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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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