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Proteome Software Inc scaffold perspectives
Serum proteomics workflow for the isolation and analysis of the molecular-form proteomes of IgA1. IgA1-containing immune complexes (IgA1-IC) from sera of 20 patients with IgA nephropathy (IgAN) and 20 healthy controls (HCs) were isolated by lectin-affinity chromatography followed by size-exclusion chromatography (SEC) to separate IgA1-IC from monomeric and polymeric IgA1 (I–III). IgA-specific protease and liquid chromatography mass spectrometry (LC-MS) sequence-grade trypsin digestion were followed by LC-MS (IV–V). After standard proteomic database searches, LC-MS results were curated by Scaffold <t>perSPECtives</t> to identify proteins of high abundance in IgA1-IC fractions of serum from patients with IgAN versus IgA1-IC from HCs with label-free quantification (LFQ). Additional comparisons were made to polymeric IgA1 (VI). Created with BioRender.com .
Scaffold Perspectives, supplied by Proteome Software Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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scaffold perspectives - by Bioz Stars, 2026-11
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Article Title: Proteomic Analysis of Circulating IgA1-Containing Immune Complexes in Patients with IgA Nephropathy

Journal: Kidney International Reports

doi: 10.1016/j.ekir.2025.07.005

Serum proteomics workflow for the isolation and analysis of the molecular-form proteomes of IgA1. IgA1-containing immune complexes (IgA1-IC) from sera of 20 patients with IgA nephropathy (IgAN) and 20 healthy controls (HCs) were isolated by lectin-affinity chromatography followed by size-exclusion chromatography (SEC) to separate IgA1-IC from monomeric and polymeric IgA1 (I–III). IgA-specific protease and liquid chromatography mass spectrometry (LC-MS) sequence-grade trypsin digestion were followed by LC-MS (IV–V). After standard proteomic database searches, LC-MS results were curated by Scaffold perSPECtives to identify proteins of high abundance in IgA1-IC fractions of serum from patients with IgAN versus IgA1-IC from HCs with label-free quantification (LFQ). Additional comparisons were made to polymeric IgA1 (VI). Created with BioRender.com .
Figure Legend Snippet: Serum proteomics workflow for the isolation and analysis of the molecular-form proteomes of IgA1. IgA1-containing immune complexes (IgA1-IC) from sera of 20 patients with IgA nephropathy (IgAN) and 20 healthy controls (HCs) were isolated by lectin-affinity chromatography followed by size-exclusion chromatography (SEC) to separate IgA1-IC from monomeric and polymeric IgA1 (I–III). IgA-specific protease and liquid chromatography mass spectrometry (LC-MS) sequence-grade trypsin digestion were followed by LC-MS (IV–V). After standard proteomic database searches, LC-MS results were curated by Scaffold perSPECtives to identify proteins of high abundance in IgA1-IC fractions of serum from patients with IgAN versus IgA1-IC from HCs with label-free quantification (LFQ). Additional comparisons were made to polymeric IgA1 (VI). Created with BioRender.com .

Techniques Used: Isolation, Affinity Chromatography, Size-exclusion Chromatography, Liquid Chromatography, Mass Spectrometry, Liquid Chromatography with Mass Spectroscopy, Sequencing, Quantitative Proteomics

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