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Optical Tweezers m-Trap

Introduction：
The m-Trap is the first entry-level optical tweezers instrument specifically developed for high-resolution single-molecule research. Ultra-high force resolution and stability, with incredible throughput, ease of use, and modularity – all at an unprecedented price level.   How does it work? In 2018 Arthur Ashkin won the Nobel Prize in Physics for his discovery that the momentum of light can be used as an incredibly sensitive set of “tweezers”. By shooting a laser through a microscope, he created a highly focused beam of light strong enough to trap and hold in place objects such as plastic beads. These beads can be coated to stick to a variety of biomolecules, such as proteins, cytoskeleton filaments, DNA, or RNA. Furthermore, the tiniest forces applied to these molecules can be measured as well, giving the world access to a tool not only capable of manipulating biomolecules but also capable of detecting what’s happening to them.   How can it be applied to my research? Whether you are aiming to make novel discoveries in the life sciences or develop successful drug candidates, we work on a personal level to find the right solution for you. Browse our extended list of applications to discover how these technologies can benefit your research. Don’t see your specific field represented? Drop us an e-mail to see what we can do!   -Stable and precise sample manipulation Advanced manipulation features that allow you to get the most out of your sample. Fully supported integration and correlation with custom optical layout allowing for 3rd party system integration.   -High throughput experiment workflow Loading your sample and analysing your data in less than 30 minutes.   -Easy and intuitive software package Check how you can completely automate your experiments using our user-centered software workflow.

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Optical Tweezers – Fluorescence & Label-free Microscopy C-Trap G2

Introduction：
The C-Trap® provides the world’s first dynamic single-molecule microscope to allow simultaneous manipulation and visualization of single-molecule interactions in real time. It combines high-resolution optical tweezers, fluorescence, and label-free microscopy, and an advanced microfluidics system in a truly integrated and correlated solution.   How does it work? In 2018 Arthur Ashkin won the Nobel Prize in Physics for his discovery that the momentum of light can be used as an incredibly sensitive set of “tweezers”. By shooting a laser through a microscope, he created a highly focused beam of light strong enough to trap and hold in place objects such as plastic beads. These beads can be coated to stick to a variety of biomolecules, such as proteins, cytoskeleton filaments, DNA, or RNA. Furthermore, the tiniest forces applied to these molecules can be measured as well, giving the world access to a tool not only capable of manipulating biomolecules but also capable of detecting what’s happening to them.   How can it be applied to my research? Whether you are aiming to make novel discoveries in the life sciences or develop successful drug candidates, we work on a personal level to find the right solution for you. Browse our extended list of applications to discover how these technologies can benefit your research.   -Stable and precise sample manipulation Different optical tweezers configurations and advanced manipulation features allow you to get the most out of your sample.   -A wide variety of visualization capabilities Choose and combine from a variety of imaging methods designed specifically to solve the needs of different experimental designs.   -Introducing the new C-Trap products Dymo & Edge With the desire to constantly produce breakthrough discoveries, you need an easy-to-use instrument, fully-optimized for your applications that should bring unprecedented insights with high precision, accuracy, and reliability, in short time. Discover your solutions below!   -High throughput experiment workflow Loading your sample and analysing your data in less than 30 minutes.   -Easy and intuitive software package Check how you can completely automate your experiments using our user-centered software workflow, experience seamless process from data collection to data analysis.

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Cell Avidity Analyzer z-Movi

