Chromatographic modes for peptide separation include reversed-phase, ion-exchange, hydrophilic-interaction, and size-exclusion chromatography and are used for applications ranging from the analysis and purification of synthetic peptides, to the characterization of complex proteolytic digests, and bioanalysis. These methods rely on taking advantage of chemical and physical differences between peptides species.
Reversed-phase chromatography using ion-pairing reagent such as TFA and formic acid can deliver highly resolved separations of complex peptide mixtures whose sequences may differ by a single amino acid. In general, the hydrophobicity of the peptide determines the elution order, with the least hydrophobic peptides eluting first.
Reversed-phase chromatography using ion-pairing reagent such as TFA and formic acid can deliver highly resolved separations of complex peptide mixtures whose sequences may differ by a single amino acid. In general, the hydrophobicity of the peptide determines the elution order, with the least hydrophobic peptides eluting first
These peptide columns range from 75 µm to 1 mm I.D. These columns are well suited for high-sensitivity, sample-limited applications, and 2-dimensional chromatographic separations.
Ion-exchange chromatography separates peptides based on charge and is consequently used when a different / orthogonal separation mechanism to reversed-phase LC is desired.
Ion-exchange chromatography separates peptides based on charge and is consequently used when a different / orthogonal separation mechanism to reversed-phase LC is desired.
Hydrophillic Interaction Chromatography (HILIC) is a useful alternative peptide separation technique to ion-exchange and reversed-phase LC. This separation mode using Bridged Hybrid Technology (BEH) amide bonded stationary phases separates compounds based on their hydrophilicity. HILIC is ideally suited when attempting to separate glycosylated from non-glycosylated peptide containing mixtures.
Hydrophillic Interaction Chromatography (HILIC) is a useful alternative peptide separation technique to ion-exchange and reversed-phase LC. This separation mode using Bridged Hybrid Technology (BEH) amide bonded stationary phases separates compounds based on their hydrophilicity. HILIC is ideally suited when attempting to separate glycosylated from non-glycosylated peptide containing mixtures.
Size exclusion chromatography, also known as gel filtration, separates molecules based on their hydrodynamic radii. In general, a two-fold difference in the molecular weight of two different peptides is required to obtain baseline resolution of each species.
Size exclusion chromatography, also known as gel filtration, separates molecules based on their hydrodynamic radii. In general, a two-fold difference in the molecular weight of two different peptides is required to obtain baseline resolution of each species.
Waters line of peptide products offers options that help ease sample preparation burdens. Products include protein digestion standards, complex peptide matrices and synthetic peptide standards for column benchmarking and system validation.
Waters line of peptide products offer specialized application relevant qualitative and quantitative standards that ease sample preparation burdens. Products include complex digestion standards, unique peptide mixes and synthetic peptide standards.
The analysis of complex N and 0-linked glycans composed of frequently similar and repeating sugar moieties requires a highly discriminating chromatographic method. Hydrophilic-interaction liquid chromatography (HILIC) using a particle modified with an amide ligand can effectively separate a wide range of released unmodified or fluorescently labeled glycans.
Hydrophilic liquid interaction chromatography (HILIC), using Ethylene Bridged Hybrid Technology (BEH) amide bonded stationary phases, separates compounds based on their hydrophilicity This makes HILIC ideally suited for the LC and LCMS analysis of released glycans, and glycopeptides.
Hydrophilic liquid interaction chromatography (HILIC), using Ethylene Bridged Hybrid Technology (BEH) amide bonded stationary phases, separates compounds based on their hydrophilicity This makes HILIC ideally suited for the LC and LCMS analysis of released glycans, and glycopeptides.
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Chromatographic modes for the analysis and purification of proteins include reversed-phase, affinity, ion-exchange, hydrophobic interaction, and size-exclusion chromatography. These methods rely on taking advantage of chemical and physical differences between protein species.
