| URL: | https://www.sdab-db.ca/ |
| Full name: | The Single Domain Antibody Database |
| Description: | We have established the first dedicated single domain antibody repository and database. The database hosts a large collection of natural and synthetic camelid single domain antibody sequences from literature sources, other online repositories (PDB and NCBI), and manual entries from users. |
| Year founded: | 2018 |
| Last update: | |
| Version: | v1.4.1 |
| Accessibility: |
Accessible
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| Country/Region: | Canada |
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| University/Institution: | University of Lethbridge |
| Address: | Alberta RNA Research and Training Institute, Department of Chemistry and Biochemistry , University of Lethbridge , Lethbridge , Alberta T1K 3M4 , Canada. |
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| Country/Region: | Canada |
| Contact name (PI/Team): | Hans-Joachim Wieden |
| Contact email (PI/Helpdesk): | hj.wieden@uleth.ca |
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sdAb-DB: The Single Domain Antibody Database. [PMID: 30441908]
The Single Domain Antibody Database, or sdAb-DB, ( www.sdab-db.ca ) is the first freely available repository for single domain antibodies and related classes of proteins. Due to their small size, modular structure, and ease of expression, single domain antibodies (sdAb) have a wide range of applications, including as a rational design tool, and are therefore of great interest for synthetic biologists and bioengineers. However, to enable effective use and sharing of existing sdAbs, including those with engineered functions ( e.g., fusions with fluorescent proteins), as well as the rational design and engineering of new sdAbs, it is necessary to have access to sequences and experimental data. We have therefore developed a publicly available, sdAb-focused database, providing access to manually curated sdAb data from protein databases, published scientific articles, and user submissions. The sdAb-DB is an open-source repository and sharing platform for the sdAb community, providing access to performance data and basic bioinformatic tools for use with previously described and validated sdAbs, as well as for the engineering of new sdAb-based designs and proteins. |