Antibodies in proteomics II: screening, high-throughput characterization and downstream applications

Bradbury, Andrew; Velappan, Nileena; Verzillo, Vittorio; Ovečka, Milan; Chasteen, Leslie; Sblattero, Daniele; Marzari, Roberto; Lou, Jianlong; Siegel, Robert W.; Pavlik, Peter

doi:10.1016/s0167-7799(03)00117-3

Cited by 53 publications

(26 citation statements)

References 57 publications

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“…Antibodies are the protein binding agents of choice because of their diversity, high affinity, and specificity. Many different methods of obtaining and purifying antibodies have been developed (Bradbury et al, 2003). However, the phage display is likely the only economically viable method that can operate in vitro.…”

Section: Discussionmentioning

confidence: 99%

Subtractive phage display technology identifies zebrafish marcksb that is required for gastrulation

Wang

Wei

Dai

et al. 2013

Gene

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Section: Discussionmentioning

confidence: 99%

Subtractive phage display technology identifies zebrafish marcksb that is required for gastrulation

Wang

Wei

Dai

et al. 2013

Gene

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“…Previous studies of antibody microarray technology have mainly focused on the immobilization techniques, including the selection of support materials [27,[40][41][42][43][44]. As it seems that these techniques have been sufficiently studied, we focused our research on techniques for signal detection.…”

Section: Spr-based Antibody Microarraymentioning

confidence: 99%

A chip‐based miniaturized format for protein‐expression profiling: The exploitation of comprehensively produced antibodies

et al. 2006

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Numerous antibodies have been developed and validated in recent years, and show promise for use in novel functional protein assays. Such assays would be an alternative to pre-existing comprehensive assays, such as DNA microarrays. Antibody microarrays are thought to represent those functional protein assays. While a variety of attempts have been made to apply DNA microarray technology to antibody microarrays, a fully optimized protocol has not been established. We have been conducting a project to comprehensively produce antibodies against mouse KIAA ("KI" stands for "Kazusa DNA Research Institute" and "AA" are reference characters) proteins. Using our library of antibodies, we established a novel antibody microarray format that utilizes surface plasmon resonance (SPR) technology. A label-free real-time measurement of protein expression in crude cell lysates was achieved by direct readout of the bindings using SPR. Further refinement of the antibody microarray format enabled us to detect a smaller quantity of target proteins in the lysate without the bulk effect. In this review, we first summarize available antibody array formats and then describe the above-mentioned format utilizing updated SPR technology.

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“…Monoclonal antibodies produced by B cell hybridoma technology have the advantage of an almost unlimited supply with identical and uniform specificity. Additionally, many successful results have recently been published dealing with the generation of genetically engineered antibodies or antibody-like molecules, [22][23][24] some of which have been used for the large-scale production of immunosorbents. 25,26 The antibody-secreting hybridomas are also useful for cloning variable region genes of an antibody, which can be a starting material for preparing such an engineered antibody.…”

Section: Introductionmentioning

confidence: 99%

Production and Characterization of a Monoclonal Antibody to Capture Proteins Tagged with Lithocholic Acid

et al. 2008

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Reactive metabolic-modified proteins have been proposed to play an important role in the mechanism(s) of the hepatotoxicity and colon cancer of lithocholic acid (LCA). To identify cellular proteins chemically modified with LCA, we have generated a monoclonal antibody that recognizes the 3a-hydroxy-5b-steroid moiety of LCA. The spleen cells from a BALB/c mouse, which was immunized with an immunogen in which the side chain of LCA was coupled to bovine serum albumin (BSA) via a succinic acid spacer, was fused with SP2/0 myeloma cells to generate antibody-secreting hybridoma clones. The resulting monoclonal antibody (g2b, k) was specific to LCA-N a -BOC-lysine as well as the amidated and nonamidated forms of LCA. The immunoblot enabled the detection of LCA residues anchored on BSA and lysozyme. The antibody will be useful for monitoring the generation, localization, and capture of proteins tagged with LCA, which may be the cause of LCA-induced toxicity.

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Antibodies in proteomics II: screening, high-throughput characterization and downstream applications

Cited by 53 publications

References 57 publications

Subtractive phage display technology identifies zebrafish marcksb that is required for gastrulation

Subtractive phage display technology identifies zebrafish marcksb that is required for gastrulation

A chip‐based miniaturized format for protein‐expression profiling: The exploitation of comprehensively produced antibodies

Production and Characterization of a Monoclonal Antibody to Capture Proteins Tagged with Lithocholic Acid

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