PubMed · 14970555
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Paul Cutler. 2004. Immunoaffinity chromatography.. https://doi.org/10.1385/1-59259-655-x%3A167
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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.
Interleukin-2 (IL-2) is the major growth factor for activated T-lymphocytes and stimulates clonal expansion and maturation of these lymphocytes. IL-2 binds to its receptor complex, IL-2Ralpha, beta, and gamma chains, and exerts its effect via second messengers, mainly tyrosine kinases, which ultimately stimulate gene expression. The heterotrimerization of the receptor chains leads to high affinity binding for IL-2. The functional importance of IL-2Ralpha in hematopoietic cell systems is well known. However, the potential role that IL-2Ralpha plays in tumorigenesis is still not fully elucidated. Il-2Ralpha expression has been found in many types of cancers, including leukemia, lymphoma, lung, breast, head-and-neck and prostate. Recent evidence shows that high expression of IL-2Ralpha in tumors correlates with a poor prognosis for the patient. This review details the current known functions of IL-2Ralpha in cancer cells and some of the therapies used to combat IL-2Ralpha-mediated cell signaling.
The interaction between single synthesized antigen and its monoclonal antibody was directly monitored by Atomic Force Microscopy (AFM) with antigen-labeled AFM tip. The details about tip modification and antibody immobilization were described. The interactions were monitored by the change of adhesive force in separating the bound antigen-antibody. The results showed that two processes could be observed in the combination of antigen-antibody system. Possible mechanisms of rupture process as independent unbinding and cooperative unbinding were discussed. At slow separation process, the antigen-antibody linkage appeared to rupture sequentially. Increasing the separation rate from 50 nm/s to 2000 nm/s led to an increase in the possibility of cooperative unbinding. The pH influenced the affinity constants greatly, but had little effect on the magnitude of unbinding forces. The obtained results were compared with affinity constants between complete antigen and antibody obtained by immunoassay method (ELISA). The observed single rupture force between individual antibody and antigen molecules provided pertinent information relating to the manner how the antibody molecule binds to its specific antigen.