Reversed-phase chromatography of proteins, done with columns consisting of wide-pore size particles ( e.g, 300Å) functionalized with short-ligand length chemistries, is a separation technique based on the relative hydrophobic characteristics of the proteins in solution. Gradients of increasing of organic solvent concentration are frequently used to affect separations in the presence of ion-pairing reagents that minimize undesired ionic interactions.
Reversed-phase chromatography of proteins, done with columns consisting of wide-pore size particles ( e.g, 300Å) functionalized with short-ligand length chemistries, is a separation technique based on the relative hydrophobic characteristics of the proteins in solution. Gradients of increasing of organic solvent concentration are frequently used to affect separations in the presence of ion-pairing reagents that minimize undesired ionic interactions.
Hydrophobic Interaction Chromatography (HIC) is characterized by the adsorption of compounds to a weakly hydrophobic surface at high salt concentrations, followed by elution with a decreasing salt gradient. This technique is well suited for protein separations due its non-denaturing characteristic.
Hydrophobic Interaction Chromatography (HIC) is characterized by the adsorption of compounds to a weakly hydrophobic surface at high salt concentrations, followed by elution with a decreasing salt gradient. This technique is well suited for protein separations due its non-denaturing characteristic.
Ion-exchange chromatography is a powerful technique with its ability to resolve different protein species, based on their surface charge. Separations are based on the use of either salt, pH, or salt/pH gradients.
Ion-exchange chromatography is a powerful technique with its ability to resolve different protein species, based on their surface charge. Separations are based on the use of either salt, pH, or salt/pH gradients.
Size exclusion, also known as gel filtration, chromatography separates biomolecules based on their sizes (hydrodynamic radii) in solution. This technique is frequently used to monitor aggregation of biotherapeutic proteins.
Size exclusion, also known as gel filtration, chromatography separates biomolecules based on their sizes (hydrodynamic radii) in solution. This technique is frequently used to monitor aggregation of biotherapeutic proteins.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
Chromatographic modes for oligonucleotide separations include reversed phase and ion exchange. The applications include the analysis and purifications of synthetic oligonucleotides used in research, diagnostic reagents or biotherapeutic compounds.
The gradient separation of synthetic oligonucleotides by ion-pair reversed-phase LC is based on sequence length with shorter failure sequence eluting prior to desired product.
The gradient separation of synthetic oligonucleotides by ion-pair reversed-phase LC is based on sequence length with shorter failure sequence eluting prior to desired product.
HPLC-based ion-exchange chromatography, using a gradient of increasing salt concentration, can be effectively used to separate PCR products as well as plasmid forms based on differing charge density characteristics.
HPLC-based ion-exchange chromatography, using a gradient of increasing salt concentration, can be effectively used to separate PCR products as well as plasmid forms based on differing charge density characteristics.
Specially formulated, synthetic oligonucleotide standard designed for verification of HPLC/UPLC instrument and column performance for analysis of oligonucleotide applications.
The Oligonucleotide Standard line provides standards designed for verification of HPLC/UPLC instruments and performance of columns used for analysis of synthetic oligos. These specially formulated standards are unique to our column chemistry.
Amino acid analyses include the separation and quantitations of either free amino acids or amino acids derived from protein hydrolysates. Matrix effects and accurate quantitations are some of the challenges that are adressed by pre-column derivatization and high resolution chromatographic separations.
The gradient separation of precolumn derivitizated amino acids by ion-pair, reversed-phase LC is based on the different hydrophobic characteristics of each labeled constituent.
The gradient separation of precolumn derivitizated amino acids by ion-pair, reversed-phase LC is based on the different hydrophobic characteristics of each labeled constituent.
Waters amino acid kits and reagents are designed for accurate and reproducible quantitation of amino acids from various sample matrices using either UPLC or HPLC methods.
Waters amino acid kits and reagents are designed for accurate and reproducible quantitation of amino acids from various sample matrices using either UPLC or HPLC methods.
