Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species
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 nor...
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| Veröffentlicht in: | Journal of immunological methods 2014-02, Vol.404, p.33-40 |
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| creator | Mikkelsen, Jakob H. Steffensen, Lasse B. Oxvig, Claus |
| description | 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. |
| doi_str_mv | 10.1016/j.jim.2013.12.002 |
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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.</description><identifier>ISSN: 0022-1759</identifier><identifier>EISSN: 1872-7905</identifier><identifier>DOI: 10.1016/j.jim.2013.12.002</identifier><identifier>PMID: 24333852</identifier><language>eng</language><publisher>Netherlands: Elsevier B.V</publisher><subject>Affinity maturation ; Amino Acid Sequence ; Animals ; Antibody Affinity ; Antibody Specificity ; Conserved Sequence ; Epitopes - chemistry ; Epitopes - immunology ; Female ; Formaldehyde ; Humans ; Immunoglobulin G - biosynthesis ; Immunoglobulin G - immunology ; Immunohistochemistry ; Immunohistochemistry - methods ; Mice ; Molecular Sequence Data ; Paraffin Embedding ; Pregnancy ; Pregnancy-Associated Plasma Protein-A - analysis ; Pregnancy-Associated Plasma Protein-A - immunology ; Pregnancy-associated plasma-protein-A ; Recombinant antibody ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - immunology ; Sequence Alignment ; Single-Chain Antibodies - biosynthesis ; Single-Chain Antibodies - immunology ; Swine ; Tissue Fixation</subject><ispartof>Journal of immunological methods, 2014-02, Vol.404, p.33-40</ispartof><rights>2013 Elsevier B.V.</rights><rights>Copyright © 2013 Elsevier B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c353t-d70d96a3f9b56b4f1da2e053ffd4fcd08e492a75445c552a07c39ee478d17bb33</citedby><cites>FETCH-LOGICAL-c353t-d70d96a3f9b56b4f1da2e053ffd4fcd08e492a75445c552a07c39ee478d17bb33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0022175913003669$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24333852$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mikkelsen, Jakob H.</creatorcontrib><creatorcontrib>Steffensen, Lasse B.</creatorcontrib><creatorcontrib>Oxvig, Claus</creatorcontrib><title>Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species</title><title>Journal of immunological methods</title><addtitle>J Immunol Methods</addtitle><description>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.</description><subject>Affinity maturation</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibody Affinity</subject><subject>Antibody Specificity</subject><subject>Conserved Sequence</subject><subject>Epitopes - chemistry</subject><subject>Epitopes - immunology</subject><subject>Female</subject><subject>Formaldehyde</subject><subject>Humans</subject><subject>Immunoglobulin G - biosynthesis</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunohistochemistry</subject><subject>Immunohistochemistry - methods</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Paraffin Embedding</subject><subject>Pregnancy</subject><subject>Pregnancy-Associated Plasma Protein-A - analysis</subject><subject>Pregnancy-Associated Plasma Protein-A - immunology</subject><subject>Pregnancy-associated plasma-protein-A</subject><subject>Recombinant antibody</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - immunology</subject><subject>Sequence Alignment</subject><subject>Single-Chain Antibodies - biosynthesis</subject><subject>Single-Chain Antibodies - immunology</subject><subject>Swine</subject><subject>Tissue Fixation</subject><issn>0022-1759</issn><issn>1872-7905</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1v1DAQxS0EokvhD-CCfOSSMP5KNuK0Kh-tVIk9wNly7LHqJY6DnRT1v8fVFo4cRiM9vfc08yPkLYOWAes-nNpTiC0HJlrGWwD-jOzYvudNP4B6TnZV4Q3r1XBBXpVyAgAGHbwkF1wKIfaK78jPT3iPU1oizitNnhqa0aY4htlUoU4Yk3uga_ptsiv0eDgemwP1KdMQ4zanu1DWZO8wBmsmuhWkYaZxm9awTFjzIVa5LGgDltfkhTdTwTdP-5L8-PL5-9V1c_vt683V4baxQom1cT24oTPCD6PqRumZMxxBCe-d9NbBHuXATa-kVFYpbqC3YkCU_d6xfhyFuCTvz71LTr82LKuOoVicJjNj2opmCiTrpJBQrexstTmVktHrJdeT84NmoB8Z65OujPUjY824rkRr5t1T_TZGdP8Sf6FWw8ezAeuT9wGzLvX92aILFe6qXQr_qf8D0TqNyQ</recordid><startdate>201402</startdate><enddate>201402</enddate><creator>Mikkelsen, Jakob H.</creator><creator>Steffensen, Lasse B.</creator><creator>Oxvig, Claus</creator><general>Elsevier B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201402</creationdate><title>Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species</title><author>Mikkelsen, Jakob H. ; Steffensen, Lasse B. ; Oxvig, Claus</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c353t-d70d96a3f9b56b4f1da2e053ffd4fcd08e492a75445c552a07c39ee478d17bb33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Affinity maturation</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibody Affinity</topic><topic>Antibody Specificity</topic><topic>Conserved Sequence</topic><topic>Epitopes - chemistry</topic><topic>Epitopes - immunology</topic><topic>Female</topic><topic>Formaldehyde</topic><topic>Humans</topic><topic>Immunoglobulin G - biosynthesis</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunohistochemistry</topic><topic>Immunohistochemistry - methods</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Paraffin Embedding</topic><topic>Pregnancy</topic><topic>Pregnancy-Associated Plasma Protein-A - analysis</topic><topic>Pregnancy-Associated Plasma Protein-A - immunology</topic><topic>Pregnancy-associated plasma-protein-A</topic><topic>Recombinant antibody</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - immunology</topic><topic>Sequence Alignment</topic><topic>Single-Chain Antibodies - biosynthesis</topic><topic>Single-Chain Antibodies - immunology</topic><topic>Swine</topic><topic>Tissue Fixation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mikkelsen, Jakob H.</creatorcontrib><creatorcontrib>Steffensen, Lasse B.</creatorcontrib><creatorcontrib>Oxvig, Claus</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of immunological methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mikkelsen, Jakob H.</au><au>Steffensen, Lasse B.</au><au>Oxvig, Claus</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species</atitle><jtitle>Journal of immunological methods</jtitle><addtitle>J Immunol Methods</addtitle><date>2014-02</date><risdate>2014</risdate><volume>404</volume><spage>33</spage><epage>40</epage><pages>33-40</pages><issn>0022-1759</issn><eissn>1872-7905</eissn><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.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>24333852</pmid><doi>10.1016/j.jim.2013.12.002</doi><tpages>8</tpages></addata></record> |
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| subjects | Affinity maturation Amino Acid Sequence Animals Antibody Affinity Antibody Specificity Conserved Sequence Epitopes - chemistry Epitopes - immunology Female Formaldehyde Humans Immunoglobulin G - biosynthesis Immunoglobulin G - immunology Immunohistochemistry Immunohistochemistry - methods Mice Molecular Sequence Data Paraffin Embedding Pregnancy Pregnancy-Associated Plasma Protein-A - analysis Pregnancy-Associated Plasma Protein-A - immunology Pregnancy-associated plasma-protein-A Recombinant antibody Recombinant Proteins - biosynthesis Recombinant Proteins - immunology Sequence Alignment Single-Chain Antibodies - biosynthesis Single-Chain Antibodies - immunology Swine Tissue Fixation |
| title | Development of a recombinant antibody towards PAPP-A for immunohistochemical use in multiple animal species |
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