IBA Lifesciences

IBA Lifesciences

Biotechnologieforschung

The leading affinity tag in recombinant protein production

Info

IBA Lifesciences is a biotechnology company providing products and custom specific services for life science applications in academia and industry worldwide. We are the original manufacturer and supplier of the Strep-tag®/Strep-Tactin® technology, an affinity chromatography system developed for protein purification. This method is based on one of the strongest non-covalent interactions in nature, which is the interaction of biotin to streptavidin, and opens up a wide range of application possibilities in the purification and analysis of recombinant proteins. Furthermore, the system has been further developed to be used for cell selection from whole blood or other single cell suspensions.

Branche
Biotechnologieforschung
Größe
11–50 Beschäftigte
Hauptsitz
Goettingen
Art
Privatunternehmen
Gegründet
1996
Spezialgebiete
Cell Selection & Expansion- Fab-TACS® und Protein Production & Assay- Strep-tag®

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Beschäftigte von IBA Lifesciences

Updates

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    📅 We are looking forward to the annual PEGS Europe Summit next week in Barcelona and will be happy to see you during our talk and poster session, as well as welcome you at our booth (1507) at the exhibitor hall. As part of the Expression Stream, Day 1, Fabian Mohr, CSO, will present, how magnetic beads distinguished by high binding capacity and specificity can be flexibly applied in screenings, small- and large-scale purifications. During Poster Session A (Tuesday-Wednesday morning), Philipp Henning will introduce the topic of purification of in vivo biotinylated proteins backed up by our latest data. If you would like to schedule a meeting at our booth in advance, please reach out to Dr. Alexandra Nordlohne and Benedikt Ni. #PEGSummit #PEGS2024 #PEGSEurope

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    💡Surface plasmon resonance (SPR) is a powerful method to study biomolecular interactions. Due to its high accuracy and ability to measure samples in high throughput, it plays a major role in research and development of drugs. A crucial step in SPR analysis is the immobilization of the ligand to the surface of the biosensor chip. The immobilization of the ligand can take place via direct covalent coupling to the surface of the chip or by capture with the help of a pre-coated capture molecule. However, the direct covalent immobilization of the ligand can change its biological activity or result in an undirected immobilization with reduced accessibility of the binding sites. The transient immobilization of tagged ligands via affinity capturing molecules overcomes these drawbacks. ➡️ Click here for the comparison of the applicability of the two widely-used affinity tags for measuring binding kinetics via SPR: https://lnkd.in/dQEDe-Y7 #biotech #biotechnology #proteininteraction #proteinstudies #drugdiscovery

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    📝White Paper of the month Choosing an appropriate affinity chromatography system for simple and efficient protein purification is a common question. There are differences between the systems which rarely are clearly represented, making it hard for scientist to reach a decision. ➡️This comprehensive comparison of the most frequently used systems, His-tag and Strep-tag®, explains these differences as well as recommends one system depending on the properties of the target protein, expression host and purification conditions: https://lnkd.in/dB9AS-e6 #molecularbiology #proteinstudies #proteinpurification #affinitychromatography #biotechnology

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    Understanding protein-protein interactions (PPIs) is fundamental to the field of molecular biology and has broad impact in many areas. From the optimization of drug discovery leads to the identification of biomarkers for disease diagnosis and monitoring, PPIs play a critical role in advancing medical research and therapeutic development. ➡️ Read our detailed description and illustration of the key steps to identify and characterize the interaction between two specific proteins and learn how each of these steps can benefit from using Strep-tag® technology here: https://lnkd.in/dXURFcCA #biotech #biotechnology #proteinpurification #proteininteraction #proteinstudies #streptag #drugdiscovery

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    Thanks to its high affinity, Strep-tag® technology is ideal for BLI kinetic analysis and SPR measurements. ➡️ Read more about these methods for measuring binding kinetics in the great summary below and on our homepage https://lnkd.in/dtJGdc9E

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    A Relentless Explorer on the Frontier of Protein Design, Lab Automation and Therapeutics! Let's challenge the status quo together!

