Agilent, 880995-209, ZORBAX StableBond 300 C3, 9.4 x 250 mm, 5 µm

ZORBAX StableBond 300 C3, 9.4 x 250 mm, 5 µm. A reversed-phase C3 semi-prep HPLC column with fully porous ZORBAX particles. StableBond technology ensures stability at low pH.

Specifications:
Brand: ZORBAX 300SB-C3
Hardware: SS
Inner Diameter (ID): 9.4 mm
LC Platform: Preparative HPLC
Length: 250 mm
Maximum Temperature: 80 °C
Part Number Application Domain: Biopharma
Part Number Application: Monoclonal Antibodies (mABs)PeptidesProteins
Particle Size: 5 µm
Particle Type: Fully Porous
Phase: 300SB-C3
Pore Size: 300 Å
Pressure Rating: 400 bar
Separation Mode: Reversed Phase
Shipping Solvent: Acetonitrile/Water
Technique: LCLC & LC/MS
UNSPSC Code: 41115709
pH Range: 1-8

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The ZORBAX StableBond 300 C3 column is designed to deliver robust and reproducible reversed-phase chromatography for bioanalytical and biopharmaceutical applications. With a dimension of 9.4 x 250 millimeters and 5 micron particle size, this column ensures excellent resolution and efficient separation of peptides, small proteins, and hydrophobic molecules. Its proprietary StableBond bonding technology offers reliable performance under low pH conditions, making it ideal for peptide mapping and protein analysis.

This column offers exceptional stability and consistency for high-throughput laboratories involved in proteomics, biotherapeutic characterization, or quality control. It is optimized for compatibility with most HPLC and UHPLC systems from Agilent and other leading manufacturers, supporting seamless integration into established workflows. Typical usage scenarios include separation of tryptic digests, peptide mapping for biopharmaceutical development, and general reversed-phase chromatographic procedures requiring reproducible retention times.

Pairing this column with related Agilent products such as compatible ZORBAX guard columns or advanced detector systems can further enhance analytical performance. It is a versatile choice for scientists requiring rigorous analytical reliability and sensitivity in peptide and protein separations across pharmaceutical, academic, and clinical research settings.