The Experts below are selected from a list of 116814 Experts worldwide ranked by ideXlab platform
Silvia Saragozza - One of the best experts on this subject based on the ideXlab platform.
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recombinant renewable Polyclonal Antibodies
mAbs, 2015Co-Authors: Fortunato Ferrara, Sara Dangelo, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Fridtjof Lundjohansen, Silvia SaragozzaAbstract:Described herein are methods that combine phage and yeast display to create Polyclonal Antibodies that are renewable, and when amplified over 100 million fold, maintain diversity without loss of representation of any of the Antibodies present. The antibody representation remains essentially constant, as confirmed by deep sequencing. The provided methods allow generation, use and propagation of Polyclonal Antibodies, without concern that representation is lost. Furthermore, because the derivation of the Polyclonal pool is carried out in vitro using phage and yeast display, it is possible in various embodiments to eliminate reactivities that are considered undesirable. Additionally, the Polyclonal pool can be enriched for higher affinity Antibodies.
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Recombinant renewable Polyclonal Antibodies.
mAbs, 2015Co-Authors: Fortunato Ferrara, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Sara D'angelo, Fridtjof Lund-johansen, Silvia SaragozzaAbstract:Only a small fraction of the Antibodies in a traditional Polyclonal antibody mixture recognize the target of interest, frequently resulting in undesirable polyreactivity. Here, we show that high-quality recombinant Polyclonals, in which hundreds of different Antibodies are all directed toward a target of interest, can be easily generated in vitro by combining phage and yeast display. We show that, unlike traditional Polyclonals, which are limited resources, recombinant Polyclonal Antibodies can be amplified over one hundred million-fold without losing representation or functionality. Our protocol was tested on 9 different targets to demonstrate how the strategy allows the selective amplification of Antibodies directed toward desirable target specific epitopes, such as those found in one protein but not a closely related one, and the elimination of Antibodies recognizing common epitopes, without significant loss of diversity. These recombinant renewable Polyclonal Antibodies are usable in different assays, and can be generated in high throughput. This approach could potentially be used to develop highly specific recombinant renewable Antibodies against all human gene products.
Fortunato Ferrara - One of the best experts on this subject based on the ideXlab platform.
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recombinant renewable Polyclonal Antibodies
mAbs, 2015Co-Authors: Fortunato Ferrara, Sara Dangelo, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Fridtjof Lundjohansen, Silvia SaragozzaAbstract:Described herein are methods that combine phage and yeast display to create Polyclonal Antibodies that are renewable, and when amplified over 100 million fold, maintain diversity without loss of representation of any of the Antibodies present. The antibody representation remains essentially constant, as confirmed by deep sequencing. The provided methods allow generation, use and propagation of Polyclonal Antibodies, without concern that representation is lost. Furthermore, because the derivation of the Polyclonal pool is carried out in vitro using phage and yeast display, it is possible in various embodiments to eliminate reactivities that are considered undesirable. Additionally, the Polyclonal pool can be enriched for higher affinity Antibodies.
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Recombinant renewable Polyclonal Antibodies.
mAbs, 2015Co-Authors: Fortunato Ferrara, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Sara D'angelo, Fridtjof Lund-johansen, Silvia SaragozzaAbstract:Only a small fraction of the Antibodies in a traditional Polyclonal antibody mixture recognize the target of interest, frequently resulting in undesirable polyreactivity. Here, we show that high-quality recombinant Polyclonals, in which hundreds of different Antibodies are all directed toward a target of interest, can be easily generated in vitro by combining phage and yeast display. We show that, unlike traditional Polyclonals, which are limited resources, recombinant Polyclonal Antibodies can be amplified over one hundred million-fold without losing representation or functionality. Our protocol was tested on 9 different targets to demonstrate how the strategy allows the selective amplification of Antibodies directed toward desirable target specific epitopes, such as those found in one protein but not a closely related one, and the elimination of Antibodies recognizing common epitopes, without significant loss of diversity. These recombinant renewable Polyclonal Antibodies are usable in different assays, and can be generated in high throughput. This approach could potentially be used to develop highly specific recombinant renewable Antibodies against all human gene products.
Peter Hraber - One of the best experts on this subject based on the ideXlab platform.
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recombinant renewable Polyclonal Antibodies
mAbs, 2015Co-Authors: Fortunato Ferrara, Sara Dangelo, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Fridtjof Lundjohansen, Silvia SaragozzaAbstract:Described herein are methods that combine phage and yeast display to create Polyclonal Antibodies that are renewable, and when amplified over 100 million fold, maintain diversity without loss of representation of any of the Antibodies present. The antibody representation remains essentially constant, as confirmed by deep sequencing. The provided methods allow generation, use and propagation of Polyclonal Antibodies, without concern that representation is lost. Furthermore, because the derivation of the Polyclonal pool is carried out in vitro using phage and yeast display, it is possible in various embodiments to eliminate reactivities that are considered undesirable. Additionally, the Polyclonal pool can be enriched for higher affinity Antibodies.
