GEN-MKT-18-7897-A
Oct 1, 2019 | Blogs, Software, Technology | 0 comments
As a researcher in a busy lab, the software driving your work is critical to your success, and the timely transition of SCIEX applications to Windows 10 is no exception. In early 2020 Microsoft will be ending Windows 7 support, and we want you to know we are taking every effort to ensure our software applications are up to date in advance of this deadline.
Why Are We Offering Windows 10 Software Application Compatibility?Computer manufacturers like Dell will not be able to ship Windows 7 compatible computers beyond the end of 2018. The reason being, they are having trouble locating components that have Windows 7 compatible drivers. New devices are already being shipped with Windows 10, and we don’t want to hold you back. Therefore, to ensure technological flexibility across your organization, we are offering application support changes now rather than later.
What SCIEX Software Platforms Are Compatible?Migrating to Microsoft’s latest operating system is essential in making sure your laboratory stays relevant and current. This move can present a number of ongoing challenges, including business disruptions or application incompatibilities, however. To address potential issues, SCIEX has released software upgrades, designed to run on Windows 10, for the entire software portfolio, including those solutions that power your mass spectrometry systems, such as Analyst® or SCIEX OS Software. The move to Windows 10 is an excellent first step toward modernizing your workstation software with minimal disruption and maximum benefit, the new SCIEX Alpha Workstation 2020 has just launched.
The Importance of Windows 10 to Your ResearchBy now, your IT team is most likely up to speed on Windows 10. As a reminder, however, Windows 10 was released more than two years ago and has since undergone many updates to improve functionality and security of your PC not to mention data. During this time, there have been some major improvements in the following areas that we feel are noteworthy to your work.
Want to Stay Ahead of the Windows 10 Curve?Get ahead of the January 2020 end-of-support deadline and take advantage of our special upgrade programs as you migrate to Windows 10 >
With this upgrade, you will benefit from a smooth transition to the new operating system and eliminate potential software downtime due to software incompatibility.
As an analytical strategy, middle-down mass spectrometry (MS) workflows characterize biotherapeutic proteins by analyzing large, digested protein fragments or defined subunits, rather than fully intact proteins (top-down) or digested peptides (bottom-up). A middle-down strategy combines the strengths of top-down and bottom-up approaches by delivering high sequence coverage and structural specificity while maintaining relatively simple sample preparation. In practice, middle-down analysis enables accurate mass measurement, rapid sequence confirmation, and localization of key post-translational modifications (PTMs) on protein subunits that are directly relevant to product quality.
In biopharmaceutical development, sequence variants (SV) are considered an inherent risk of producing complex proteins in living systems. Sequence variants are unintended changes to the amino acid sequence of a biotherapeutic and can be caused by errors in transcription or translation in the host cell, or cell culture and process conditions. Detailed analysis of SVs is important in process and product development to ensure the drug’s safety and efficacy. Even low‑level sequence variants can have significant implications for product quality, safety, and efficacy, making their accurate detection and characterization a critical requirement across development, process optimization, and regulatory submission.
CE‑SDS remains a cornerstone assay for characterizing fragmentation, aggregation, and product‑related impurities in therapeutic proteins. UV detection has been the long‑standing standard. However, it frequently struggles with baseline noise, limited sensitivity for minor fragments, and subjective integration.
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