The Bioseparations Columns Advisor, organized by biomolecule type, helps users select an appropriate UPLC/UHPLC or HPLC for a desired application. You can search by either Biomolecule / Separation Mode or by Column / Biomolecule with relevant offerings being highlighted.
Start by moving your mouse to the desired biocompound class in the left margin and click on the selectable tabs. The middle screen will then reveal useful information to help you toward the select of a recommended chemistry to address your need.
Remarkable, pH stable column chemistries with the benefits of sub-2-µm particles for ultimate peak capacities and component resolution.
Remarkable, pH stable column chemistries with the benefits of sub-2-µm particles for ultimate peak capacities and component resolution.
ACQUITY UPLC C18 oligonucleotide Columns deliver high resolution of oligonucleotide mixtures using high pH ion-paired reversed phase separations. The enhanced resolving power and pH stability of these sub-2 μm particles make these columns a viable option to electrophoresis based methods.
Based on AccQ-Tag HPLC AA derivatization method, AccQ-Tag Ultra offering is part of a complete solution that provide higher throughput.
Sub-2 micron UPLC Peptide columns are specifically designed for UPLC/UHPLC Systems to deliver high efficiency separation delivering superior component resolution and increased throughput compared to traditional HPLC.
These SEC columns are QC tested with relevant protein standards and deliver high-througput size-based separations of proteins without compromising chromatographic resolution. Use of Ethylene Bridged Hybrid Technology (BEH) particles provides superior basic pH stability compared to traditional silica based columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
These SEC columns are QC tested with relevant protein standards and deliver high-througput size-based separations of proteins without compromising chromatographic resolution. Use of Ethylene Bridged Hybrid Technology (BEH) particles provides superior basic pH stability compared to traditional silica based columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
Protein-Pak Hi Res IEX Columns are well suited for use with UPLC/UHPLC Systems. The non-porous, high binding capacity of these columns yields outstanding resolution of charged species in less time compared to traditional porous IEX columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
These UPLC columns are specifically QC tested for the HILIC separation of released glycans. They may also be used for the analyses of glycopeptides based on their N-linked and O-linked glycosylation.
10,000 PSI rated trapping and nano flow columns containing a variety of chemistries for use on Waters nanoACQUITY UPLC Systems for the analysis of sample limited and two-dimensional separations of peptides.
15,000 PSI rated trapping and nano flow columns containing a variety of Waters Chemistries. Specifically engineered to take advantage of the capabilities of the ACQUITY UPLC M-Class System to provide the highest peak capacities for the analysis of sample limited and two-dimensional separations of peptides.
Wide range of HPLC column particle sizes and dimensions for consistent separations of biomolecules.
Wide range of HPLC column particle sizes and dimensions for consistent separations of biomolecules.
XBridge Oligonucleotides Columns containing 2.5 µm particles are the preferred HPLC offering for detritylated oligonucleotide purifications. Increasing column length (plate number) will support higher sample loads or provide improved resolution.
Waters AccQ-Tag HPLC-based method uses, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate that derivatizes primary and secondary amines in a simple, single-step reaction to yield highly stable, fluorescent derivatives.
Xselect columns are charged surface hybrid (CSH) C18 reversed-phase columns for the separation of proteins and peptides. The CSH modification of these particles enables the use of more MS friendly mobile phases (e.g. formic acid) and provide different selectivities versus non CSH particles.
These 300Å pore size Protein columns are available in 3.5 µm, 5 µm, and 10 µm Ethylene Bridged Hybrid Technology (BEH) particles containing C4 ligands. They are used for the isolation and lab-scale purification of proteins and deliver high efficiency separations while minimizing sample carryover. These columns are QC tested with a protein mixture.
The methacrylic ester-based polymeric particle used in the BioSuite family of ion-exchange columns, contains either anionic (Q, DEAE) or cationic (CM, SP) ligands that can be used for the HPLC analysis and lab-scale purification of various peptides or proteins based on charge.
