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IBA Lifesciences GmbH
Primary Product Categories
- Cell Selection and Expansion
- Exosomes Isolation
- Protein Production and Assays
- Custom Services
IBA Lifesciences GmbH – Protein and Cell Isolation Tools
For more than two decades IBA high quality products for life science research in academia and industry based on their proprietary Strep-tag® technology. The product portfolio offers solutions for the entire production chain of recombinant proteins, from cloning, transfection, protein expression and purification, to detection, immobilization, and assays as well as innovative cell isolation and expansion tools.
Cell Selection & Expansion
The Strep-tag® technology provides methods for isolating cells via their surface markers or via their antigen specificity. It allows label-free positive cell isolation targeting the surface markers via three different methods: Affinity chromatographic, magnetic, or fluorescent cell separation. For surface marker specific cell isolation, the Fab-based Traceless Affinity Cell Selection (Fab-TACS®) technology utilizes a non-magnetic and fully reversible column-based immune affinity chromatography. This delivers label-free, non-activated target cells in a standardized manner of highly reproducible quality. Isolated cells are suitable for all further immunologic or cell biologic investigations including cell-based diagnostics or assays, e.g. pharmacological analysis of drug levels in the isolated cell fraction. Cells can also be isolated according to their antigen specificity using major histocompatibility complexes (MHCs) that present a specific peptide/antigen to target T cells of interest, this approach is called MHC I Streptamer®. Further, IBA provides completely reversible reagents for stimulation & expansion of T cells. All reagents preserve the cells’ full effector function and ensure highest viability.
Protein Production & Assays
The Strep-tag® system enables cloning, expression, detection, purification, and immobilization of recombinant proteins. The highly specific interaction of the Strep-tag®II or Twin-Strep-tag® with Strep-Tactin® or its high affinity variant Strep-Tactin®XT ensures efficient one-step purification of the protein of interest in unparalleled purity even from crude cell lysates. Depending on the application and properties of the protein of interest one can combine the different tags and Strep-Tactin® variants according to the required affinity.
The further developed Strep-Tactin®XT provides extra tight binding to Twin-Strep-tag® fullfils the high demands of protein interaction analysis or assays and downstream applications like SPR, thus covering all steps from purification to immobilization efficiently. This opens new possibilities in the pharmaceutical and biotech sector for, e.g., screening of new diagnostic targets and the development of diagnostic assays.
With over 20 years of experience IBA also offers customized solutions. Custom protein production service includes cloning of the desired DNA into an expression vector, protein expression of the desired expression construct and protein purification via our proprietary Strep-tag® technology. Furthermore, they develop and produce MHC I Streptamer® reagents with your specific allele and antigen.
Links and Resources
- Application note : BLI&SPR with Strep-TactinXT
- Application note: Combining MHC-I and CD8+Fab-Streptamer Reagents
- Application Note: Depletion of cell populations from different samples
- Application note: Label-Free Central Memory T-cells
- Application note: Label-Free T-Lymphocytes
- Application Note: Negative cell selection using affinity chromatography
- Application note: Specific Elution+Avoidance of Contaminations in BioId
- Application note: Strep-Tactin-hc-vs-Strep-Tactin-XT
- Application note: Strep-TactinXT high capacity
- Application note: Strep-TactinXT vs. His-tag
- Application note: Strep-TactinXT vs. Strep-Tactin
- Product overview: IBA-Lifesciences
- White paper: Comparison protein purification systems
- White paper: Transient expression in mammalian cells
- White Paper: UnderstandingThe World of MHC I Multimers
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