Cube Biotech

🎉 We're excited to be attending the Human Proteome Organization (HUPO) World Congress in Germany! Stop by Booth 3 and say hello 👋. Or arrange a meeting with our Strategic Partnership Managers, Thomas Perkins, Jr. and Sebastian Lühn – they're looking forward to answering your questions and are happy to assist you! 🤝 See you at HUPO! 🔬💼 #HUPO2024

Our co-founder and CSO Jan Kubicek had the opportunity to share some insights at Discovery on Target 2024 about one of the biggest challenges in membrane protein research: stabilization. In our talk, we discussed how next-generation NativeMP copolymers are paving the way for more efficient stabilization of membrane proteins into native nanodiscs, preserving their natural environment and functionality. If you’re working in biotherapeutics or are interested in membrane protein research, this approach could be a game changer! Check out the full talk here: https://lnkd.in/eKZ8ngFM

The COVID-19 pandemic, resulting in over 5 million deaths, has highlighted the urgent 𝗻𝗲𝗲𝗱 𝗳𝗼𝗿 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝗮𝗽𝗽𝗿𝗼𝗮𝗰𝗵𝗲𝘀, 𝘄𝗶𝘁𝗵 𝘁𝗵𝗲 𝘃𝗶𝗿𝘂𝘀'𝘀 𝘀𝗽𝗶𝗸𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝗲𝗺𝗲𝗿𝗴𝗶𝗻𝗴 𝗮𝘀 𝗮 𝗽𝗿𝗼𝗺𝗶𝘀𝗶𝗻𝗴 𝗰𝗮𝗻𝗱𝗶𝗱𝗮𝘁𝗲, 𝗳𝗼𝗿 𝘁𝗵𝗲 𝗱𝗲𝘃𝗲𝗹𝗼𝗽𝗺𝗲𝗻𝘁 𝗼𝗳 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝘁𝗮𝗿𝗴𝗲𝘁𝘀.   🇵🇦🇵🇪🇷 🇴🇫 🇹🇭🇪 🇲🇴🇳🇹🇭 - 𝘐𝘯𝘴𝘦𝘤𝘵 𝘤𝘦𝘭𝘭 𝘦𝘹𝘱𝘳𝘦𝘴𝘴𝘪𝘰𝘯 𝘢𝘯𝘥 𝘱𝘶𝘳𝘪𝘧𝘪𝘤𝘢𝘵𝘪𝘰𝘯 𝘰𝘧 𝘳𝘦𝘤𝘰𝘮𝘣𝘪𝘯𝘢𝘯𝘵 𝘚𝘈𝘙𝘚-𝘊𝘖𝘝-2 𝘴𝘱𝘪𝘬𝘦 𝘱𝘳𝘰𝘵𝘦𝘪𝘯𝘴 𝘵𝘩𝘢𝘵 𝘥𝘦𝘮𝘰𝘯𝘴𝘵𝘳𝘢𝘵𝘦 𝘈𝘊𝘌2 𝘣𝘪𝘯𝘥𝘪𝘯𝘨 (2022)   𝗝𝗼𝗶𝗻 𝘂𝘀 𝗮𝘀 𝘄𝗲 𝗱𝗲𝗹𝘃𝗲 𝗶𝗻𝘁𝗼 𝗮 𝗺𝗲𝘁𝗵𝗼𝗱 𝘁𝗵𝗮𝘁 𝗼𝗳𝗳𝗲𝗿𝘀 𝗮 𝘀𝗰𝗮𝗹𝗮𝗯𝗹𝗲, 𝗰𝗼𝘀𝘁-𝗲𝗳𝗳𝗲𝗰𝘁𝗶𝘃𝗲 𝗽𝗹𝗮𝘁𝗳𝗼𝗿𝗺 𝗳𝗼𝗿 𝗽𝗿𝗼𝗱𝘂𝗰𝗶𝗻𝗴 𝗳𝘂𝗻𝗰𝘁𝗶𝗼𝗻𝗮𝗹 𝘀𝗽𝗶𝗸𝗲 𝗽𝗿𝗼𝘁𝗲𝗶𝗻𝘀 𝗳𝗼𝗿 𝗿𝗲𝘀𝗲𝗮𝗿𝗰𝗵 𝗮𝗻𝗱 𝘁𝗵𝗲𝗿𝗮𝗽𝗲𝘂𝘁𝗶𝗰 𝗱𝗲𝘃𝗲𝗹𝗼𝗽𝗺𝗲𝗻𝘁. Struble 𝘦𝘵 𝘢𝘭. from the Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Media Center, developed and optimized a robust SARS-CoV-2 spike protein expression and purification protocol using insect cells.    The study focused on four recombinant SARS-CoV-2 spike protein constructs, including the spike receptor-binding domain (S-RBD-eGFP) and various spike ectodomains, with and without stabilizing mutations. The team tested the protein yield in two insect cell lines, Sf9 and Tni, demonstrating higher yields in Tni cells. The purified spike proteins were functional, glycosylated, and capable of binding to the ACE2 receptor, with validation through flow cytometry.     https://lnkd.in/eisiK2jt   Lucas Struble, Audrey Smith, William E. Lutz Nebraska, Gabrielle Grubbs, Sagar Satish, Ken Bayles, Dr. Prakash Radhakrishnan, Surender Khurana, Dalia El-Gamal, Gloria Borgstahl -University of Nebraska Medical Center- We are dedicating a spot in our "Paper of the Month" series to this exciting research. Check it out on our website: https://lnkd.in/eUQds2qu    For the purification procedure of the different SARS-CoV-2 spike protein constructs, 𝘁𝗵𝗲 𝘀𝘁𝘂𝗱𝘆 𝘁𝗲𝘀𝘁𝗲𝗱 𝘁𝗵𝗿𝗲𝗲 𝗜𝗠𝗔𝗖 𝗿𝗲𝘀𝗶𝗻𝘀, 𝗳𝗶𝗻𝗱𝗶𝗻𝗴 𝘁𝗵𝗮𝘁 𝗜𝗡𝗗𝗜𝗚𝗢-𝗡𝗶 𝗿𝗲𝘀𝗶𝗻 𝘄𝗮𝘀 𝘁𝗵𝗲 𝗺𝗼𝘀𝘁 𝗲𝗳𝗳𝗶𝗰𝗶𝗲𝗻𝘁 𝗱𝘂𝗲 𝘁𝗼 𝗶𝘁𝘀 𝗿𝗲𝘀𝗶𝘀𝘁𝗮𝗻𝗰𝗲 𝘁𝗼 𝗻𝗶𝗰𝗸𝗲𝗹 𝗶𝗼𝗻 𝗹𝗲𝗮𝗰𝗵𝗶𝗻𝗴 𝗮𝗻𝗱 𝗿𝗲𝗱𝘂𝗰𝗲𝗱 𝗶𝗺𝗽𝘂𝗿𝗶𝘁𝘆 𝗰𝗼-𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻, 𝗰𝗼𝗺𝗽𝗮𝗿𝗲𝗱 𝘁𝗼 𝘄𝗲𝗹𝗹-𝗸𝗻𝗼𝘄𝗻 𝗰𝗼𝗺𝗽𝗲𝘁𝗶𝘁𝗼𝗿𝘀.  