Protein-Pak Hi Res HIC (Hydrophobic Interaction Chromatography) columns contain non-porous, polymethacrylate-based particles (2.5 μm) functionalized with a butyl ligand for the characterization of proteins and biotherapeutics including monoclonal antibodies and antibody drug conjugates.
HPLC SEC columns are based on the same Waters ethylene bridged hybrid (BEH)-based particle technology with stable diol-bonding to deliver superior performance compared to traditional, 100% silica-based SEC offerings.
These HPLC columns containing either 2.5 or 3.5 µm particles, were developed and are QC tested for the HILIC separation of released glycans. They may also be used for the analyses of glycopeptides based on their N-linked and O-linked glycosylation.
High-quality standards, reagents and sample preparation products, specifically designed for critical life science applications, that help getting to successful results while adding an additional layer of assurance to your analyses
High-quality standards, reagents and sample preparation products, specifically designed for critical life science applications, that help getting to successful results while adding an additional layer of assurance to your analyses
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Waters Amino acid kits and reagents are designed for accurate quantitation of amino acids from protein/peptide hydrolysates, physiologic fluids, feeds, foods, pharmaceutical preparations, and other samples using a UPLC- or HPLC-based technology.
The Oligonucleotide Standard line provides standards designed for verification of HPLC/UPLC instruments and performance of columns used for analysis of synthetic oligos. These specially formulated standards are unique to our column chemistry.
Waters line of peptide products offer specialized application relevant qualitative and quantitative standards that ease sample preparation burdens. Products include complex digestion standards, unique peptide mixes and synthetic peptide standards.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
Remarkable, pH stable column chemistries with the benefits of sub-2-µm particles for ultimate peak capacities and component resolution.
Remarkable, pH stable column chemistries with the benefits of sub-2-µm particles for ultimate peak capacities and component resolution.
ACQUITY UPLC C18 oligonucleotide Columns deliver high resolution of oligonucleotide mixtures using high pH ion-paired reversed phase separations. The enhanced resolving power and pH stability of these sub-2 μm particles make these columns a viable option to electrophoresis based methods.
Based on AccQ-Tag HPLC AA derivatization method, AccQ-Tag Ultra offering is part of a complete solution that provide higher throughput.
Sub-2 micron UPLC Peptide columns are specifically designed for UPLC/UHPLC Systems to deliver high efficiency separation delivering superior component resolution and increased throughput compared to traditional HPLC.
These SEC columns are QC tested with relevant protein standards and deliver high-througput size-based separations of proteins without compromising chromatographic resolution. Use of Ethylene Bridged Hybrid Technology (BEH) particles provides superior basic pH stability compared to traditional silica based columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
These SEC columns are QC tested with relevant protein standards and deliver high-througput size-based separations of proteins without compromising chromatographic resolution. Use of Ethylene Bridged Hybrid Technology (BEH) particles provides superior basic pH stability compared to traditional silica based columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
Protein-Pak Hi Res IEX Columns are well suited for use with UPLC/UHPLC Systems. The non-porous, high binding capacity of these columns yields outstanding resolution of charged species in less time compared to traditional porous IEX columns. These columns are available in 125Å, 200Å, and 450Å pore sizes and are capable of resolving proteins ranging in size from 1,000 to 2,000,000 MW.
These UPLC columns are specifically QC tested for the HILIC separation of released glycans. They may also be used for the analyses of glycopeptides based on their N-linked and O-linked glycosylation.
10,000 PSI rated trapping and nano flow columns containing a variety of chemistries for use on Waters nanoACQUITY UPLC Systems for the analysis of sample limited and two-dimensional separations of peptides.
15,000 PSI rated trapping and nano flow columns containing a variety of Waters Chemistries. Specifically engineered to take advantage of the capabilities of the ACQUITY UPLC M-Class System to provide the highest peak capacities for the analysis of sample limited and two-dimensional separations of peptides.