    Part 11 of my series on 30 Biophysical Techniques in 30 Days! 🔬 𝗕𝗶𝗼𝗹𝗮𝘆𝗲𝗿 𝗜𝗻𝘁𝗲𝗿𝗳𝗲𝗿𝗼𝗺𝗲𝘁𝗿𝘆 (𝗕𝗟𝗜) 𝗳𝗼𝗿 𝗣𝗿𝗼𝘁𝗲𝗶𝗻 𝗤𝘂𝗮𝗻𝘁𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝗮𝗻𝗱 𝗣𝗿𝗼𝘁𝗲𝗶𝗻-𝗣𝗿𝗼𝘁𝗲𝗶𝗻 𝗜𝗻𝘁𝗲𝗿𝗮𝗰𝘁𝗶𝗼𝗻𝘀 (𝗣𝗣𝗜)  𝗕𝗟𝗜 is a label-free biophysical technique that has revolutionized the study of protein-protein interactions (PPI) and protein quantification. Developed in the early 2000s, BLI uses optical interference to measure binding events in real time, providing fast, reliable data on binding kinetics and affinity (Kd). It’s become an essential tool for studying biomolecular interactions in research and drug discovery. 𝗛𝗼𝘄 𝗕𝗟𝗜 𝗪𝗼𝗿𝗸𝘀: One interacting partner is immobilized on a biosensor tip, which is then dipped into a solution containing its partner. As binding occurs, changes in light interference are detected and converted into real-time data, including association and dissociation rates (Kon and Koff) and affinity (Kd). 𝗠𝗮𝗶𝗻 𝗣𝗿𝗼𝘃𝗶𝗱𝗲𝗿𝘀: Sartorius offers the widely-used Octet series, popular in academia, biotech, and pharma. Gator Bio is emerging with versatile and high-throughput BLI platforms, advancing automation in BLI. 𝗙𝗿𝗼𝗺 𝗠𝘆 𝗣𝗲𝗿𝘀𝗽𝗲𝗰𝘁𝗶𝘃𝗲: 𝗣𝗿𝗼𝘀: 𝗟𝗮𝗯𝗲𝗹-𝗙𝗿𝗲𝗲 𝗮𝗻𝗱 𝗦𝗼𝗹𝘂𝘁𝗶𝗼𝗻-𝗕𝗮𝘀𝗲𝗱: Allows for the study of proteins in their native state, preserving natural binding behavior. 𝗥𝗲𝗮𝗹-𝗧𝗶𝗺𝗲 𝗞𝗶𝗻𝗲𝘁𝗶𝗰 𝗗𝗮𝘁𝗮: Provides fast, accurate measurements of Kon, Koff, and Kd. 𝗛𝗶𝗴𝗵-𝗧𝗵𝗿𝗼𝘂𝗴𝗵𝗽𝘂𝘁: Supports simultaneous analysis of multiple samples (96/384 well plates), making it ideal for screening and research. 𝗖𝗼𝗻𝘀: 𝗦𝘂𝗿𝗳𝗮𝗰𝗲 𝗜𝗺𝗺𝗼𝗯𝗶𝗹𝗶𝘇𝗮𝘁𝗶𝗼𝗻: Immobilizing one partner on the biosensor may affect its binding behavior. Avi-tag and Twin-Strep II tag by IBA Lifesciences are great tags for immobilization. 𝗢𝗽𝘁𝗶𝗺𝗶𝘇𝗮𝘁𝗶𝗼𝗻 𝗳𝗼𝗿 𝗧𝗶𝗴𝗵𝘁 𝗕𝗶𝗻𝗱𝗶𝗻𝗴: For very tight interactions (<20-50 pM), optimizing the loading step, especially with fast Kon, is necessary. 𝗗𝗶𝗱 𝗜 𝗲𝘃𝗲𝗿 𝘂𝘀𝗲 𝘁𝗵𝗶𝘀 𝘁𝗲𝗰𝗵𝗻𝗶𝗾𝘂𝗲: ☑️ I have used this technique ☑️ I am using this technique ☑️ I am planning to use it in the future BLI has become indispensable for real-time protein interaction studies, particularly in antibody development and therapeutic candidate characterization. 𝗪𝗵𝗮𝘁’𝘀 𝘆𝗼𝘂𝗿 𝗲𝘅𝗽𝗲𝗿𝗶𝗲𝗻𝗰𝗲 𝘄𝗶𝘁𝗵 𝗕𝗟𝗜? #Biophysics #BLI #ProteinInteraction #LabTech #Kinetics #30biophys30days 🚀 I’m Nikolay – 𝗔 𝗥𝗲𝗹𝗲𝗻𝘁𝗹𝗲𝘀𝘀 𝗘𝘅𝗽𝗹𝗼𝗿𝗲𝗿 𝗼𝗻 𝘁𝗵𝗲 𝗙𝗿𝗼𝗻𝘁𝗶𝗲𝗿 𝗼𝗳 𝗣𝗿𝗼𝘁𝗲𝗶𝗻 𝗗𝗲𝘀𝗶𝗴𝗻, 𝗟𝗮𝗯 𝗔𝘂𝘁𝗼𝗺𝗮𝘁𝗶𝗼𝗻 𝗮𝗻𝗱 𝗧𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰𝘀 🚀 Driven by an unquenchable curiosity, I’m passionately dedicated to pioneering the latest techniques and innovations in protein design. If you like my content, please click my name and follow me. Image credit: XanTec bioanalytics GmbH