The 2024 Nobel Prize in Chemistry has celebrated groundbreaking work in protein science, recognizing David Baker for creating new kinds of proteins and Demis Hassabis and John Jumper for revolutionizing protein structure prediction with AlphaFold2. Their discoveries are truly a game-changer in structural biology. But as I’ve discussed at recent conferences, the challenge now lies in translating these computational models into real-world structures. Many times, what we see in silico doesn’t fully reflect real-life protein behavior—and one key missing piece might be the native lipid environment. Lipids are critical. Proteins do not exist in isolation; they often interact with lipids, which play a fundamental role in preserving the protein’s structure and function. We must not overlook this factor when validating AI-predicted models in the lab. These discoveries are certainly opening up new horizons, but the wet lab work remains vital to ensure these models meet biological reality. It's up to us to prove these predictions and fully unlock the potential of AI-driven protein science. At Cube Biotech, we're committed to providing the tools and insights necessary to bridge this gap. Through our NativeMP™ platform, we enable researchers to work with membrane proteins in their native lipid environment, getting as close as possible to the real structure. Let's talk more about these advancements and potential collaborations at upcoming events. I'll be attending Festival of Biologics in Basel. Looking forward to connecting! #ProteinScience #NobelPrize2024 #MembraneProteins #StructuralBiology

NOW LIVE: Join us to learn more about cell-free, cryo-EM, GPCRs, and structural biology with Dr. Frank Bernhard from Goethe University Frankfurt, Germany 🎬

🚨 Last Day to Visit Us at Discovery on Target (Booth 503)! If you're looking for membrane protein drug targets, today is your final chance to stop by! We’d love to meet you in Boston with Jan Kubicek, Barbara Maertens, DIDIER DARGENT, and Daniel Turman.   💡 Don't miss Barbara M.'s poster presentation this morning at DOT A21 on Next Generation Copolymers for membrane protein characterization in near-native conditions.   Come chat with us and explore how we can support your research needs!

📢 Join Our Masterclass with Dr. Frank Bernhard Learn how cell-free expression systems offer rapid pathways to Cryo-EM structures of GPCR complexes. Key Takeaways: - Cell-free expression is a modular system and protocols can be adjusted to different targets. - E. coli lysates represent an affordable and efficient production pipeline giving fast access to non-truncated GPCR structures in active conformation. - Co-translational insertion of membrane proteins into preformed nanoparticles avoids any detergent contacts and reduces sample preparation procedures to less than 24 hours. - Cell-free expression is an interesting alternative platform for the production of membrane proteins that are difficult to synthesize in conventional cell-based expression systems #CryoEM #GPCR #BiophysicalChemistry #MembraneProteins #CellFreeSynthesis #StructuralBiology

NOW LIVE: Join us to learn more about conjugation chemistry, CRM197, immunogens, and immunization with Andrew Lees, Ph.D. 🎬

Working with complex proteins and drug targets like #GPCRs and ion channels can be very challenging. These targets are crucial but notoriously tricky to handle, slowing down research and development progress. If you’re interested in the surrounding #lipids, their interaction with the membrane protein, and physiological temperatures, another layer of complexity is added. Which technologies help you the most in circumventing these issues?

