Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Rodrigo, Gustav; Gruvegard, Mats; Alstine, James M. Van

doi:10.3390/antib4030259

Cited by 80 publications

(47 citation statements)

References 119 publications

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“…In biotechnology, affinity protein purification using antibody-based separation or a matrix with specific tags for binding target protein are commonly used methods [108]. The challenge is to use a common matrix for purification of different proteins.…”

Section: Protein Purificationmentioning

confidence: 99%

A biotechnological perspective on the application of iron oxide nanoparticles

et al. 2016

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In recent decades, magnetic iron nanoparticles (NPs) have attracted much attention due to properties such as superparamagnetism, high surface area, large surface-to-volume ratio, and easy separation under external magnetic fields. Therefore, magnetic iron oxides have potential for use in numerous applications, including magnetic resonance imaging contrast enhancement, tissue repair, immunoassay, detoxification of biological fluids, drug delivery, hyperthermia, and cell separation. This review provides an updated and integrated focus on the fabrication and characterization of suitable magnetic iron NPs for biotechnological applications. The possible perspective and some challenges in the further development of these NPs are also discussed.

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Section: Protein Purificationmentioning

confidence: 99%

A biotechnological perspective on the application of iron oxide nanoparticles

et al. 2016

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“…Moreover, a high concentration of complete antibody restricts its ability to infiltrate tumors (Weiner and Adams, 2000). Additional engineered antibody fragments include CDRs, Fab, F(ab') 2 , monospecific Fab 2 , bispecific Fab 2 , trispecific Fab 3 , monovalent IgG, bispecific diabody, trispecific triabody, scFv-Fc, minibody, new antigen receptor (IgNAR), variable new antigen receptor (V-NAR) domains in sharks, camelid heavy chain IgG (hcIgG), and VhH (Nelson, 2010;Rodrigo et al, 2015).…”

Section: Other Gene Engineered Antibody Fragmentsmentioning

confidence: 99%

Antibody Engineering for Pursuing a Healthier Future

et al. 2017

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Since the development of antibody-production techniques, a number of immunoglobulins have been developed on a large scale using conventional methods. Hybridoma technology opened a new horizon in the production of antibodies against target antigens of infectious pathogens, malignant diseases including autoimmune disorders, and numerous potent toxins. However, these clinical humanized or chimeric murine antibodies have several limitations and complexities. Therefore, to overcome these difficulties, recent advances in genetic engineering techniques and phage display technique have allowed the production of highly specific recombinant antibodies. These engineered antibodies have been constructed in the hunt for novel therapeutic drugs equipped with enhanced immunoprotective abilities, such as engaging immune effector functions, effective development of fusion proteins, efficient tumor and tissue penetration, and high-affinity antibodies directed against conserved targets. Advanced antibody engineering techniques have extensive applications in the fields of immunology, biotechnology, diagnostics, and therapeutic medicines. However, there is limited knowledge regarding dynamic antibody development approaches. Therefore, this review extends beyond our understanding of conventional polyclonal and monoclonal antibodies. Furthermore, recent advances in antibody engineering techniques together with antibody fragments, display technologies, immunomodulation, and broad applications of antibodies are discussed to enhance innovative antibody production in pursuit of a healthier future for humans.

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“…Because of their ability to be raised, selected, or designed to bind practically any protein of interest 6,8,9 , these protein binders have found multiple applications in diagnostics 3,10,11 , therapeutics 4,12,13 and biologics manufacturing 14–16 . As such, they have revolutionized the way we treat disease 13,17–19 , purify proteins 20–23 , and study biological phenomena 9,24–27 . The enormous impact that high affinity protein binders have had in medicine, biotechnology, and research stems from their usually irreversible binding to very specific targets.…”

Section: Introductionmentioning

confidence: 99%

Light-responsive monobodies for dynamic control of customizable protein binding

Carrasco-López

Zhao

Gil

et al. 2020

Preprint

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Customizable, high affinity protein-protein interactions, such as those mediated by antibodies and antibody-like molecules, are invaluable to basic and applied research and have become pillars for modern therapeutics. The ability to reversibly control the binding activity of these proteins to their targets on demand would significantly expand their applications in biotechnology, medicine, and research. Here we present, as proof-of-principle, a light-controlled monobody (OptoMB) that works in vitro and in vivo, whose affinity for its SH2-domain target exhibits a 300-fold shift in binding affinity upon illumination. We demonstrate that our αSH2-OptoMB can be used to purify SH2-tagged proteins directly from crude E. coli extract, achieving 99.8% purity and over 40% yield in a single purification step. This OptoMB belongs to a new class of light-sensitive protein binders we call OptoBinders (OptoBNDRs) which, by virtue of their ability to be designed to bind any protein of interest, have the potential to find new powerful applications as light-switchable binders of untagged proteins with high affinity and selectivity, and with the temporal and spatial precision afforded by light.

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Antibody Fragments and Their Purification by Protein L Affinity Chromatography

Cited by 80 publications

References 119 publications

A biotechnological perspective on the application of iron oxide nanoparticles

A biotechnological perspective on the application of iron oxide nanoparticles

Antibody Engineering for Pursuing a Healthier Future

Light-responsive monobodies for dynamic control of customizable protein binding

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