Modern affinity reagents: Recombinant antibodies and aptamers

Groff, Katherine; Brown, Jerram L.; Clippinger, Amy J.

doi:10.1016/j.biotechadv.2015.10.004

Cited by 113 publications

(78 citation statements)

References 113 publications

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“…Many of them have been continuously developed to inhibit the RT protein of HIV [46][47][48][49][50][51][52]. In a battle to replace antibodies destroyed by the virus, the spotlight gradually shifted to the diagnostic and therapeutic functions of aptamers in targeting immune systems [53,54]. A review of the attainments within this field was listed in Hu 's publication [55].…”

Section: Aptamer Timelinementioning

confidence: 99%

Predicting Future Prospects of Aptamers in Field-Effect Transistor Biosensors

Chen

2020

Molecules

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Aptamers, in sensing technology, are famous for their role as receptors in versatile applications due to their high specificity and selectivity to a wide range of targets including proteins, small molecules, oligonucleotides, metal ions, viruses, and cells. The outburst of field-effect transistors provides a label-free detection and ultra-sensitive technique with significantly improved results in terms of detection of substances. However, their combination in this field is challenged by several factors. Recent advances in the discovery of aptamers and studies of Field-Effect Transistor (FET) aptasensors overcome these limitations and potentially expand the dominance of aptamers in the biosensor market.

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Section: Aptamer Timelinementioning

confidence: 99%

Predicting Future Prospects of Aptamers in Field-Effect Transistor Biosensors

Chen

2020

Molecules

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“…They also recommend that the European Union Reference Laboratory for Alternatives to Animal Testing (eurl ecvam) extends its activities to include the production of animalfriendly affinity reagents (afas) and their subsequent use (p. 967). In addition, there are reported concerns about the quality and unreliability of commercial, animal-derived antibodies (Groff, Brown andClippinger, 2015, p. 1788); and scientists are being encouraged to use the non-animal affinity reagents that are available.…”

Section: 6mentioning

confidence: 99%

When Is an Alternative Not an Alternative? Supporting Progress for Absolute Replacement of Animals in Science

Redmond¹

2019

Animal Experimentation: Working Towards a Paradigm Change

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“…There is an active group in the antibody community suggesting abandoning the use of polyclonal and non-recombinant monoclonal antibodies due to a lack of "validation", in favor of the use of entirely recombinant reagents in combination with their sequence information [11][12][13][14]. This approach seems to be quite elegant to get rid of many problems at once.…”

Section: Introductionmentioning

confidence: 99%

Fast Confirmation of Antibody Identity by MALDI-TOF MS Fingerprints

2020

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Thousands of antibodies for diagnostic and other analytical purposes are on the market. However, it is often difficult to identify duplicates, reagent changes, and to assign the correct original publications to an antibody. This slows down scientific progress and might even be a cause of irreproducible research and a waste of resources. Recently, activities were started to suggest the sole use of recombinant antibodies in combination with the open communication of their sequence. In this case, such uncertainties should be eliminated. Unfortunately, this approach seems to be rather a long-term vision since the development and manufacturing of recombinant antibodies remain quite expensive in the foreseeable future. Nearly all commercial antibody suppliers also may be reluctant to publish the sequence of their antibodies, since they fear counterfeiting. De novo sequencing of antibodies is also not feasible today for a reagent user without access to the hybridoma clone. Nevertheless, it seems to be crucial for any scientist to have the opportunity to identify an antibody undoubtedly to guarantee the traceability of any research activity using antibodies from a third party as a tool. For this purpose, we developed a method for the identification of antibodies based on a MALDI-TOF MS fingerprint. To circumvent lengthy denaturation, reduction, alkylation, and enzymatic digestion steps, the fragmentation was performed with a simple formic acid hydrolysis step. Eighty-nine unknown monoclonal antibodies were used for this study to examine the feasibility of this approach. Although the molecular assignment of peaks was rarely possible, antibodies could be easily recognized in a blinded test, simply from their mass-spectral fingerprint. A general protocol is given, which could be used without any optimization to generate fingerprints for a database. We want to propose that, in most scientific projects relying critically on antibody reagents, such a fingerprint should be established to prove and document the identity of the used antibodies, as well as to assign a specific reagent to a datasheet of a commercial supplier, public database record, or antibody ID.

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Modern affinity reagents: Recombinant antibodies and aptamers

Cited by 113 publications

References 113 publications

Predicting Future Prospects of Aptamers in Field-Effect Transistor Biosensors

Predicting Future Prospects of Aptamers in Field-Effect Transistor Biosensors

When Is an Alternative Not an Alternative? Supporting Progress for Absolute Replacement of Animals in Science

Fast Confirmation of Antibody Identity by MALDI-TOF MS Fingerprints

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