Agilent, PL1912-1503, PLRP-S 4000Å, 2.1 x 50 mm, 5 µm

PLRP-S 4000Å, 2.1 x 50 mm, 5 µm. Reversed-phase HPLC column with fully porous PS/DVB particle support stable at elevated temperatures and a wide pH range(1-14). Available in range of particle and pore sizes for targeted applications

Specifications:
Brand: PLRP-S
Hardware: SS
Inner Diameter (ID): 2.1 mm
LC Platform: Stainless Steel
Length: 50 mm
Maximum Temperature: 200 °C
Part Number Application Domain: Biopharma
Part Number Application: Intact & Subunit AnalysisMonoclonal Antibodies (mABs)PeptidesProteins
Particle Size: 5 µm
Particle Type: Fully Porous
Phase: DVB
Pore Size: 4000 Å
Pressure Rating: 207 bar
Separation Mode: Reversed Phase
Shipping Solvent: Acetonitrile/Water
Technique: LCLC & LC/MS
UNSPSC Code: 41115711
pH Range: 1-14

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This reversed-phase high-performance liquid chromatography column features a 5 micron particle size and a pore diameter of 4000 angstroms, making it highly effective for the analysis and purification of large biomolecules, such as proteins, peptides, and oligonucleotides. With dimensions of 2.1 by 50 millimeters, it is optimized for rapid separations with high resolution and excellent sample recovery. The chemically stable, polymeric stationary phase offers superior performance across a wide pH range, providing robust operation for both analytical and semi-preparative workflows.

Ideal for use in research and quality control environments, this column supports applications such as intact protein characterization, antibody analysis, and the study of post-translational modifications. Its large pore structure is specifically designed for high molecular weight compounds, ensuring minimal analyte degradation or loss. It is fully compatible with standard HPLC and UHPLC systems from Agilent and other major manufacturers, facilitating easy integration into existing laboratory setups. For enhanced workflow flexibility, it may be used in conjunction with related chromatographic columns of different pore sizes to address a broader spectrum of analytical challenges in proteomics and biopharmaceutical development.