Introduction：
Cell Avidity Analyzer   Measure cell-target binding strengths with the z-Movi Cell Avidity Analyzer to accelerate the development of immunotherapeutic strategies The z-Movi is a unique instrument that measures the avidity between immune cells and their targets, enabling you to identify the most potent immunotherapeutic effector cells. This new technology provides you with predictive, reproducible, and fast results at a single-cell resolution without compromising cell viability. All within a compact little box that easily fits inside the flow hood for sterile and safe sample handling.   How does it work? The z-Movi Cell Avidity Analyzer offers you a fast and simple solution for validating and optimizing immunotherapeutic strategies in a highly predictive and reproducible manner. By measuring cell avidity, the z-Movi provides you with quick and accurate results to characterize optimal immune cells for immunotherapy. While immuno-oncology has introduced valuable therapeutic options to clinical oncology, the efficacy of adoptive cell therapy is often challenged by hostile microenvironments, relapses, or off-target toxicities. As a result, some cancer patients undergoing immunotherapy either respond partially or not at all, and several patients experience severe adverse effects. This inconsistent response rate results from the inherently complex immune system and the context-dependent and dynamic nature of cancer cells. Clinical immunotherapeutic strategies like CAR T cell therapies, consequently, are difficult to predict, and the field lacks a proper understanding of what defines a good therapy. The z-Movi is an easy-to-use benchtop instrument that offers a crucial parameter to the field of immuno-oncology.   How can it be applied to my research? Binding events between a T cell and its target tumor cell determine the initiation of immunological synapse formation and T cell activation. Cell–cell interactions are, therefore, crucial to consider when trying to comprehend T cell response processes. Compared with affinity, cell avidity measurements enable you to compare several types of immunotherapeutic strategies, including CAR T cells, TCR T cells, bispecific antibody-engaged T cells, and NK cells.  Browse our extended list of applications to discover how this technology can benefit your research.   -Rapid experiment with the optimized workflow We have optimized the workflow of the z-Movi to facilitate the user experience and provide you with reliable and reproducible results in a matter of minutes. The z-Movi Chip is specialized to simplify cell culturing and maintain your samples in physiological conditions while you perform experiments. Once you have performed one run of analyses, you can simply flush in a new batch of effector cells. Running multiple chips sequentially allows you to measure several experimental conditions per day.   -Dive in and discover our software The only software that analyzes the avidity of hundreds of cells in parallel and real time In collaboration with end users, we have developed a fast and intuitive workflow that takes you from defining your parameters to viewing your data in no time. The powerful tracking algorithms for cell detection and measurements are performed in the background while the software generates your data live on your screen.  

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Nano Coulter Counter Nanocoulter G

Introduction：
After the invention of the microscope, combining it with a blood cell counting board became a classic method for cell counting. Experimenters usually spend several hours estimating cell numbers, and the results largely depend on the experimenters themselves, which is time-consuming and laborious, and inaccurate counting experiments are unbearable.   In 1953, the Kurt brothers first proposed the Kurt principle, which gave rise to the entire field of particle analysis due to its high accuracy, good repeatability, and fast speed. It has become the gold standard for blood cell counting, and 98% of blood analyzers use the Kurt principle. After more than half a century of development, Kurt's principle related equipment is now widely used in particle analysis in various industries and has been included in ASTM and ISO international standards.   Based on this, Resuntech (Shenzhen) Technology Co., Ltd. has developed a nano Kurt particle size analyzer, which is the world's first solid nanopore particle analysis platform. By bypassing the drawbacks of traditional optical detection methods (large particles block small particle scattering light; sample refractive index, absorbance, and viscosity affect test results), a new generation of electrical detection methods are adopted. The particle size detection lower limit of the traditional Kurt counter is lowered from the micrometer level to 50nm, and the particle size resolution can reach 1nm, achieving single particle detection of nanoparticles. Multiple dimensional data (particle size, concentration, zeta potential, morphology) are obtained in one test. High precision nanoparticle detection is required in scientific research, production quality control, process control, clinical diagnosis, pharmaceutical research and development, etc. The scene provides the most accurate data, taking you into the exciting and diverse nano world.

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Nano Coulter Counter Nanocoulter S

Introduction：
After the invention of the microscope, combining it with a blood cell counting board became a classic method for cell counting. Experimenters usually spend several hours estimating cell numbers, and the results largely depend on the experimenters themselves, which is time-consuming and laborious, and inaccurate counting experiments are unbearable.   In 1953, the Kurt brothers first proposed the Kurt principle, which gave rise to the entire field of particle analysis due to its high accuracy, good repeatability, and fast speed. It has become the gold standard for blood cell counting, and 98% of blood analyzers use the Kurt principle. After more than half a century of development, Kurt's principle related equipment is now widely used in particle analysis in various industries and has been included in ASTM and ISO international standards.   Based on this, Resuntech (Shenzhen) Technology Co., Ltd. has developed a nano Kurt particle size analyzer, which is the world's first solid nanopore particle analysis platform. By bypassing the drawbacks of traditional optical detection methods (large particles block small particle scattering light; sample refractive index, absorbance, and viscosity affect test results), a new generation of electrical detection methods are adopted. The particle size detection lower limit of the traditional Kurt counter is lowered from the micrometer level to 50nm, and the particle size resolution can reach 1nm, achieving single particle detection of nanoparticles. Multiple dimensional data (particle size, concentration, zeta potential, morphology) are obtained in one test. High precision nanoparticle detection is required in scientific research, production quality control, process control, clinical diagnosis, pharmaceutical research and development, etc. The scene provides the most accurate data, taking you into the exciting and diverse nano world.