Wide range of HPLC column particle sizes and dimensions for consistent separations of biomolecules.
Wide range of HPLC column particle sizes and dimensions for consistent separations of biomolecules.
XBridge Oligonucleotides Columns containing 2.5 µm particles are the preferred HPLC offering for detritylated oligonucleotide purifications. Increasing column length (plate number) will support higher sample loads or provide improved resolution.
Waters AccQ-Tag HPLC-based method uses, 6-aminoquinolyl-N-hydroxysuccinimidyl carbamate that derivatizes primary and secondary amines in a simple, single-step reaction to yield highly stable, fluorescent derivatives.
Xselect columns are charged surface hybrid (CSH) C18 reversed-phase columns for the separation of proteins and peptides. The CSH modification of these particles enables the use of more MS friendly mobile phases (e.g. formic acid) and provide different selectivities versus non CSH particles.
These 300Å pore size Protein columns are available in 3.5 µm, 5 µm, and 10 µm Ethylene Bridged Hybrid Technology (BEH) particles containing C4 ligands. They are used for the isolation and lab-scale purification of proteins and deliver high efficiency separations while minimizing sample carryover. These columns are QC tested with a protein mixture.
The methacrylic ester-based polymeric particle used in the BioSuite family of ion-exchange columns, contains either anionic (Q, DEAE) or cationic (CM, SP) ligands that can be used for the HPLC analysis and lab-scale purification of various peptides or proteins based on charge.
Protein-Pak Hi Res HIC (Hydrophobic Interaction Chromatography) columns contain non-porous, polymethacrylate-based particles (2.5 μm) functionalized with a butyl ligand for the characterization of proteins and biotherapeutics including monoclonal antibodies and antibody drug conjugates.
HPLC SEC columns are based on the same Waters ethylene bridged hybrid (BEH)-based particle technology with stable diol-bonding to deliver superior performance compared to traditional, 100% silica-based SEC offerings.
These HPLC columns containing either 2.5 or 3.5 µm particles, were developed and are QC tested for the HILIC separation of released glycans. They may also be used for the analyses of glycopeptides based on their N-linked and O-linked glycosylation.
High-quality standards, reagents and sample preparation products, specifically designed for critical life science applications, that help getting to successful results while adding an additional layer of assurance to your analyses
High-quality standards, reagents and sample preparation products, specifically designed for critical life science applications, that help getting to successful results while adding an additional layer of assurance to your analyses
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Waters Amino acid kits and reagents are designed for accurate quantitation of amino acids from protein/peptide hydrolysates, physiologic fluids, feeds, foods, pharmaceutical preparations, and other samples using a UPLC- or HPLC-based technology.
The Oligonucleotide Standard line provides standards designed for verification of HPLC/UPLC instruments and performance of columns used for analysis of synthetic oligos. These specially formulated standards are unique to our column chemistry.
Waters line of peptide products offer specialized application relevant qualitative and quantitative standards that ease sample preparation burdens. Products include complex digestion standards, unique peptide mixes and synthetic peptide standards.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
The Bioseparations Columns Advisor, organized by biomolecule type, helps users select an appropriate UPLC/UHPLC or HPLC for a desired application. You can search by either Biomolecule / Separation Mode or by Column / Biomolecule with relevant offerings being highlighted.
Start by moving your mouse to the desired biocompound class in the left margin and click on the selectable tabs. The middle screen will then reveal useful information to help you toward the select of a recommended chemistry to address your need.
Chromatographic modes for peptide separation include reversed-phase, ion-exchange, hydrophilic-interaction, and size-exclusion chromatography and are used for applications ranging from the analysis and purification of synthetic peptides, to the characterization of complex proteolytic digests, and bioanalysis. These methods rely on taking advantage of chemical and physical differences between peptides species.