Have you ever wondered which affinity beads you can use for your protein purification system? 𝗗𝗼 𝘆𝗼𝘂 𝘂𝘀𝗲 Ä𝗸𝘁𝗮 𝘀𝘆𝘀𝘁𝗲𝗺𝘀, 𝗡𝗚𝗖 𝗖𝗵𝗿𝗼𝗺𝗮𝘁𝗼𝗴𝗿𝗮𝗽𝗵𝘆 𝘀𝘆𝘀𝘁𝗲𝗺𝘀, 𝗞𝗶𝗻𝗴𝗙𝗶𝘀𝗵𝗲𝗿 𝘀𝘆𝘀𝘁𝗲𝗺𝘀 𝗼𝗿 𝗮𝘂𝘁𝗼𝗺𝗮𝘁𝗲𝗱 𝗹𝗶𝗾𝘂𝗶𝗱 𝗵𝗮𝗻𝗱𝗹𝗶𝗻𝗴 𝘀𝘆𝘀𝘁𝗲𝗺𝘀 𝗳𝗼𝗿 𝘆𝗼𝘂𝗿 𝗮𝗳𝗳𝗶𝗻𝗶𝘁𝘆 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻?   ÄKTA, NGC Chromatography, or KingFisher are advantageous for protein purification with affinity beads. These systems automate the most critical steps, such as binding, washing, and elution, and ensure precision and reproducibility. ÄKTA and NGC systems allow customization of purification conditions, while KingFisher systems automate magnetic bead-based protein capture. Liquid handling platforms streamline sample preparation or resin loading, improve consistency, and reduce errors. These systems improve throughput while maintaining bead integrity, making them valuable for efficient and scalable protein purification.     𝗔𝗴𝗮𝗿𝗼𝘀𝗲 𝗯𝗲𝗮𝗱𝘀 𝗮𝗻𝗱 𝗠𝗮𝗴𝗕𝗲𝗮𝗱𝘀 𝗱𝗲𝘀𝗶𝗴𝗻𝗲𝗱 𝗳𝗼𝗿 𝗛𝗶𝘀-𝘁𝗮𝗴 𝗮𝗳𝗳𝗶𝗻𝗶𝘁𝘆, 𝗥𝗵𝗼𝟭𝗗𝟰-𝘁𝗮𝗴 𝗮𝗳𝗳𝗶𝗻𝗶𝘁𝘆, 𝗦𝘁𝗿𝗲𝗽-𝘁𝗮𝗴® 𝗮𝗳𝗳𝗶𝗻𝗶𝘁𝘆, 𝗼𝗿 𝗚𝗦𝗧-𝘁𝗮𝗴 𝗮𝗳𝗳𝗶𝗻𝗶𝘁𝘆 𝗳𝗿𝗼𝗺 𝗖𝘂𝗯𝗲 𝗕𝗶𝗼𝘁𝗲𝗰𝗵 𝗮𝗿𝗲 𝗵𝗶𝗴𝗵𝗹𝘆 𝘃𝗲𝗿𝘀𝗮𝘁𝗶𝗹𝗲 𝗮𝗻𝗱 𝗰𝗼𝗺𝗽𝗮𝘁𝗶𝗯𝗹𝗲 𝘄𝗶𝘁𝗵 𝘁𝗵𝗲 𝘀𝘆𝘀𝘁𝗲𝗺𝘀 𝗺𝗲𝗻𝘁𝗶𝗼𝗻𝗲𝗱. 𝗧𝗵𝗲𝘀𝗲 𝗯𝗲𝗮𝗱𝘀 𝗮𝗿𝗲 𝗽𝗮𝗿𝘁𝗶𝗰𝘂𝗹𝗮𝗿𝗹𝘆 𝗲𝗳𝗳𝗲𝗰𝘁𝗶𝘃𝗲 𝗶𝗻 𝗮𝘂𝘁𝗼𝗺𝗮𝘁𝗶𝗻𝗴 𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝗽𝗿𝗼𝗰𝗲𝘀𝘀𝗲𝘀 𝗯𝘂𝘁 𝗮𝗹𝘀𝗼 𝘄𝗼𝗿𝗸 𝗳𝗹𝗮𝘄𝗹𝗲𝘀𝘀 𝗶𝗻 𝗯𝗮𝘁𝗰𝗵 𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻 𝘀𝘆𝘀𝘁𝗲𝗺𝘀.   Would you like to delve deeper into the range of affinity beads and their properties? Our Purification Technology Platform is a valuable resource for this: https://lnkd.in/eUu3HNZU Are you more interested in phosphopeptide enrichment? Click on this link: https://lnkd.in/em7UBc37