GTxResolve Premier BEH Amide Columns
High resolution, MS-compatible analysis for a wide range of GTx applications
Hydrophilic interaction chromatography (HILIC) is widely used for the retention and analysis of polar analytes, allowing analysts to separate up to 100 residue long single and double stranded oligonucleotides.
Accelerate the analysis of your polar analytes with Waters GTxResolve Premier BEH Amide methods that offer drug developers a platform approach for multiple analytes, and provide a valuable alternative to ion-pairing reversed-phase (IP-RP) methods that require dedicated LC and LC-MS systems.
- GTxResolve Premier Amide columns are double batch-tested to ensure optimal chromatographic performance for cell and gene therapeutics.
- Robust amide-bonded stationary phase provides numerous separation possibilities for an extensive range of nucleic acids and viral proteins.
- Reduce the need for lengthy column conditioning using low adsorption column hardware for improved recovery.
- Eliminate dependency on running separations with ion-pairing dedicated LC-MS systems.
GTxResolve Premier BEH Amide Columns
Specifications
Overview
- Implement complementary separations to ion-pairing RPLC reversed phase liquid chromatography (RPLC)
- Prepare simple ammonium based, ion-pair free mobile phases
- Develop versatile separation options for oligonucleotides, CRISPR sgRNA, mRNA, and viral capsid proteins
- Utilize low adsorption hardware that provides high sample recovery even from the first injection
- Gain confidence knowing every column is double batch tested with both protein and oligonucleotide reference materials
Recommended Use: Improve your therapeutic understanding with stability and potency-indicating assays.
Evaluating duplex siRNA and their single stranded impurities
Analysis of siRNA in both denaturing and non-denaturing conditions allows full characterization of products and their related impurities. Scientists can easily apply HILIC methods with both denaturing and non-denaturing conditions to help support purity and identity measurements of small interfering RNA (siRNA). At room temperature, the annealed duplex maintains its structure. Above the melting temperature (~40 °C), the duplex dissociates into its individual constituents. The gentle nature of HILIC’s buffered mobile phase enables duplex formation and supports the presence of excess non-hybridized single stranded RNA (ssRNA). There is a significant promise in these approaches for both development and release testing.
Analysis of viral capsid proteins
HILIC is an alternative to reversed-phase analysis for separating virus like particle (VLP) components and viral vector capsid protein isoforms. Viral protein ratios and modifications can be evaluated with UV, MS, and fluorescence detection. Oxidized and phosphorylated variants can be readily resolved from their unmodified counterparts with an optimally applied HILIC separation.
Nucleic acid sizing up to 100 mers with HILIC
Improved resolution of oligonucleotides and digested nucleic acids can be achieved using a GTxResolve Premier BEH Amide Column and its optimized sorbent particles. While different pore size sorbents exhibit similar chromatographic resolution at shorter nucleotide lengths, the wide pore 300 Å exhibits remarkable separation up to 100-mers. The utility of larger pores is not only observed for nucleic acids, but also allows for the diffusion of larger proteins which comprise viral capsids. Wide pore particles enable versatile separations for a wide range of cell and gene therapeutics.
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