Reversed-phase chromatography using ion-pairing reagent such as TFA and formic acid can deliver highly resolved separations of complex peptide mixtures whose sequences may differ by a single amino acid. In general, the hydrophobicity of the peptide determines the elution order, with the least hydrophobic peptides eluting first.
Reversed-phase chromatography using ion-pairing reagent such as TFA and formic acid can deliver highly resolved separations of complex peptide mixtures whose sequences may differ by a single amino acid. In general, the hydrophobicity of the peptide determines the elution order, with the least hydrophobic peptides eluting first
These peptide columns range from 75 µm to 1 mm I.D. These columns are well suited for high-sensitivity, sample-limited applications, and 2-dimensional chromatographic separations.
Ion-exchange chromatography separates peptides based on charge and is consequently used when a different / orthogonal separation mechanism to reversed-phase LC is desired.
Ion-exchange chromatography separates peptides based on charge and is consequently used when a different / orthogonal separation mechanism to reversed-phase LC is desired.
Hydrophillic Interaction Chromatography (HILIC) is a useful alternative peptide separation technique to ion-exchange and reversed-phase LC. This separation mode using Bridged Hybrid Technology (BEH) amide bonded stationary phases separates compounds based on their hydrophilicity. HILIC is ideally suited when attempting to separate glycosylated from non-glycosylated peptide containing mixtures.
Hydrophillic Interaction Chromatography (HILIC) is a useful alternative peptide separation technique to ion-exchange and reversed-phase LC. This separation mode using Bridged Hybrid Technology (BEH) amide bonded stationary phases separates compounds based on their hydrophilicity. HILIC is ideally suited when attempting to separate glycosylated from non-glycosylated peptide containing mixtures.
Size exclusion chromatography, also known as gel filtration, separates molecules based on their hydrodynamic radii. In general, a two-fold difference in the molecular weight of two different peptides is required to obtain baseline resolution of each species.
Size exclusion chromatography, also known as gel filtration, separates molecules based on their hydrodynamic radii. In general, a two-fold difference in the molecular weight of two different peptides is required to obtain baseline resolution of each species.
Waters line of peptide products offers options that help ease sample preparation burdens. Products include protein digestion standards, complex peptide matrices and synthetic peptide standards for column benchmarking and system validation.
Waters line of peptide products offer specialized application relevant qualitative and quantitative standards that ease sample preparation burdens. Products include complex digestion standards, unique peptide mixes and synthetic peptide standards.
The analysis of complex N and 0-linked glycans composed of frequently similar and repeating sugar moieties requires a highly discriminating chromatographic method. Hydrophilic-interaction liquid chromatography (HILIC) using a particle modified with an amide ligand can effectively separate a wide range of released unmodified or fluorescently labeled glycans.
Hydrophilic liquid interaction chromatography (HILIC), using Ethylene Bridged Hybrid Technology (BEH) amide bonded stationary phases, separates compounds based on their hydrophilicity This makes HILIC ideally suited for the LC and LCMS analysis of released glycans, and glycopeptides.
Hydrophilic liquid interaction chromatography (HILIC), using Ethylene Bridged Hybrid Technology (BEH) amide bonded stationary phases, separates compounds based on their hydrophilicity This makes HILIC ideally suited for the LC and LCMS analysis of released glycans, and glycopeptides.
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Waters glycan line offers labeled standards for column and system calibration and benchmarking, inclusive kits to ease the sample preparation burden and easy to use concentrated mobile phase buffers specific for glycan application work.
Chromatographic modes for the analysis and purification of proteins include reversed-phase, affinity, ion-exchange, hydrophobic interaction, and size-exclusion chromatography. These methods rely on taking advantage of chemical and physical differences between protein species.
Reversed-phase chromatography of proteins, done with columns consisting of wide-pore size particles ( e.g, 300Å) functionalized with short-ligand length chemistries, is a separation technique based on the relative hydrophobic characteristics of the proteins in solution. Gradients of increasing of organic solvent concentration are frequently used to affect separations in the presence of ion-pairing reagents that minimize undesired ionic interactions.
