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Claus Oxvig

Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species

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Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species. / Mikkelsen, Jakob H; Steffensen, Lasse B; Oxvig, Claus.

In: Journal of Immunological Methods, Vol. 404, 02.2014, p. 33-40.

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@article{49c9373eea2842c895a0a5160efeefdb,
title = "Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species",
abstract = "The metalloproteinase, pregnancy-associated plasma protein-A (PAPP-A), is increasingly recognized as a modulator of insulin-like growth factor (IGF) signaling; it cleaves IGF binding proteins causing the release of bioactive IGF. Accumulating evidence supports an important role of PAPP-A in both normal physiology and under different pathological conditions. However, antibodies for the detection of PAPP-A in non-human tissues have been lacking, although needed for use with several animal models which are currently being developed. To develop a monoclonal antibody suitable for the immunohistochemical detection of PAPP-A, we therefore selected a phage-derived scFv antibody, PAC1, specifically recognizing an epitope of PAPP-A, which is highly conserved between multiple animal species. We first converted this antibody into bivalent IgG, and verified its ability to recognize PAPP-A in sections of formalin-fixed and paraffin-embedded tissue. For increased sensitivity, affinity maturation to sub-nanomolar affinity was then carried out. The resulting recombinant antibody, PAC1-D8-mIgG2a, detects PAPP-A specifically and sensitively in human tissue. In addition, this antibody allows detection of PAPP-A in non-human species. We demonstrate its usefulness for the visualization of PAPP-A in murine and porcine tissues.",
author = "Mikkelsen, {Jakob H} and Steffensen, {Lasse B} and Claus Oxvig",
note = "Copyright {\circledC} 2013 Elsevier B.V. All rights reserved.",
year = "2014",
month = "2",
doi = "10.1016/j.jim.2013.12.002",
language = "English",
volume = "404",
pages = "33--40",
journal = "Journal of Immunological Methods",
issn = "0022-1759",
publisher = "Elsevier BV",

}

RIS

TY - JOUR

T1 - Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species

AU - Mikkelsen, Jakob H

AU - Steffensen, Lasse B

AU - Oxvig, Claus

N1 - Copyright © 2013 Elsevier B.V. All rights reserved.

PY - 2014/2

Y1 - 2014/2

N2 - The metalloproteinase, pregnancy-associated plasma protein-A (PAPP-A), is increasingly recognized as a modulator of insulin-like growth factor (IGF) signaling; it cleaves IGF binding proteins causing the release of bioactive IGF. Accumulating evidence supports an important role of PAPP-A in both normal physiology and under different pathological conditions. However, antibodies for the detection of PAPP-A in non-human tissues have been lacking, although needed for use with several animal models which are currently being developed. To develop a monoclonal antibody suitable for the immunohistochemical detection of PAPP-A, we therefore selected a phage-derived scFv antibody, PAC1, specifically recognizing an epitope of PAPP-A, which is highly conserved between multiple animal species. We first converted this antibody into bivalent IgG, and verified its ability to recognize PAPP-A in sections of formalin-fixed and paraffin-embedded tissue. For increased sensitivity, affinity maturation to sub-nanomolar affinity was then carried out. The resulting recombinant antibody, PAC1-D8-mIgG2a, detects PAPP-A specifically and sensitively in human tissue. In addition, this antibody allows detection of PAPP-A in non-human species. We demonstrate its usefulness for the visualization of PAPP-A in murine and porcine tissues.

AB - The metalloproteinase, pregnancy-associated plasma protein-A (PAPP-A), is increasingly recognized as a modulator of insulin-like growth factor (IGF) signaling; it cleaves IGF binding proteins causing the release of bioactive IGF. Accumulating evidence supports an important role of PAPP-A in both normal physiology and under different pathological conditions. However, antibodies for the detection of PAPP-A in non-human tissues have been lacking, although needed for use with several animal models which are currently being developed. To develop a monoclonal antibody suitable for the immunohistochemical detection of PAPP-A, we therefore selected a phage-derived scFv antibody, PAC1, specifically recognizing an epitope of PAPP-A, which is highly conserved between multiple animal species. We first converted this antibody into bivalent IgG, and verified its ability to recognize PAPP-A in sections of formalin-fixed and paraffin-embedded tissue. For increased sensitivity, affinity maturation to sub-nanomolar affinity was then carried out. The resulting recombinant antibody, PAC1-D8-mIgG2a, detects PAPP-A specifically and sensitively in human tissue. In addition, this antibody allows detection of PAPP-A in non-human species. We demonstrate its usefulness for the visualization of PAPP-A in murine and porcine tissues.

U2 - 10.1016/j.jim.2013.12.002

DO - 10.1016/j.jim.2013.12.002

M3 - Journal article

VL - 404

SP - 33

EP - 40

JO - Journal of Immunological Methods

JF - Journal of Immunological Methods

SN - 0022-1759

ER -