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Spectral Shift & MST Technologies MO Automated

Introduction：
Spectral Shift & MST Technologies   Directly measure the strength of molecular interactions in solution, without the need for immobilization. Characterize nearly all types of molecular interactions — even the most challenging ones. With ultra-low sample consumption and versatile capabilities, Monolith is the best solution for your binding affinity experiments.   With Monolith X, you’ll get Spectral Shift and MST — two biophysical modalities to help cover all the types of interactions you encounter. You’ll enjoy high-quality results without spending your time on assay development and finally perform experiments without worrying about sample aggregation or impurities.   -Work with challenging interactions that are difficult for SPR For one reason or another, SPR has a difficult time analyzing challenging binding events no matter how many times you’ve tried to develop an assay. When you find yourself in these challenging situations, turn to Monolith to help.   -Immobilization prevents you from getting a Kd Suboptimal immobilization or regeneration conditions in SPR negatively impact ligand-binding activity. Because Monolith measures binding in-solution under controlled equilibrium conditions, it will help you handle more challenging ligands, like IDPs with complex conformational dynamics.   -You experience non-specific binding between the analyte and matrix Since SPR doesn’t differentiate between binding of an analyte to an immobilized ligand or to the matrix on a sensor, you’ll find yourself doing further testing to recognize and avoid non-specific binding. With Monolith, there’s no need to test for non-specific binding since measurements are done in solution.   -You’re unable to easily resolve high affinity interactions It’s so difficult to assess high affinity interactions using SPR. Why? Because these types of interactions have very slow dissociation rates and since SPR uses this information to derive binding data — getting a result could take forever. With Monolith, binding is measured directly, so you don’t have to wait.   -You’re dealing with covalent interactions Studying covalent binders with SPR is very complex. Because Monolith measures interactions in solution, it’s easy to measure covalent interactions — there’s no need to figure out how to regenerate biosensors.   -Validate your SPR results with an immobilization-free method It’s common practice to validate your results with more than one technique because you want to be confident that the results are real. Monolith, with its immobilization-free measurement, is the perfect orthogonal tool for SPR users. It removes the immobilization bias and helps to confirm your results, identify false positives, or find binding partners that your primary assay missed.   -Use a versatile tool to tackle a wide variety of projects Rely on Monolith’s versatile capabilities to execute immobilization-free experiments quickly and efficiently. Tackle projects that involve almost any molecule, buffer composition, or binding strength, all while consuming only a small amount of sample.   -Get binding affinity data for almost any type of molecule Work with almost any molecule including IDPs, membrane proteins, large protein complexes, PROTACS, small molecules or ions.   -Capture mass and size⁠-⁠independent measurements Evaluate results independently of size and mass differences in binding partners.   -Utilize a myriad of assay buffer formulations Analyze the binding of purified and crude samples without worrying about interference from buffer additives like detergents.   -Quantify low and high binding affinities Measure a broad range of binding affinities, from pM to mM, allowing you to detect strong and weak binders.   -Get more than just a Kd Scientists use Monolith to study binding stoichiometry* and thermodynamic parameters*, assess relative affinities with competition assays, and characterize binding cooperativity*. *Requires offline data handling, not supported by Monolith software  

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Spectral Shift & MST Technologies MO LabelFree

