Cube Biotech

NOW LIVE: Join us to learn more about cell-free expression for the structural and biophysical characterization of complex and challenging proteins and protein complexes with Dr. Alex Snow 🎬

𝗔𝗿𝗲 𝘆𝗼𝘂 𝘂𝘀𝗶𝗻𝗴 Ä𝗸𝘁𝗮 𝗦𝘆𝘀𝘁𝗲𝗺𝘀, 𝗡𝗚𝗖 𝗖𝗵𝗿𝗼𝗺𝗮𝘁𝗼𝗴𝗿𝗮𝗽𝗵𝘆 𝗦𝘆𝘀𝘁𝗲𝗺𝘀, 𝗞𝗶𝗻𝗴𝗙𝗶𝘀𝗵𝗲𝗿 𝗦𝘆𝘀𝘁𝗲𝗺𝘀, 𝗮𝘂𝘁𝗼𝗺𝗮𝘁𝗲𝗱 𝗹𝗶𝗾𝘂𝗶𝗱 𝗵𝗮𝗻𝗱𝗹𝗶𝗻𝗴 𝘀𝘆𝘀𝘁𝗲𝗺𝘀, 𝗼𝗿 𝗯𝗮𝘁𝗰𝗵 𝘀𝘆𝘀𝘁𝗲𝗺𝘀 𝗳𝗼𝗿 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝗽𝘂𝗿𝗶𝗳𝗶𝗰𝗮𝘁𝗶𝗼𝗻? Here's how to optimize your histidine-tagged protein purification process: 𝗢𝘄𝗶𝗻𝗴 𝘁𝗼 𝗶𝘁𝘀 𝘂𝗻𝗶𝗾𝘂𝗲 𝗽𝗿𝗼𝗰𝗲𝘀𝘀𝗶𝗻𝗴, 𝗣𝘂𝗿𝗲𝗖𝘂𝗯𝗲 𝗡𝗶-𝗡𝗧𝗔 𝗔𝗴𝗮𝗿𝗼𝘀𝗲 𝗼𝗳𝗳𝗲𝗿𝘀 𝗮 𝗽𝗿𝗼𝘁𝗲𝗶𝗻 𝗯𝗶𝗻𝗱𝗶𝗻𝗴 𝗰𝗮𝗽𝗮𝗰𝗶𝘁𝘆 𝘂𝗽 𝘁𝗼 𝟯𝟲% 𝗵𝗶𝗴𝗵𝗲𝗿 𝘁𝗵𝗮𝗻 𝗡𝗶-𝗡𝗧𝗔 𝗿𝗲𝘀𝗶𝗻 𝗽𝗿𝗼𝗱𝘂𝗰𝘁𝘀 𝗼𝗳 𝘁𝗵𝗿𝗲𝗲 𝗹𝗲𝗮𝗱𝗶𝗻𝗴 𝗰𝗼𝗺𝗽𝗲𝘁𝗶𝘁𝗼𝗿𝘀, 𝘄𝗲 𝗿𝗲𝗳𝗲𝗿 𝘁𝗼 𝘁𝗵𝗲𝗺 𝗮𝘀 "𝗔"," 𝗕" 𝗮𝗻𝗱 "𝗖".   In our comparative analysis of Ni-NTA resin products, protein isolation was carried out using E. coli lysate and insect cell lysate in a batch system, as you can see in the figure.  PureCube Ni-NTA Agarose demonstrates superior performance compared to three leading competitor materials, establishing it as the premier Ni-NTA resin currently available. This feedback has already been submitted to us by customers.    Additionally, the resin is designed for long-term reuse, ensuring sustained efficiency over years. 

Even though summer hasn't really arrived in Germany yet, we want to offer you some hot science with Dr. Alex Snow from the University of Leeds. ☀️ Alex Snow will present findings and insights of the application of cell-free expression for the structural and biophysical characterization of complex and challenging proteins and protein complexes. Join us on July 10th to learn about his workflows, how to troubleshoot, and what else is happening in protein research. #pioneeringtogether #leeds #cryoem #cellfree #copolymers

Listen up structural biologists and drug discovery experts! We are thrilled to announce a significant breakthrough at Cube Biotech! Leveraging just one of our newest copolymer inventions in our NativeMP™ Platform, we have successfully obtained the very first structure of the ‘Human’ P2X4 membrane protein in its native membrane environment via cryo-EM. P2X4, a crucial player in synaptic transmission and inflammation, holds significant promise in drug discovery, particularly for developing novel therapies for chronic pain and inflammatory diseases. Traditionally, detergents have been the standard method for stabilizing membrane proteins for cryo-EM. However, they fall short of preserving the protein’s native environment, affecting functional stability and further analysis (Schmidpeter et al., 2022 https://lnkd.in/etCdXuSv; Corradi et al., 2018 https://lnkd.in/eA5K2aHQ). Our Next Generation Copolymers – AASTYs, Ultrasolute™ Amphipols, and our newest invention, Ultrasolute™ Cubipol – address this challenge by stabilizing membrane proteins in their native environment in a single step. This enhances the functional stability of these proteins and makes them suitable for sensitive downstream applications like cryo-EM. Stay tuned for the upcoming launch, where we will unveil the full lineup of the new copolymers joining our Next Generation Copolymers. Get ready to explore how these innovative solutions can revolutionize your research and drug discovery efforts! #CryoEM #MembraneProteins #DrugDiscovery #BiotechInnovation #P2X4 #ScientificBreakthrough #CubeBiotech 

