![Identification of dentinogenic cell-specific surface antigens in odontoblast-like cells derived from adult dental pulp | Stem Cell Research & Therapy | Full Text Identification of dentinogenic cell-specific surface antigens in odontoblast-like cells derived from adult dental pulp | Stem Cell Research & Therapy | Full Text](https://media.springernature.com/full/springer-static/image/art%3A10.1186%2Fs13287-019-1232-y/MediaObjects/13287_2019_1232_Fig3_HTML.png)
Identification of dentinogenic cell-specific surface antigens in odontoblast-like cells derived from adult dental pulp | Stem Cell Research & Therapy | Full Text
![Sequence analysis of feline immunoglobulin mRNAs and the development of a felinized monoclonal antibody specific to feline panleukopenia virus | Scientific Reports Sequence analysis of feline immunoglobulin mRNAs and the development of a felinized monoclonal antibody specific to feline panleukopenia virus | Scientific Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41598-017-12725-5/MediaObjects/41598_2017_12725_Fig1_HTML.jpg)
Sequence analysis of feline immunoglobulin mRNAs and the development of a felinized monoclonal antibody specific to feline panleukopenia virus | Scientific Reports
![Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0022175914000052-gr1.jpg)
Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect
![A Mouse Ig κ Domain of Very Unusual Framework Structure Loses Function when Converted to the Consensus (∗) - Journal of Biological Chemistry A Mouse Ig κ Domain of Very Unusual Framework Structure Loses Function when Converted to the Consensus (∗) - Journal of Biological Chemistry](https://els-jbs-prod-cdn.jbs.elsevierhealth.com/cms/attachment/0d3b8e85-1c8a-49d6-b474-79a3a73ed813/gr1_lrg.jpg)
A Mouse Ig κ Domain of Very Unusual Framework Structure Loses Function when Converted to the Consensus (∗) - Journal of Biological Chemistry
![Complete humanization of the mouse immunoglobulin loci enables efficient therapeutic antibody discovery | Nature Biotechnology Complete humanization of the mouse immunoglobulin loci enables efficient therapeutic antibody discovery | Nature Biotechnology](https://media.springernature.com/full/springer-static/image/art%3A10.1038%2Fnbt.2825/MediaObjects/41587_2014_Article_BFnbt2825_Fig1_HTML.jpg)
Complete humanization of the mouse immunoglobulin loci enables efficient therapeutic antibody discovery | Nature Biotechnology
![Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0022175914000052-gr7.jpg)
Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect
![Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect](https://ars.els-cdn.com/content/image/1-s2.0-S0022175914000052-gr5.jpg)
Analysis of heavy and light chain sequences of conventional camelid antibodies from Camelus dromedarius and Camelus bactrianus species - ScienceDirect
![Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains | Scientific Reports Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains | Scientific Reports](https://media.springernature.com/m685/springer-static/image/art%3A10.1038%2Fs41598-019-55805-4/MediaObjects/41598_2019_55805_Fig1_HTML.png)
Antigen-binding affinity and thermostability of chimeric mouse-chicken IgY and mouse-human IgG antibodies with identical variable domains | Scientific Reports
![Amino-acid sequence alignment of the HL4E10 hamster IgG light chain... | Download Scientific Diagram Amino-acid sequence alignment of the HL4E10 hamster IgG light chain... | Download Scientific Diagram](https://www.researchgate.net/profile/Katie-Podshivalova/publication/51181486/figure/fig7/AS:341857633619969@1458516619392/Amino-acid-sequence-alignment-of-the-HL4E10-hamster-IgG-light-chain-with-those-of-other.png)