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    🧲 Magnetic beads are a versatile purification and protein-interaction analysis tool. Depending on the experimental conditions, it is possible to shorten the purification protocol and increase protein yield by adjusting specific parameters, such as - bead volume - incubation time - and protein concentration. ➡️ Click here for the corresponding tips, FAQs and data: https://lnkd.in/dAZkPR7Z #biotech #biotechnology #proteinpurification #affinitychromatography #streptag

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    ❓What are the differences between Strep-Tactin® and Strep-Tactin®XT? The two engineered Streptavidin variants, Strep-Tactin® and its high-affinity counterpart Strep-Tactin®XT, differ in their binding affinities towards Strep-tag® and Twin-Strep-tag® peptides, as well as usability in different analytical applications, protein purification efficiency, yield, costs per mg of protein, and resin stability. ➡️ Learn more about the differences between the two ligands here: https://lnkd.in/dRjAptMW #biotech #biotechnology #proteinpurification #affinitychromatography #streptag

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    ❓ What are the different types of magnetic beads offered by IBA and what is their intended use? 🧲Magnetic beads are one of the most versatile protein purification tools. The magnetic core allows them to be separated from the supernatant with a magnet. This eliminates centrifugation steps and enables quick and easy handling during batch purification. Besides batch protein purification, magnetic beads can be used for interaction studies via immunoprecipitation, BioID or Pull-Down assays, in high-throughput applications, or even for cell isolation. We currently have 3 different types of magnetic beads in our product portfolio: 🔹MagStrep® Strep-Tactin®XT beads – Purification of Strep-tag®II and Twin-Strep-tag® fusion proteins, Ø 30 µm, magnetic core coated with 6 % agarose 🔹MagStrep® Strep-Tactin® beads - Purification of biotinylated, Strep-tag®II and Twin-Strep-tag® fusion proteins, Ø 30 µm, magnetic core coated with 6 % agarose 🔹Strep-Tactin® Magnetic Microbeads - Multimerization of Strep-tag®II and Twin-Strep-tag® fusion proteins for cell isolation, Ø 1-3 µm, magnetic microspheres #biotech #biotechnology #proteinpurification #affinitychromatography

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