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Antibodies, immobilization for

Anderson, G. P., Jacoby, M. A., Ligler, F. S., and King, K. D. (1997). Effectiveness of protein A for antibody immobilization for a fiber optic biosensor. Biosens. Bioelectron. 12,329-336. Baeumner, A. (2004). Nanosensors identify pathogens in food. Food Technol. 58, 51-55. Balbus, J. M., and Embrey, M. A. (2002). Risk factors for waterborne enteric infections. Curr. Opin. Gastroenterol. 18, 46-50. [Pg.32]

Ligler, F. S., King, K. D. (1997). Effectiveness of protein A for antibody immobilization for a fiber optic biosensor. Biosens Bioelectron 12, 329-336. [Pg.151]

Maraldo, D., Mutharasan, R. Optimization of antibody immobilization for sensing using piezoelectrically excited-millimeter-sized cantilever (PEMC) sensors. Sensors and Actuators B Chemical2007, 123 (1), 474-479... [Pg.82]

Figure 4. Experimental apparatus. A reagent reservoir manifold containing four cylindrical chambers was connected via a four port manifold into the inlet of the sample flow cell (SFC). A peristaltic pump, connected to the SFC outlet, maintained constant flow rate between 0.4 and 1.0 ml/min. The experimental apparatus allows for a single pass through the SFC as well as for recirculation during antibody immobilization. For the E. coli detection experiments, a fifth reagent reservoir (not shown) was added for hydroxylamine or Protein G. Figure 4. Experimental apparatus. A reagent reservoir manifold containing four cylindrical chambers was connected via a four port manifold into the inlet of the sample flow cell (SFC). A peristaltic pump, connected to the SFC outlet, maintained constant flow rate between 0.4 and 1.0 ml/min. The experimental apparatus allows for a single pass through the SFC as well as for recirculation during antibody immobilization. For the E. coli detection experiments, a fifth reagent reservoir (not shown) was added for hydroxylamine or Protein G.
Ferreira, N.S., Sales, M.G.F., 2014. Disposable immunosensor using a simple method for oriented antibody immobilization for label-free real-time detection of an oxidative stress biomarker implicated in cancer diseases. Biosens. Bioelectron. 53, 193-199. Available at http //linkinghub.elsevier.com/retrieve/pii/S095656631300674X. [Pg.358]

In contrast to the protection afforded to suckling rats by Tyv-specific antibodies, passive immunization of weaned rats fails to cause expulsion of T. spiralis (Otubu et al., 1993). Nevertheless, Tyv-specific antibodies do affect the behaviour of larvae in the intestines of weaned rats in the early hours following infection in that larvae are immobile in the intestinal tissue of such rats, though immobility is reversed when the larvae moult. These findings provide further evidence that antibodies specific for Tyv interfere with the LI larva s niche. [Pg.116]

Narang U., Anderson G.P., King K.D., Liss H.S., Ligler F.S., Enhanced biosensor performance using an avidin-biotin bridge for antibody immobilization, Proc. SPIE. 2980 187-194,1997. [Pg.454]

Peluso P., Wilson D.S., Do D., Tran H., Venkatasubbaiah M., Quincy D., Heidecker B., Poindexter K., Tolani N., Phelan M., Witte K., Jung L.S., Wagner P., Nock S., Optimizing antibody immobilization strategies for the construction of protein microarrays, Anal Biochem. 2003 312 113-124. [Pg.499]

NSC content was assessed in a population of cells expanded on EGF-His-immobilized surfaces for 5 days. Cells were immunocytochemically stained with antibodies specific for nestin, a marker for NSCs, and (1-tubulin III (pill),... [Pg.182]

Heat at 37°C for lOminutes to fully solubilize and maintain crosslinked proteins, and then enrich specific complexes by immunoprecipitation using an immobilized antibody specific for the bait protein that was used. Alternatively, heat at 96°C for 20 minutes to solubilize and break all crosslinks (this may be used as a control). [Pg.1011]

O. Ouerghi, A. Touhami, N. Jaffrezic-Renault, C. Martelet, H. Ben Ouada, and S. Cosnier, Impedimetric immunosensor using avidin-biotin for antibody immobilization. Bioelectrochemistry 56, 131—133... [Pg.166]

Conductometric transducers, as the oldest electrochemical devices, seem not to enjoy wide applications due to their poor selectivity. For example, Yagiuda et al. proposed a conductometric immunosensor for the determination of methamphetamine (MA) in urine [89], The decrease in the conductivity between a pair of platinum electrodes might result from the direct attachment of MA onto the anti-MA antibodies immobilized on the electrode surface. The system was claimed to be a useful detection technique of MA in comparison with a gas chromatography-mass spectrometry method. [Pg.267]

Z.Y. Wu, Y.H. Yan, G.L. Shen, and R.Q. Yu, A novel approach of antibody immobilization based on n-butyl amine plasma-polymerized films for immunosensors. Anal. Chim. Acta 412, 29-35 (2000). [Pg.276]

A continuous semiautomated FIIA system has been reported [208,235]. In this device the analyte-containing medium is allowed to flow through a column containing the antibodies immobilized on a support. First, the antibodies are saturated with a fluorescent dye-labeled analog of the analyte. As the analyte passes through the immunosorbent, some dye-labeled antigen is displaced and is then detected in a fluorometer located downstream from the column. The LOD achieved for the developed system is 1 pg L 1. [Pg.158]

The general method utilized to prepare E5-Ab solutions obviates the need for stocking large numbers of reagents which would be necessary if different activation methods were used for each antibody. A number of specific antibodies immobilized by this process have shown response similar to that of the same antibodies when adsorbed as immune complexes in the Stratus system. In addition, the dendrimer-coupled antibodies have shown dramatic improvements in sensitivity, flexibility and precision for the enzyme immunoassay system. Feasibility demonstration of an assay for DNA probes is a prelude to what can possibly be achieved with these dendrimer-based reagents. [Pg.482]

The surface activation time of the polymer required for maximum site activity for binding antibodies was determined by evaluating the fluorescence intensity of a series of probes incubated in inorganic acids at different times. Knowledge of the surface activation time is necessary to obtain maximum activation, thus allowing maximum antibody immobilization on the probe. Consequently, lower detection limits may be achieved. [Pg.213]


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