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Establishment of a high-sensitivity time-resolved fluorescence immunoassay with PLA2R-IgG1 antibody and its clinical application in idiopathic membranous nephropathy prognosis.
Clin Chim Acta
January 2025
Kidney Disease Center, The first affiliated hospital, Zhejiang University School of Medicine, Hangzhou, China. Electronic address:
Introduction: The objective of this study was to develop a highly sensitive time-resolved fluorescence immunoassay (TRFIA) method to detect phospholipase A2 receptor (PLA2R)-IgG1 antibodies and evaluate its clinical relevance in predicting the prognosis of individuals with idiopathic membranous nephropathy (IMN).
Materials And Methods: A three-step indirect TRFIA method was established using a PLA2R antigen-coated microtiter plate to capture PLA2R-IgG antibodies, followed by detection using mouse anti-human IgG1 and Eu-labeled goat anti-mouse IgG antibodies. This method was applied to the initial serum of 56 patients with PLA2R-IMN to investigate the clinical value of PLA2R-IgG1 antibody levels in predicting IMN prognosis.
Abnormal human immunoglobulin G (IgG) may induce the risk of immune system disorder, infectious diseases, tumors and so on. However, the current detection methods exhibit low sensitivity, which limits their practical application. In this work, an SPR optical fiber sensor (SPR-OFS) with high sensitivity is designed for label-free detection of human IgG.
View Article and Find Full Text PDFOptofluidic chip with directly printed polymer optical waveguide Mach-Zehnder interferometer sensors for label-free biodetection.
Biomed Opt Express
May 2024
Photonics Research Institute, Department of Electrical and Electronic Engineering, The Hong Kong Polytechnic University, Kowloon, Hong Kong SAR, China.
Optofluidic devices hold great promise in biomedical diagnostics and testing because of their advantages of miniaturization, high sensitivity, high throughput, and high scalability. However, conventional silicon-based photonic chips suffer from complicated fabrication processes and less flexibility in functionalization, thus hindering their development of cost-effective biomedical diagnostic devices for daily tests and massive applications in responding to public health crises. In this paper, we present an optofluidic chip based on directly printed polymer optical waveguide Mach-Zehnder interferometer (MZI) sensors for label-free biomarker detection.
View Article and Find Full Text PDFPurification and partial characterization of a sperm motility-inhibitory protein of ram cauda epididymal plasma.
Cell Biochem Funct
January 2024
Division of Animal Physiology & Biochemistry, ICAR-Central Sheep and Wool Research Institute, Avikanagar, Rajasthan, India.
Mammalian sperm remain quiescent but fertile for several weeks in cauda epididymis. Although several sperm quiescent factors of epididymal plasma have been identified in goat, pig and cattle; however, little is known in sheep. In the present study, purification and characterization of a novel sperm quiescent protein of ovine cauda epididymal plasma (CEP) was carried out.
View Article and Find Full Text PDFInfluence of bovine and human serum albumin on the binding kinetics of biomolecular interactions.
Analyst
October 2023
Département de chimie, Quebec center for advanced materials (QCAM), Regroupement québécois sur les matériaux de pointe (RQMP), and Centre interdisciplinaire de recherche sur le cerveau et l'apprentissage (CIRCA), Université de Montréal, CP. 6128 Succ. Centre-Ville, Montréal, Qc, H3C 3J7, Canada.
Article Synopsis
- Bovine serum albumin (BSA) is commonly used in biosensing as a blocking buffer, but human serum albumin (HSA) has a significant impact on binding assays and has been underexplored.
- A study utilized surface plasmon resonance (SPR) to investigate the effects of different albumins and human serum on a simple binding assay involving human IgG and goat anti-human IgG, revealing that HSA substantially influences the SPR shifts and binding constants.
- The findings suggest BSA is effective for surface blocking but recommend using HSA for optimizing assays intended for clinical applications involving human blood or serum, highlighting the necessity of considering specific protein interactions in such contexts.
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