Introduction：
Directly measure the strength of molecular interactions in solution, without the need for immobilization. Characterize nearly all types of molecular interactions — even the most challenging ones. With ultra-low sample consumption and versatile capabilities, Monolith is the best solution for your binding affinity experiments.   With Monolith X, you’ll get Spectral Shift and MST — two biophysical modalities to help cover all the types of interactions you encounter. You’ll enjoy high-quality results without spending your time on assay development and finally perform experiments without worrying about sample aggregation or impurities.   -Work with challenging interactions that are difficult for SPR For one reason or another, SPR has a difficult time analyzing challenging binding events no matter how many times you’ve tried to develop an assay. When you find yourself in these challenging situations, turn to Monolith to help.   -Immobilization prevents you from getting a Kd Suboptimal immobilization or regeneration conditions in SPR negatively impact ligand-binding activity. Because Monolith measures binding in-solution under controlled equilibrium conditions, it will help you handle more challenging ligands, like IDPs with complex conformational dynamics.   -You experience non-specific binding between the analyte and matrix Since SPR doesn’t differentiate between binding of an analyte to an immobilized ligand or to the matrix on a sensor, you’ll find yourself doing further testing to recognize and avoid non-specific binding. With Monolith, there’s no need to test for non-specific binding since measurements are done in solution.   -You’re unable to easily resolve high affinity interactions It’s so difficult to assess high affinity interactions using SPR. Why? Because these types of interactions have very slow dissociation rates and since SPR uses this information to derive binding data — getting a result could take forever. With Monolith, binding is measured directly, so you don’t have to wait.   -You’re dealing with covalent interactions Studying covalent binders with SPR is very complex. Because Monolith measures interactions in solution, it’s easy to measure covalent interactions — there’s no need to figure out how to regenerate biosensors.   -Validate your SPR results with an immobilization-free method It’s common practice to validate your results with more than one technique because you want to be confident that the results are real. Monolith, with its immobilization-free measurement, is the perfect orthogonal tool for SPR users. It removes the immobilization bias and helps to confirm your results, identify false positives, or find binding partners that your primary assay missed.   -Use a versatile tool to tackle a wide variety of projects Rely on Monolith’s versatile capabilities to execute immobilization-free experiments quickly and efficiently. Tackle projects that involve almost any molecule, buffer composition, or binding strength, all while consuming only a small amount of sample.   -Get binding affinity data for almost any type of molecule Work with almost any molecule including IDPs, membrane proteins, large protein complexes, PROTACS, small molecules or ions.   -Capture mass and size⁠-⁠independent measurements Evaluate results independently of size and mass differences in binding partners.   -Utilize a myriad of assay buffer formulations Analyze the binding of purified and crude samples without worrying about interference from buffer additives like detergents.   -Quantify low and high binding affinities Measure a broad range of binding affinities, from pM to mM, allowing you to detect strong and weak binders.   -Get more than just a Kd Scientists use Monolith to study binding stoichiometry* and thermodynamic parameters*, assess relative affinities with competition assays, and characterize binding cooperativity*. *Requires offline data handling, not supported by Monolith software

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Spectral Shift & MST Technologies MO Pico

