76884

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Showing 1-10 of 10 results for "76884" within Papers

Versatile characterization of glycosylation modification in CTLA4-Ig fusion proteins by liquid chromatography-mass spectrometry.

Lei Zhu et al.

mAbs, 6(6), 1474-1485 (2014-12-09)

CTLA4-Ig is a highly glycosylated therapeutic fusion protein that contains multiple N- and O-glycosylation sites. Glycosylation plays a vital role in protein solubility, stability, serum half-life, activity, and immunogenicity. For a CTLA4-Ig biosimilar development program, comparative analytical data, especially the

Profiling and characterization of sialylated N-glycans by 2D-HPLC (HIAX/PGC) with online orbitrap MS/MS and offline MSn.

Andrew J S Hanneman et al.

Journal of pharmaceutical sciences, 103(2), 400-408 (2013-12-05)

Glycosylation is a critical parameter used to evaluate protein quality and consistency. N-linked glycan profiling is fundamental to the support of biotherapeutic protein manufacturing from early stage process development through drug product commercialization. Sialylated glycans impact the serum half-life of

Development and application of a robust N-glycan profiling method for heightened characterization of monoclonal antibodies and related glycoproteins.

Tanya Q Shang et al.

Journal of pharmaceutical sciences, 103(7), 1967-1978 (2014-05-21)

A highly robust hydrophilic interaction liquid chromatography (HILIC) method that involves both fluorescence and mass spectrometric detection was developed for profiling and characterizing enzymatically released and 2-aminobenzamide (2-AB)-derivatized mAb N-glycans. Online HILIC/mass spectrometry (MS) with a quadrupole time-of-flight mass spectrometer

Glycosylation profiles determine extravasation and disease-targeting properties of armed antibodies.

Dario Venetz et al.

Proceedings of the National Academy of Sciences of the United States of America, 112(7), 2000-2005 (2015-02-04)

The ability of antibodies to extravasate out of blood vessels is critical for therapeutic activity, because molecular targets for most diseases are located outside of the endothelial lining. By performing detailed biodistribution studies with a novel IL9-armed cancer-specific antibody, we

Improved analysis of oligosaccharides for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry using aminopyrazine as a derivatization reagent and a co-matrix.

Yan Cai et al.

The Analyst, 138(21), 6270-6276 (2013-09-07)

Analysis of oligosaccharides by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) is often limited by their low ionization efficiency and inadequate fragmentation information. Derivatizations of oligosaccharides to enhance their ionization in MS are widely used, but most of these

Changes to serum sample tube and processing methodology does not cause Intra-Individual [corrected] variation in automated whole serum N-glycan profiling in health and disease.

Nicholas T Ventham et al.

PloS one, 10(4), e0123028-e0123028 (2015-04-02)

Serum N-glycans have been identified as putative biomarkers for numerous diseases. The impact of different serum sample tubes and processing methods on N-glycan analysis has received relatively little attention. This study aimed to determine the effect of different sample tubes

Target-directed development and preclinical characterization of the proposed biosimilar rituximab GP2013.

Antonio da Silva et al.

Leukemia & lymphoma, 55(7), 1609-1617 (2013-09-13)

Biosimilar development involves a target-directed iterative process to ensure a similar product to the originator. Here we report the preclinical development of the proposed biosimilar rituximab (GP2013). Post-translational modifications and bioactivities of GP2013 versus originator rituximab were engineered and monitored

Comparison of methods for the analysis of therapeutic immunoglobulin G Fc-glycosylation profiles--part 1: separation-based methods.

Dietmar Reusch et al.

mAbs, 7(1), 167-179 (2014-12-20)

Immunoglobulin G (IgG) crystallizable fragment (Fc) glycosylation is crucial for antibody effector functions, such as antibody-dependent cell-mediated cytotoxicity, and for their pharmacokinetic and pharmacodynamics behavior. To monitor the Fc-glycosylation in bioprocess development, as well as product characterization and release analytics

Caenorhabditis elegans bacterial pathogen resistant bus-4 mutants produce altered mucins.

Lisa M Parsons et al.

PloS one, 9(10), e107250-e107250 (2014-10-09)

Caenorabditis elegans bus-4 glycosyltransferase mutants are resistant to infection by Microbacterium nematophilum, Yersinia pestis and Yersinia pseudotuberculosis and have altered susceptibility to two Leucobacter species Verde1 and Verde2. Our objective in this study was to define the glycosylation changes leading

Identification of potential pancreatic cancer serum markers: Increased sialyl-Lewis X on ceruloplasmin.

Meritxell Balmaña et al.

Clinica chimica acta; international journal of clinical chemistry, 442, 56-62 (2015-01-18)

Pancreatic adenocarcinoma (PDAC) usually shows an enhanced expression of sialyl-Lewis X (sLe(x)) and related epitopes. PDAC may secrete some of the proteins carrying such increased sLe(x) determinant into serum, so they could be used as PDAC markers. Previously, we identified

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