Site-directed biotinylation of antibodies for controlled immobilization on solid surfaces

Cho, Il-Hoon; Paek, Eui-Hwan; Lee, Haiwon; Kang, Ji Yoon; Kim, Tae Song; Paek, Se‐Hwan

doi:10.1016/j.ab.2007.02.028

Cited by 110 publications

(60 citation statements)

References 32 publications

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“…This increased Ab fragment density should theoretically result in enhanced detection sensitivity of the target antigen. Cho et al [3] experimentally confirmed this when an enhanced binding capacity was reported from an assay using Fab fragments compared to full Abs (Fig. 2).…”

Section: Immobilisation Of Recognition Elementssupporting

confidence: 55%

“…Although highly stable, Abs covalently-linked through amino groups are randomly oriented with their antigen binding capacities reported as 2-3-fold lower compared to those of welloriented Abs [3,16]. Strategies available for the covalent site-specific oriented immobilisation of Abs exist using the carbohydrate chains of Abs for immobilisation [17].…”

Section: Fig (3)mentioning

confidence: 99%

“…2) [2]. Whole Ab's when immobilised may tilt due to the presence of the Fc region, or lie on their side, leaving the antigen binding sites close to the assay surface [3]. Pronounced steric hindrance may result, in particular if the antibody reacts with a large-molecular-weight antigen.…”

Section: Immobilisation Of Recognition Elementsmentioning

confidence: 99%

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Trends and Perspectives in Immunosensors

2012

Antibodies Applications and New Developments

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Immunosensors are devices that comprise both a biomolecular recognition system, such as an antibody and its corresponding antigen, and a transducer to translate the high affinity and specific binding event into a physical signal.Antibodies are produced by an immunological response to the presence of a foreign substance called an antigen. Antibodies may be immobilised onto a variety of platforms including bulk planar surfaces and nanoparticles by either covalent or adsorption strategies. Different interfaces between the bio-components and the detector are available to monitor in 'real-time' the signal generated by biological interactions. The transducers detect, for example, the change in electron transfer, absorbance, fluorescence, refractive index, mass change or heat transfer as the antibody binds to the antigen of interest. Such analytical devices have allowed a wide range of analytes to be identified and quantified such as pathogens, toxins, environmental food contaminants and disease biomarkers.The demand for sensitive, rapid, 'on-site' techniques has taken advantage of the latest advances in microfluidics and nanotechnology. This chapter will highlight current trends in immobilisation, micro/nano-fluidics/ and transducers utilised. A number of examples outlining the exploitation of these elements in immunosensors and their successful applications will be described.

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Section: Immobilisation Of Recognition Elementssupporting

confidence: 55%

Section: Fig (3)mentioning

confidence: 99%

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Trends and Perspectives in Immunosensors

2012

Antibodies Applications and New Developments

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“…The currently used techniques are in principle based on these studies and they have been applied to a variety of IgG molecules (Kato et al 1976, Karyakin et al 2000, Cho et al 2007, Pereira and Lai 2008, Cho et al 2009, Billah et al 2010, Ho et al 2010, Hu et al 2010, KausaiteMinkstimiene et al 2010, Wu et al 2014). Another of their advantages is that in cases when the amount of antibody is limited, it enables the reduction and/or conjugation procedures to be tested using other IgG antibodies at first.…”

Section: Introductionmentioning

confidence: 99%

“…One of them is following the established protocol (Hermanson 2008) not taking the antibody type into consideration (Karyakin et al 2000, Billah et al 2010, Ho et al 2010, Hu et al 2010. The second one is tailoring the reduction conditions to particular antibodies resulting in many rather widely distributed adaptations of the original protocol (Kato et al 1976, Cho et al 2007, Pereira and Lai 2008, Kausaite-Minkstimiene et al 2010). Although it is sometimes implied that the reduction protocol has to be adapted for particular antibodies used, it is not clear how the reduction products differ when different antibodies are used.…”

Section: Introductionmentioning

confidence: 99%

Considerations in producing preferentially reduced half-antibody fragments

Makaraviciute

Jackson

Millner

et al. 2016

Journal of Immunological Methods

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Half-antibody fragments are a promising reagent for biosensing, drug-delivery and labeling applications, since exposure of the free thiol group in the Fc hinge region allows oriented Preferential reduction of rabbit anti-myoglobin IgG antibodies was optimized and the highest half-antibody yield was obtained with 35 mM TCEP. Finally, it has been demonstrated that produced anti-myoglobin half-IgG fragments retained their binding activity.

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