New Week, new potential drug target! This time, our project manager, Dr. Maryna Löwe, presented hERG (Kv11.1). Want to know how our NativeMP™ Technology Platform allows us to stabilize these hot targets so quickly? - Then book yourself a little chat with Maryna or one of our other project managers right here: https://lnkd.in/eMjH3cag #nativemp #drugtarget #cubebiotech #drugdiscovery #herg

𝗖𝗵𝗮𝗹𝗹𝗲𝗻𝗴𝗲 𝗨𝘀 𝘄𝗶𝘁𝗵 𝗬𝗼𝘂𝗿 𝗧𝗮𝗿𝗴𝗲𝘁! Just two weeks ago, we unveiled our highly anticipated Drug Discovery Pipeline, and today, we’re excited to present our first target: FAS, the tumor necrosis factor receptor superfamily member 6. 𝗙𝗔𝗦 forms the death-inducing signaling complex DISC upon ligand binding, can trigger apoptosis, and is associated with cancer. It plays a critical role in the immune system and, therefore, poses a promising target for preclinical studies and assay development. Do you need 10 mg of stabilized FAS protein? Are you interested in the high-resolution cryo-EM structure? Your goal is to generate a therapeutic antibody? Together, we can make it happen. Made in Europe and ready within 4 weeks, our human full-length targets accelerate your journey! Still unsure? Challenge Cube with your hardest target, the one you struggle with the most, and we’ll push your research together! Please contact us to learn more about our unique 𝗡𝗮𝘁𝗶𝘃𝗲𝗠𝗣 𝗧𝗲𝗰𝗵𝗻𝗼𝗹𝗼𝗴𝘆 𝗣𝗹𝗮𝘁𝗳𝗼𝗿𝗺 for any membrane protein class (https://lnkd.in/eAZu28WC) or directly book a meeting with one of our project managers: https://lnkd.in/eMjH3cag. #pioneeringtogether #drugdiscovery #targetpipeline #nativeMP

NOW LIVE: Join us to learn more about self-removing affinity tags for highly purified and tagless proteins with Prof. David Wood 🎬

🚀 New Study Highlights the Vital Role of Physiological Temperatures in Membrane Protein Research! 🌡️   Hu et al.'s recent publication in Nature (2024) shows the critical role of temperature in studying TRPM4 ion channels. The authors reveal distinct behaviors at physiological temperatures crucial for understanding their function. This underscores the broader importance of maintaining physiological conditions when investigating membrane proteins.  https://lnkd.in/e9p_3kSr   At Cube Biotech, our synthetic copolymer technology in nanodiscs enables the stabilization of membrane proteins at temperatures of up to 37 °C and over, ensuring accurate structural and functional studies.

☀️ June is here and has brought us some hot science from The Ohio State University David Wood, Professor at Ohio State and CSO of Protein Capture Science will present his self-removing affinity tag for highly purified & tagless proteins. Join us on June 20th to learn about his methods, how to troubleshoot, and what else is happening in his field of research. #pioneeringtogether #intelligentinfusions #ohiostate #cubebiotech

🔬 When it comes to purifying proteins, every detail matters! 𝐃𝐢𝐝 𝐲𝐨𝐮 𝐤𝐧𝐨𝐰 𝐭𝐡𝐚𝐭 𝐚𝐛𝐨𝐮𝐭 𝐲𝐨𝐮𝐫 𝐍𝐢-𝐍𝐓𝐀 𝐀𝐟𝐟𝐢𝐧𝐢𝐭𝐲 𝐂𝐡𝐫𝐨𝐦𝐚𝐭𝐨𝐠𝐫𝐚𝐩𝐡𝐲? His-tagged Proteins can bind to free nickel ions instead of binding to the nickel ions immobilized on the beads, leading to inefficiencies in your purification process. In addition, free nickel ions cause His-tagged proteins to aggregate. 💡 𝐒𝐚𝐯𝐞 𝐭𝐢𝐦𝐞, 𝐦𝐨𝐧𝐞𝐲, 𝐚𝐧𝐝 𝐡𝐮𝐦𝐚𝐧 𝐫𝐞𝐬𝐨𝐮𝐫𝐜𝐞𝐬 𝐰𝐢𝐭𝐡 𝐍𝐢-𝐈𝐍𝐃𝐈𝐆𝐎 𝐀𝐠𝐚𝐫𝐨𝐬𝐞 𝐛𝐞𝐚𝐝𝐬 𝐨𝐫 𝐌𝐚𝐠𝐁𝐞𝐚𝐝𝐬, the evolution of Ni-NTA resin. It has a much stronger bond to nickel than the ligand NTA; the free nickel is significantly reduced in the flowthrough. This is one of the reasons why Ni-INDIGO boasts higher protein yields, revolutionizing your research outcomes. Do you have questions or want to learn more about how Ni-INDIGO Agarose can elevate your project? Reach out to us! We're here to support your scientific journey every step of the way. #ProteinPurification #Biochemistry #ResearchAdvancements