Reversed-phase chromatography of proteins, done with columns consisting of wide-pore size particles ( e.g, 300Å) functionalized with short-ligand length chemistries, is a separation technique based on the relative hydrophobic characteristics of the proteins in solution. Gradients of increasing of organic solvent concentration are frequently used to affect separations in the presence of ion-pairing reagents that minimize undesired ionic interactions.
Hydrophobic Interaction Chromatography (HIC) is characterized by the adsorption of compounds to a weakly hydrophobic surface at high salt concentrations, followed by elution with a decreasing salt gradient. This technique is well suited for protein separations due its non-denaturing characteristic.
Hydrophobic Interaction Chromatography (HIC) is characterized by the adsorption of compounds to a weakly hydrophobic surface at high salt concentrations, followed by elution with a decreasing salt gradient. This technique is well suited for protein separations due its non-denaturing characteristic.
Ion-exchange chromatography is a powerful technique with its ability to resolve different protein species, based on their surface charge. Separations are based on the use of either salt, pH, or salt/pH gradients.
Ion-exchange chromatography is a powerful technique with its ability to resolve different protein species, based on their surface charge. Separations are based on the use of either salt, pH, or salt/pH gradients.
Size exclusion, also known as gel filtration, chromatography separates biomolecules based on their sizes (hydrodynamic radii) in solution. This technique is frequently used to monitor aggregation of biotherapeutic proteins.
Size exclusion, also known as gel filtration, chromatography separates biomolecules based on their sizes (hydrodynamic radii) in solution. This technique is frequently used to monitor aggregation of biotherapeutic proteins.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
Waters protein standard line contains specially formulated and designed protein standard mixes to benchmark and monitor column performance and enhance and validate protein applications performed on UPLC, HPLC, or LC/MS.
Chromatographic modes for oligonucleotide separations include reversed phase and ion exchange. The applications include the analysis and purifications of synthetic oligonucleotides used in research, diagnostic reagents or biotherapeutic compounds.
The gradient separation of synthetic oligonucleotides by ion-pair reversed-phase LC is based on sequence length with shorter failure sequence eluting prior to desired product.
The gradient separation of synthetic oligonucleotides by ion-pair reversed-phase LC is based on sequence length with shorter failure sequence eluting prior to desired product.
HPLC-based ion-exchange chromatography, using a gradient of increasing salt concentration, can be effectively used to separate PCR products as well as plasmid forms based on differing charge density characteristics.
HPLC-based ion-exchange chromatography, using a gradient of increasing salt concentration, can be effectively used to separate PCR products as well as plasmid forms based on differing charge density characteristics.
Specially formulated, synthetic oligonucleotide standard designed for verification of HPLC/UPLC instrument and column performance for analysis of oligonucleotide applications.
The Oligonucleotide Standard line provides standards designed for verification of HPLC/UPLC instruments and performance of columns used for analysis of synthetic oligos. These specially formulated standards are unique to our column chemistry.
Amino acid analyses include the separation and quantitations of either free amino acids or amino acids derived from protein hydrolysates. Matrix effects and accurate quantitations are some of the challenges that are adressed by pre-column derivatization and high resolution chromatographic separations.
The gradient separation of precolumn derivitizated amino acids by ion-pair, reversed-phase LC is based on the different hydrophobic characteristics of each labeled constituent.
The gradient separation of precolumn derivitizated amino acids by ion-pair, reversed-phase LC is based on the different hydrophobic characteristics of each labeled constituent.
Waters amino acid kits and reagents are designed for accurate and reproducible quantitation of amino acids from various sample matrices using either UPLC or HPLC methods.
Waters amino acid kits and reagents are designed for accurate and reproducible quantitation of amino acids from various sample matrices using either UPLC or HPLC methods.