IBA Lifesciences is a biotechnology company providing products and custom specific services for life science applications in academia and industry worldwide.[1] IBA focusses on two business segments: cell selection and protein purification.[2]
The company is the original manufacturer and supplier of the Strep-tag/Strep-Tactin technology, an affinity chromatography system developed for protein purification.[3]
The method is based on one of the strongest non-covalent interactions in nature, which is the interaction of biotin to streptavidin. An intrinsic binding affinity of the Strep-tag towards Strep-Tactin results in a highly specific interaction, which enables the isolation and purification of sensitive proteins in a native state as wells as intact protein complexes, respectively.[4][5] The technology was patented by the Max Planck Society (former “Garching Innovations”) and later assigned to IBA.[6][7]
Recently, the method was further developed to be used for cell selection from whole blood or other single cell suspensions.[8]
Products and technologies
Cell Selection & Expansion
IBA has developed an affinity chromatography system for non-magnetic isolation of peripheral blood mononuclear cells, T cells, B cells and other cells of interest. This technology is known as Fab-TACS (Traceless Affinity Cell Selection) and is based on Strep-tagged Fab fragments, which reversibly capture and release the target cells. This delivers label-free, non-activated cells suitable for immunologic or cell biological assays. The technology can be used with manual gravity flow columns as well as with the automated cell selection device FABian.[9]
Isolated and purified cells are being deployed for basic research as well as diagnostic applications.[10][11]
The Streptamers for cell expansion enable the controlled stimulation of T cells. They consist of non-magnetic soluble protein complexes generated by multimerization of αCD3- and αCD28 Fab-Streps with a Strep-Tactin multimer. The reversible reagents can be easily removed from the cells by the addition of biotin. This allows to regulate the extent of stimulation precisely and to study functional and label-free activated T cells.
This can be used for i.e. drug screening, diagnostic assays, immobilization and interaction studies. Due to its small size and biochemically almost inert character, the Strep-tag does not influence protein folding, secretion and function.[17][18]
The latest generation of the system is called Strep-Tactin XT. In combination with the Twin Strep-tag it binds the recombinant protein of interest with an extremely high affinity. This results in improved batch purification runs, higher yields of the expressed recombinant protein and a versatile approach for the immobilization on solid surfaces like beads, slides/arrays or microplates.
History
1996 - Institut für Bioanalytik GmbH was founded by Herbert Stadler,
IBA introduces Strep-tag products
2011 - Innovation Award for Streptamer cell isolation technology [21]
2012 - IBA introduces Fab-TACS (Formerly known as T-CATCH) column based cell purification
2014 - IBA earned its ISO 9001:2008 certification for Quality Management Standard,[22] IBA introduces Strep-Tactin XT products
2015 - 6th foreign Trade Award of Lower Saxony (Germany),[23] IBA launches MEXi mammalian expression system
2016 - IBA introduces cell selection device FABian [24]
Awards & Sponsorship
In 2011 IBA was granted multiple local innovation awards, e.g. for its Streptamer technology, which allows reversible isolation and staining of antigen-specific T cells.[25][26] Additionally, a diagnostic test developed by IBA and Fassisi for veterinary diseases was chosen as one of the top five innovations by the county of Göttingen in 2015.[27] Furthermore, the company honors young scientists and participated in research consortia as well.[28][29][30]
Structure
IBA Lifesciences is a limited liability company (referred to as GmbH in Germany). The officers of the company are Dr. Herbert Stadler (Founder and President), Dr. Mike Rothe (CEO) and Dr. Joachim Bertram (CSO). Headquartered in Göttingen, Germany with locations in Leipzig, Munich (both Germany) and Saint Louis (United States).
^Schmidt, T. G.; Skerra, A. (2007). "The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins". Nat Protoc. 2 (6): 1528–1535. doi:10.1038/nprot.2007.209. PMID17571060.
^Schmidt, T. G.; Skerra, A. (2007). "The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins". Nat Protoc. 2 (6): 1528–1535. doi:10.1038/nprot.2007.209. PMID17571060.
^Skerra, A.; Schmidt, T. G. (2000). "Use of the Strep- tag and streptavidin for detection and purification of recombinant proteins". Use of the strep-tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol. Vol. 326. pp. 271–304. doi:10.1016/S0076-6879(00)26060-6. ISBN978-0-12-182227-9. PMID11036648.
^Pelák, O.; Kužílková, D.; Thürner, D.; Kiene, M. L.; Stanar, K.; Stuchlý, J.; Vášková, M.; Starý, J.; Hrušák, O.; Stadler, H.; Kalina, T. (2016). "Lymphocyte enrichment using CD81-targeted immunoaffinity matrix". Cytometry A. 91A: 62–72.
^Pelák, O.; Kužílková, D.; Thürner, D.; Kiene, M. L.; Stanar, K.; Stuchlý, J.; Vášková, M.; Starý, J.; Hrušák, O.; Stadler, H.; Kalina, T. (2016). "Lymphocyte enrichment using CD81-targeted immunoaffinity matrix". Cytometry A. 91A: 62–72.
^Neudorfer, J; Schmidt, B; Huster, K. M.; Ander, F.; Schiemann, M.; Holzapfel, G.; Schmidt, T.; Germeroth, L.; Wagner, H.; Peschel, C.; Busch, D. H.; Bernhard, H. (2007). "Reversible HLA multimers (Streptamers) for the isolation of human cytotoxic T lymphocytes functionally active against tumor- and virus-derived antigens". J Immunol Methods. 320 (1–2): 119–131. doi:10.1016/j.jim.2007.01.001. PMID17306825.
^Schmidt, T. G.; Skerra, A. (2007). "The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins". Nat Protoc. 2 (6): 1528–1535. doi:10.1038/nprot.2007.209. PMID17571060.
^Schmidt, T.; Skerra, A. (2015). The Strep-tag system for one-step affinity purification of proteins from mammalian cell culture. Methods Mol Biol. Vol. 1286. pp. 83–95.
^Schmidt, T.; Skerra, A. (1994). "One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin". J Chromatogr A. 676 (2): 337–345. doi:10.1016/0021-9673(94)80434-6. PMID7921186.
^Schmidt, T.; Koepke, J.; Frank, R.; Skerra, A. (1996). "Molecular interaction between the Strep-tag affinity peptide and its cognate target, streptavidin". J Mol Biol. 255 (5): 753–766. doi:10.1006/jmbi.1996.0061. PMID8636976.
^Skerra, A.; Schmidt, T. G. (2000). "Use of the Strep- tag and streptavidin for detection and purification of recombinant proteins". Use of the strep-tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol. Vol. 326. pp. 271–304. doi:10.1016/S0076-6879(00)26060-6. ISBN978-0-12-182227-9. PMID11036648.
