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Jun 21, 2017 | Blogs, Food / Beverage | 0 comments
A recent study published by the Annals of Allergy, Asthma, and Immunology (ACAAI), pointed out, in a study of 109 people tested, that skin prick tests are not 100 percent reliable. In the study, participants were subjected to oral food challenges prior to skin testing in which 50 percent of individuals had no reaction. It was also discovered that blood tests were not full-proof even though they measure the presence of IgE antibodies to specific foods. These results are not surprising given that 50 to 60 percent of tests result in false-positives.
This occurs for several reasons:
It would seem, therefore, that more reliable tests are needed which brings me back to the lab. Today, blood tests are commonly interpreted using Enzyme-Linked Immunosorbent Assay (ELISA) despite a high incidence of false-positives. ELISA is affordable, straightforward, and provides effective testing results when used in conjunction with a person’s medical history. However mass spectrometry is more effective in detecting allergens due to its sensitivity, ability to correspond to unique allergen peptides, and its multi-allergen capabilities. Yes, mass spec is more expensive, but because of their versatility and sensitivity, you get a swift ROI while reducing those pesky false positives. You can learn more about Mass Spectrometry Myths in one of my previous posts.
Want to learn more about mass spectrometry and food allergen testing? Visit our Allergen page or read previous blog posts.
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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