1.Details
Ion Exchange Chromatography (IEC) is the most commonly used method for the separation and purification of biomacromolecules based on the type, number, and distribution of its specific surface charges. Q HL anion exchange resins use polymethacrylate as the matrix. The hydrophilicity of the matrix is improved through surface modification. The high loading ligand improves the binding performance of ion exchange groups, resulting in advantages such as high DBC, low non-specific binding, and excellent biocompatibility. It fully meets the separation and purification needs of biological macromolecules including peptides, recombinant proteins, nucleic acids, vaccines, antibodies, viruses, and virus-like particles. High flow-through capacity is also suitable for viscous loading samples. Products with different sizes and pore sizes are available according to application needs, meeting the requirements of capture, intermediate purification, polishing, and analytical purification processes. Duoning provides comprehensive solutions for biological sample purification from laboratory to industrial production.
2.Features
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Properties
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HPQHL-30
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HPQHL-60
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Average Particle Size
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40μm±10μm
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70μm±20μm
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Pore Size
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30nm
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Matrix
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Polyacrylate
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Ligand
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quaternary ammonium group (-CH2N+ (CH3)3)
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Type of Ligand
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Strong base ligand
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Dynamic binding Capacity
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≥85mg BSA/ml wet resin gel
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Application
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Polishing of recombinant proteins, enzymes, peptides, nucleic acids, etc.
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purification of proteins, enzymes, polysaccharides, nucleic acids, etc.
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Maximum Pressure Limit
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1 MPa
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pH Stability
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pH 3-13
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Storage
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2~30 ℃(20%Ethanol)
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Chromatographic operation Procedure
Ion exchange resin is widely used for the separation and purification of proteins, enzymes, polysaccharides, nucleic acids, etc. Chromatographic operation typically includes steps such as equilibration, sample loading, washing, elution, and regeneration. The specific operating methods are as follows:
Equilibration: Equilibrate the column with 5-10 column volumes (CV) of equilibration buffer (e.g., 20 mM PB, pH 7.0; the specific buffer system should be selected and optimized based on the stability and isoelectric point of the target protein) at a flow rate not exceeding the maximum pressure limit, until the conductivity and pH of the effluent remain constant (consistent with the equilibration buffer).
Sample Loading: The sample loading buffer should be as consistent as possible with the equilibration buffer; solid samples can be dissolved and prepared in equilibration buffer; dilute samples can be dialyzed with equilibration buffer or supplemented with the corresponding amount of salt; concentrated sample solutions can be diluted with equilibration buffer. To avoid clogging the chromatography column, sample solutions should be centrifuged or microfiltered (0.45 μm). The loading volume should be calculated based on the binding capacity and the target protein content in the sample solution.
Washing: After loading, continue washing with equilibration buffer until the UV absorbance drops to baseline.
Elution: Elute with elution buffer (e.g., 20 mM PB + 1M NaCl, pH 7.0). Elution methods include pH gradient elution, linear gradient elution, or step gradient elution.
Regeneration: After each cycle, clean the column with 1-2 M NaCl to remove strongly bound proteins.
Cleaning In Place (CIP): After 5-10 uses (the specific number depends on the type and source of raw materials and experimental requirements), the column requires Cleaning In Place, which can refer to the table below.
Storage: Store in 20% ethanol at 2-30°C; The unpacked resins can be flushed with 20% ethanol and then stored at 2-30°C.
Other Considerations: When using and storing the column, avoid letting it run dry or become poorly sealed to prevent air bubbles from entering.
3.Specification

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