GEN-MKT-18-7897-A
Apr 29, 2026 | Biopharma, Blogs | 0 comments
Differentiation of Leu and Ile residues using EAD. EAD can lead to secondary fragmentation of the side chains of Leu and Ile residues in the z ions, producing signature w ions (z-29 and z-43) from the neutral loss of C3H7 (43 Da) for Leu and C2H5 (29 Da) for Ile. The detection of these diagnostic fragments enables unambiguous differentiation of Leu vs. Ile.
EAD spectrum of a low-abundant V→Xle (Xle=Lue or Ile) sequence variant (<0.05%) of the VVSV peptide in NISTmAb. The detection of a z13-29 (w13) ion in this EAD spectrum shows that the Xle residue is an Ile instead of a Leu.
Glycosylation is one of the more structurally diverse and biologically impactful PTMs in protein therapeutics. Both N‑linked and O‑linked glycans influence protein folding, stability, and biological activity. Given these effects on biotherapeutics, glycosylation is a closely monitored critical quality attribute (CQA). Comprehensive and site‑specific characterization of glycosylation is essential for informed decision‑making throughout drug discovery and development.
Warranty expiration is more than an administrative milestone—it is a transition point that can significantly impact instrument uptime, laboratory productivity, operating budgets, and scientific outcomes.
For more than 20 years, the CDCO has supported academic, commercial, and not‑for‑profit drug discovery programs with deep expertise in pharmaceutical lead optimization. Within the bioanalytical group, their role is to enable rapid and reliable decision‑making through quantitative analysis of candidate drugs in biological matrices.
Posted by
You must be logged in to post a comment.
Share this post with your network