, outside of a very low flow rate of ca. 1-20 nL/min, the ionization efficiency drops exponentially and coupling higher flow rates from a typical liquid chromatography (LC) system to ESI loses most of the benefits such as enhanced sensitivity and reduced ion suppression in mass spectrometry analysis (LC/ESI/MS). The Advion silicon-based ESI Chip accommodates micro flow LC/MS applications at ionization efficiencies near optimal levels and comparable to nanoelectrospray ionization (nanoESI).
ChipSoftX is an entirely new operating software for the TriVersa NanoMate automated nanoelectrospray source. Besides improvement in program compatibility with Windows and integration of existing software features, it also provides access to the new Developers Kit – a platform for customized method development with direct access to robot controls allowing entirely novel analysis workflows such as LESAPLUS.
Our goal is to provide the research community at IRB Barcelona and their co-workers with state-of-the-art tools and methodologies for the MS analysis of a broad range of biological species, from large proteins and DNA to small molecules. The final purpose is to get insight into these molecules’ identity, structure, interaction with other molecules and biological function in order to help in drug design, protein mechanism elucidation and in the search for biomarkers. We have implemented methods specialized in top-down proteomics and we are pioneers in this MS strategy in Spain.
As a core facility, we are responsible for working with different biologic molecules, and we are required to change methods constantly and efficiently.
How does the TriVersa NanoMate® align with your research goals?
Originally, we purchased the TriVersa NanoMate® for its chip-based direct infusion mode for noncovalent interaction analysis, but we learned quickly that it could be applied to other areas of our research. Prior to using the TriVersa NanoMate®, the steps involved in collecting fractions were painful and time-consuming. With the TriVersa NanoMate®, we can run LC/fraction collection or infusion without changing the setup and wasting time with stabilization. We do not experience the problems typical with traditional nanoelectrospray sources.
One aspect of the TriVersa NanoMate® that impressed us was the ability to analyze complicated top-down samples with the LC compatibility. It is not possible to analyze these samples on an LC time scale, and the fraction collection capability allowed us to analyze in a way that was not possible previously.
To whom would you recommend the TriVersa NanoMate® for their research?
We use the TriVersa NanoMate® for everything; noncovalent interactions, top-down, middle-down, bottom-up, basic infusion, LC coupled to fraction collection. The instrument is useful in all of its different set-ups, especially without having to change sources and waiting for a stable spray.
The reliability of the system is one of the greatest benefits especially for people who have to change frequently between applications. We have found the spray sensing feature to be very valuable because we know our precious samples will not be lost.
Do you have any publications or presentations using the TriVersa NanoMate®?
Characterization of Human Sperm Protamine Proteoforms Through a Combination of Top-Down and Bottom-Up Mass Spectrometry Approaches Soler-Ventura et al. J Proteome Res, 2020, 19(1), 221-237. DOI: 10.1021/acs.jproteome.9b00499
Identified the sperm protamine proteoforms profile, including their post-translational modifications, in normozoospermic individuals using a top-down MS approach and a proteinase-K-digestion-based bottom-up MS approach.
Arauz-Garofalo et al. Protamine characterization by top-down proteomics: Boosting proteoform identification with DBSCAN. Proteoms, 2021. DOI: 10.3390/proteomes9020021
Yero et al. The Pseudomonas aeruginosa substrate-binding protein Ttg2D functions as a general glycerophospholipid transporter across the periplasm. Comm Bio, 2021. DOI: 10.1038/s42003-021-01968-8
Molnar et al. The histone code reader PHD finger protein 7 controls sex-linked disparities in gene expression and malignancy in Drosophila. Sci Adv, 2019. DOI: 10.1126/sciadv.aaw7965
Nadal et al. Structure of the homodimeric androgen receptor ligand-binding domain. Nat Commun, 2017. DOI: 10.1038/ncomms14388
Testoni et al. Lack of glycogenin causes glycogen accumulation and muscle function impairment. Cell Metabolism, 2017. DOI: 10.1016/j.cmet.2017.06.008
Izquierdo-Serra et al. Optical control of endogenous receptors and cellular excitability using targeted covalent photoswitches. Nat Commun, 2016. DOI: 10.1038/ncomms12221
Pujol-Pina et al. SDS-PAGE analysis of Aβ oligomers is disserving research into Alzheimer’s disease: Appealing for ESI-IM-MS. Sci Rep, 2015. DOI: 10.1038/srep14809
Saez et al. Influence of PPh3 moiety in the anticancer activity of new organometallic ruthenium complexes. J Inorg Biochem, 2014. DOI: j.jinorgbio.2014.03.002
Borg et al. Spectral counting assessment of protein dynamic range in cerebrospinal fluid following depletion with plasma-designed immunoaffinity columns. Clin Proteomics, 2011. DOI: 10.1186/1559-0275-8-6
A: One of the topics of our lab is the interaction of insect pheromones and their analogues with pheromone-binding proteins (PBPs) which are part of an extremely sensitive multi-component pheromone detection system.
We utilize binding assays to determine the function of the PBPs through affinity measurements of the protein-ligand receptors, calculate binding constants, the spatial arrangement of the complex and do modeling. In addition, point-mutated PBPs are used for a better understanding of the contribution of individual amino acids to the binding event.
Q: How does the TriVersa NanoMate® (TVNM) align with your research goals?
A: The TVNM enabled us to develop a high-throughput method to study protein-ligand-interactions for large series of different pheromones and their analogues.
As the binding energies involved are very low and we need to preserve the native structure of the molecules, the soft-ionization conditions of the TVNM are perfect for us. Further, these studies are difficult with classic electrospray, due to the stickiness of the samples. They create problems from short cleaning cycles and produce contaminations.
In contrast, the established method with the TVNM is reliable and stable, and it eliminates the sticky sample issues. In addition, multiple experiments with very low quantities of protein (1 nmol) at different cone-voltage conditions are possible.
We recently added the LESA™ (Liquid Extraction Surface Analysis) capability to the TVNM. This enables us to detect putative signal molecules on leaf surfaces and to track down their production and storage sites by comparing the data with extracts from samples derived from the inner compartments of the leaves.
Q: To whom would you recommend the TriVersa NanoMate for their research?
A: I would recommend the TriVersa NanoMate to everybody because it is a universal source. With direct infusion, coupling for fraction collection and surface analysis, it may replace all ionization sources.
Description: Obtaining extended sequence coverage of intact proteins and characterizing multiple post-translational modification (PTM) sites can pose key technical challenges. In this webinar, we describe how we have implemented Advion’s TriVersa NanoMate® and RePlay® technologies to address these issues using an integrated top-down/bottom-up approach.
We demonstrate how the TriVersa NanoMate’s capabilities of chip-based electrospray ionization (ESI) and fraction collection are used to profile isoforms, further investigate targeted proteins at the intact level using ECD or CID, perform bottom-up proteomics on a collected fraction to get confident protein identifications, perform targeted MS/MS on particular fractions of interest, and better characterize where PTMs may have occurred.
We also discuss how RePlay simplifies the data analysis process by allowing you to see the correlation between the intact protein and the observed peptides, even when you are sample limited. Using RePlay, we incorporated an on-line digestion strategy with the integrated top-down/bottom-up approach. This technique allows you to implement LC-MS/MS during both the intact run and a secondary RePlay run with digestion, so you can see the correlation in time between the observed parent ions and the digested ions as well as the MS/MS of the fragment ions.