Introduction：
Directly measure the strength of molecular interactions in solution, without the need for immobilization. Characterize nearly all types of molecular interactions — even the most challenging ones. With ultra-low sample consumption and versatile capabilities, Monolith is the best solution for your binding affinity experiments.   With Monolith X, you’ll get Spectral Shift and MST — two biophysical modalities to help cover all the types of interactions you encounter. You’ll enjoy high-quality results without spending your time on assay development and finally perform experiments without worrying about sample aggregation or impurities.   -Work with challenging interactions that are difficult for SPR For one reason or another, SPR has a difficult time analyzing challenging binding events no matter how many times you’ve tried to develop an assay. When you find yourself in these challenging situations, turn to Monolith to help.   -Immobilization prevents you from getting a Kd Suboptimal immobilization or regeneration conditions in SPR negatively impact ligand-binding activity. Because Monolith measures binding in-solution under controlled equilibrium conditions, it will help you handle more challenging ligands, like IDPs with complex conformational dynamics.   -You experience non-specific binding between the analyte and matrix Since SPR doesn’t differentiate between binding of an analyte to an immobilized ligand or to the matrix on a sensor, you’ll find yourself doing further testing to recognize and avoid non-specific binding. With Monolith, there’s no need to test for non-specific binding since measurements are done in solution.   -You’re unable to easily resolve high affinity interactions It’s so difficult to assess high affinity interactions using SPR. Why? Because these types of interactions have very slow dissociation rates and since SPR uses this information to derive binding data — getting a result could take forever. With Monolith, binding is measured directly, so you don’t have to wait.   -You’re dealing with covalent interactions Studying covalent binders with SPR is very complex. Because Monolith measures interactions in solution, it’s easy to measure covalent interactions — there’s no need to figure out how to regenerate biosensors.   -Validate your SPR results with an immobilization-free method It’s common practice to validate your results with more than one technique because you want to be confident that the results are real. Monolith, with its immobilization-free measurement, is the perfect orthogonal tool for SPR users. It removes the immobilization bias and helps to confirm your results, identify false positives, or find binding partners that your primary assay missed.   -Use a versatile tool to tackle a wide variety of projects Rely on Monolith’s versatile capabilities to execute immobilization-free experiments quickly and efficiently. Tackle projects that involve almost any molecule, buffer composition, or binding strength, all while consuming only a small amount of sample.   -Get binding affinity data for almost any type of molecule Work with almost any molecule including IDPs, membrane proteins, large protein complexes, PROTACS, small molecules or ions.   -Capture mass and size⁠-⁠independent measurements Evaluate results independently of size and mass differences in binding partners.   -Utilize a myriad of assay buffer formulations Analyze the binding of purified and crude samples without worrying about interference from buffer additives like detergents.   -Quantify low and high binding affinities Measure a broad range of binding affinities, from pM to mM, allowing you to detect strong and weak binders.   -Get more than just a Kd Scientists use Monolith to study binding stoichiometry* and thermodynamic parameters*, assess relative affinities with competition assays, and characterize binding cooperativity*. *Requires offline data handling, not supported by Monolith software

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Spectral Shift & MST Technologies MO

Introduction：
Directly measure the strength of molecular interactions in solution, without the need for immobilization. Characterize nearly all types of molecular interactions — even the most challenging ones. With ultra-low sample consumption and versatile capabilities, Monolith is the best solution for your binding affinity experiments.   With Monolith X, you’ll get Spectral Shift and MST — two biophysical modalities to help cover all the types of interactions you encounter. You’ll enjoy high-quality results without spending your time on assay development and finally perform experiments without worrying about sample aggregation or impurities.   -Work with challenging interactions that are difficult for SPR For one reason or another, SPR has a difficult time analyzing challenging binding events no matter how many times you’ve tried to develop an assay. When you find yourself in these challenging situations, turn to Monolith to help.   -Immobilization prevents you from getting a Kd Suboptimal immobilization or regeneration conditions in SPR negatively impact ligand-binding activity. Because Monolith measures binding in-solution under controlled equilibrium conditions, it will help you handle more challenging ligands, like IDPs with complex conformational dynamics.   -You experience non-specific binding between the analyte and matrix Since SPR doesn’t differentiate between binding of an analyte to an immobilized ligand or to the matrix on a sensor, you’ll find yourself doing further testing to recognize and avoid non-specific binding. With Monolith, there’s no need to test for non-specific binding since measurements are done in solution.   -You’re unable to easily resolve high affinity interactions It’s so difficult to assess high affinity interactions using SPR. Why? Because these types of interactions have very slow dissociation rates and since SPR uses this information to derive binding data — getting a result could take forever. With Monolith, binding is measured directly, so you don’t have to wait.   -You’re dealing with covalent interactions Studying covalent binders with SPR is very complex. Because Monolith measures interactions in solution, it’s easy to measure covalent interactions — there’s no need to figure out how to regenerate biosensors.   -Validate your SPR results with an immobilization-free method It’s common practice to validate your results with more than one technique because you want to be confident that the results are real. Monolith, with its immobilization-free measurement, is the perfect orthogonal tool for SPR users. It removes the immobilization bias and helps to confirm your results, identify false positives, or find binding partners that your primary assay missed.   -Use a versatile tool to tackle a wide variety of projects Rely on Monolith’s versatile capabilities to execute immobilization-free experiments quickly and efficiently. Tackle projects that involve almost any molecule, buffer composition, or binding strength, all while consuming only a small amount of sample.   -Get binding affinity data for almost any type of molecule Work with almost any molecule including IDPs, membrane proteins, large protein complexes, PROTACS, small molecules or ions.   -Capture mass and size⁠-⁠independent measurements Evaluate results independently of size and mass differences in binding partners.   -Utilize a myriad of assay buffer formulations Analyze the binding of purified and crude samples without worrying about interference from buffer additives like detergents.   -Quantify low and high binding affinities Measure a broad range of binding affinities, from pM to mM, allowing you to detect strong and weak binders.   -Get more than just a Kd Scientists use Monolith to study binding stoichiometry* and thermodynamic parameters*, assess relative affinities with competition assays, and characterize binding cooperativity*. *Requires offline data handling, not supported by Monolith software

