Agilent, 5190-6903, Bio-Monolith Recombinant Protein A, 4.95 x 5.2 mm

Bio-Monolith Recombinant Protein A, 4.95 x 5.2 mm. A biomonolith recombinant Protein A column which has a tendency for less non-specific binding and increased robustness. Store columns at 4-8 °C, extra delivery cost for cold shipment.

Specifications:
Brand: Bio-Monolith Protein A
Hardware: SS
Inner Diameter (ID): 5.2 mm
LC Platform: Stainless Steel
Length: 5 mm
Maximum Temperature: 40 °C
Particle Type: Monolith
Phase: Protein A
Pressure Rating: 150 bar
Separation Mode: Affinity
Shipping Solvent: 20mM Tris + 20% Ethanol
Storage Temp Conditions: Refrigeration required, 2-8°C
Technique: LC
pH Range: 2-11

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The Bio-Monolith Recombinant Protein A, 4.95 x 5.2 mm, is a high-performance affinity chromatography column designed for the rapid purification and analysis of immunoglobulins from complex biological samples. Utilizing stable recombinant Protein A immobilized on a robust monolithic polymer support, this column offers exceptional binding capacity and low nonspecific adsorption, ideal for both analytical and preparative workflows. Its advanced structure allows for high flow rates and minimal backpressure, facilitating faster processing and seamless integration into both manual and automated purification systems.

This monolith is particularly well-suited for applications in protein characterization, monoclonal antibody screening, and process development within biopharmaceutical and academic research laboratories. Compatible with Agilent liquid chromatography instruments, including the 1260 Infinity II and 1290 Infinity II series, it ensures reliable and reproducible results. The compact cartridge format supports easy scalability and integration with existing workflows. For optimal performance, it can be paired with Agilent’s range of chromatography accessories and reagents. The Bio-Monolith is an excellent choice for laboratories seeking efficient, high-throughput solution for immunoglobulin purification and analysis, supporting rigorous research and development in protein science.