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Recombinant renewable Polyclonal Antibodies.
mAbs, 2015Co-Authors: Fortunato Ferrara, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Sara D'angelo, Fridtjof Lund-johansen, Silvia SaragozzaAbstract:Only a small fraction of the Antibodies in a traditional Polyclonal antibody mixture recognize the target of interest, frequently resulting in undesirable polyreactivity. Here, we show that high-quality recombinant Polyclonals, in which hundreds of different Antibodies are all directed toward a target of interest, can be easily generated in vitro by combining phage and yeast display. We show that, unlike traditional Polyclonals, which are limited resources, recombinant Polyclonal Antibodies can be amplified over one hundred million-fold without losing representation or functionality. Our protocol was tested on 9 different targets to demonstrate how the strategy allows the selective amplification of Antibodies directed toward desirable target specific epitopes, such as those found in one protein but not a closely related one, and the elimination of Antibodies recognizing common epitopes, without significant loss of diversity. These recombinant renewable Polyclonal Antibodies are usable in different assays, and can be generated in high throughput. This approach could potentially be used to develop highly specific recombinant renewable Antibodies against all human gene products.
Tiziano Gaiotto - One of the best experts on this subject based on the ideXlab platform.
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recombinant renewable Polyclonal Antibodies
mAbs, 2015Co-Authors: Fortunato Ferrara, Sara Dangelo, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Fridtjof Lundjohansen, Silvia SaragozzaAbstract:Described herein are methods that combine phage and yeast display to create Polyclonal Antibodies that are renewable, and when amplified over 100 million fold, maintain diversity without loss of representation of any of the Antibodies present. The antibody representation remains essentially constant, as confirmed by deep sequencing. The provided methods allow generation, use and propagation of Polyclonal Antibodies, without concern that representation is lost. Furthermore, because the derivation of the Polyclonal pool is carried out in vitro using phage and yeast display, it is possible in various embodiments to eliminate reactivities that are considered undesirable. Additionally, the Polyclonal pool can be enriched for higher affinity Antibodies.
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Recombinant renewable Polyclonal Antibodies.
mAbs, 2015Co-Authors: Fortunato Ferrara, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Sara D'angelo, Fridtjof Lund-johansen, Silvia SaragozzaAbstract:Only a small fraction of the Antibodies in a traditional Polyclonal antibody mixture recognize the target of interest, frequently resulting in undesirable polyreactivity. Here, we show that high-quality recombinant Polyclonals, in which hundreds of different Antibodies are all directed toward a target of interest, can be easily generated in vitro by combining phage and yeast display. We show that, unlike traditional Polyclonals, which are limited resources, recombinant Polyclonal Antibodies can be amplified over one hundred million-fold without losing representation or functionality. Our protocol was tested on 9 different targets to demonstrate how the strategy allows the selective amplification of Antibodies directed toward desirable target specific epitopes, such as those found in one protein but not a closely related one, and the elimination of Antibodies recognizing common epitopes, without significant loss of diversity. These recombinant renewable Polyclonal Antibodies are usable in different assays, and can be generated in high throughput. This approach could potentially be used to develop highly specific recombinant renewable Antibodies against all human gene products.
Leslie Naranjo - One of the best experts on this subject based on the ideXlab platform.
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recombinant renewable Polyclonal Antibodies
mAbs, 2015Co-Authors: Fortunato Ferrara, Sara Dangelo, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Fridtjof Lundjohansen, Silvia SaragozzaAbstract:Described herein are methods that combine phage and yeast display to create Polyclonal Antibodies that are renewable, and when amplified over 100 million fold, maintain diversity without loss of representation of any of the Antibodies present. The antibody representation remains essentially constant, as confirmed by deep sequencing. The provided methods allow generation, use and propagation of Polyclonal Antibodies, without concern that representation is lost. Furthermore, because the derivation of the Polyclonal pool is carried out in vitro using phage and yeast display, it is possible in various embodiments to eliminate reactivities that are considered undesirable. Additionally, the Polyclonal pool can be enriched for higher affinity Antibodies.
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Recombinant renewable Polyclonal Antibodies.
mAbs, 2015Co-Authors: Fortunato Ferrara, Tiziano Gaiotto, Leslie Naranjo, Hongzhao Tian, S Graslund, Elena Dobrovetsky, Peter Hraber, Sara D'angelo, Fridtjof Lund-johansen, Silvia SaragozzaAbstract:Only a small fraction of the Antibodies in a traditional Polyclonal antibody mixture recognize the target of interest, frequently resulting in undesirable polyreactivity. Here, we show that high-quality recombinant Polyclonals, in which hundreds of different Antibodies are all directed toward a target of interest, can be easily generated in vitro by combining phage and yeast display. We show that, unlike traditional Polyclonals, which are limited resources, recombinant Polyclonal Antibodies can be amplified over one hundred million-fold without losing representation or functionality. Our protocol was tested on 9 different targets to demonstrate how the strategy allows the selective amplification of Antibodies directed toward desirable target specific epitopes, such as those found in one protein but not a closely related one, and the elimination of Antibodies recognizing common epitopes, without significant loss of diversity. These recombinant renewable Polyclonal Antibodies are usable in different assays, and can be generated in high throughput. This approach could potentially be used to develop highly specific recombinant renewable Antibodies against all human gene products.