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Protein Stability Analyzer NT.Plex + NT.RA

Introduction：
Prometheus consistently delivers trustworthy, high-resolution stability characterization   Collect precise, high-resolution data and reliable results every time Measuring with precision matters when the differences between your candidates are subtle. Prometheus delivers the high-resolution stability data you need to spot those differences and decide which candidates are best to work with moving forward.   Learn more about your protein samples without wasting sample With multiple technologies collecting conformational and colloidal stability data from a single sample, you gain a deeper understanding of your molecule’s behavior when assessing your protein. Prometheus offers a combinatorial approach to selecting ideal drug candidates and conditions.   Future-proof your lab and be prepared for any throughput or experiment type Prometheus works for large experiments with a single purpose, such as buffer screening; or for complex, multi-step processes like developability profiling. And when big projects come your way, get all your conformational and colloidal stability info in a hands-free, automated manner.   Get started right away with hassle-free software It doesn’t take an expert to learn everything you need to know about your protein samples. Prometheus makes it easy to get started, both with operation and data analysis. Spend less time struggling to interpret your data and more time making decisions about your proteins.

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Protein Stability Analyzer NT.Plex

Introduction：
Prometheus consistently delivers trustworthy, high-resolution stability characterization   Collect precise, high-resolution data and reliable results every time Measuring with precision matters when the differences between your candidates are subtle. Prometheus delivers the high-resolution stability data you need to spot those differences and decide which candidates are best to work with moving forward.   Learn more about your protein samples without wasting sample With multiple technologies collecting conformational and colloidal stability data from a single sample, you gain a deeper understanding of your molecule’s behavior when assessing your protein. Prometheus offers a combinatorial approach to selecting ideal drug candidates and conditions.   Future-proof your lab and be prepared for any throughput or experiment type Prometheus works for large experiments with a single purpose, such as buffer screening; or for complex, multi-step processes like developability profiling. And when big projects come your way, get all your conformational and colloidal stability info in a hands-free, automated manner.   Get started right away with hassle-free software It doesn’t take an expert to learn everything you need to know about your protein samples. Prometheus makes it easy to get started, both with operation and data analysis. Spend less time struggling to interpret your data and more time making decisions about your proteins.

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Protein Stability Analyzer NT.48

Introduction：
Prometheus consistently delivers trustworthy, high-resolution stability characterization   Collect precise, high-resolution data and reliable results every time Measuring with precision matters when the differences between your candidates are subtle. Prometheus delivers the high-resolution stability data you need to spot those differences and decide which candidates are best to work with moving forward.   Learn more about your protein samples without wasting sample With multiple technologies collecting conformational and colloidal stability data from a single sample, you gain a deeper understanding of your molecule’s behavior when assessing your protein. Prometheus offers a combinatorial approach to selecting ideal drug candidates and conditions.   Future-proof your lab and be prepared for any throughput or experiment type Prometheus works for large experiments with a single purpose, such as buffer screening; or for complex, multi-step processes like developability profiling. And when big projects come your way, get all your conformational and colloidal stability info in a hands-free, automated manner.   Get started right away with hassle-free software It doesn’t take an expert to learn everything you need to know about your protein samples. Prometheus makes it easy to get started, both with operation and data analysis. Spend less time struggling to interpret your data and more time making decisions about your proteins.

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