Search PubMed⌕ Search

PubMed · 11070869

Thin-layer chromatography immunostaining.

Abstract

The source did not provide an abstract. Follow the original record for more information.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

D Ishikawa, T Taki. 2000. Thin-layer chromatography immunostaining.. https://doi.org/10.1016/s0076-6879(00)12906-4

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

ZrO₂@C-based colorimetric/photothermal dual-mode immunosensor coupled with a novel monoclonal antibody for quantification of Aspergillus ochraceus biomass.

Aspergillus ochraceus contaminates agricultural products and produces nephrotoxic, carcinogenic ochratoxin A (OTA), posing severe food safety hazards. A dual-signal lateral flow immunochromatographic assay (dLFIA) based on ZrO₂@C nanoprobes was established for quantitative detection of A. ochraceus biomass. A novel monoclonal antibody (mAb 4B4) was prepared as the capture antibody to immobilize A. ochraceus mycelial lysate antigen on the test line, and a rabbit polyclonal antibody (pAb G2801) as the detection antibody to modify ZrO₂@C composites (synthesized via UiO-66 pyrolysis) into 200 nm colorimetric/photothermal nanoprobes. This dLFIA achieved limits of detection of 0.164 μg/mL (colorimetric) and 0.517 μg/mL (photothermal). This efficient and reliable method allows quantitative analysis of A. ochraceus biomass, which is suitable for routine monitoring of fungal contamination in agro-food matrices.

Antibodies, Monoclonal↗

Colloidal gold-based immunochromatographic assay for detection of ricin.

A rapid immunochromatographic assay was developed to detect ricin. The assay was based on the sandwich format using monoclonal antibodies (Mabs) of two distinct specificities. One anti-ricin B chain Mab (1G7) was immobilized to a defined detection zone on a porous nitrocellulose membrane, while the other anti-ricin A chain Mab (5E11) was conjugated to colloidal gold particles which served as a detection reagent. The ricin-containing sample was added to the membrane and allowed to react with Mab (5E11)-coated particles. The mixture was then passed along the porous membrane by capillary action past the Mab (1G7) in the detection zone, which will bind the particles that had ricin bound to their surface, giving a red color within this detection zone with an intensity proportional to ricin concentration. In the absence of ricin, no immunogold was bound to the solid-phase antibody. With this method, 50 ng/ml of ricin was detected in less than 10 min. The assay sensitivity can be increased by silver enhancement to 100 pg/ml.

Antibodies, Monoclonal↗

Anti-IgE antibody therapy.

From the published studies of E25, it is now clear that this approach to treating atopic disease can be successful. But there remain many issues, both practical and biological. For the study of atopic disease, a potentially excellent new tool has been provided that could allow IgE to be effectively eliminated, given the correct-dosing regimen, and provide the investigator with a means to ask questions about the role of IgE in the expression of a particular disease. No place is this more evident than in the study of asthma for which a long-standing debate revolves around the precise contribution of atopy to the genesis and maintenance of this disease. Furthermore, use of the drug may finally resolve questions about the role of IgE in parasitic rejection. From the perspective of the patient, at a minimum, the drug provides a proof-of-concept for all potential therapies seeking to reduce circulating IgE levels. With proper consideration of dosing, the drug appears as if it could provide remarkable improvement in the course of atopic disease. Some concerns still revolve around the improvement roles IgE may play in parasitic diseases, the cost of therapy, and that very long-term treatment effects have yet to be studied.

Antibodies, Monoclonal↗