SKU: 186007637
XBridge Protein  BEH  SEC  Column, 125Å, 3.5 µm, 7.8 mm X 300 mm

XBridge Protein BEH SEC Columns | 186007637


Streamline Purchasing with Customized Quotes

Streamline Purchasing with Customized Quotes

Shop on Waters.com and add items to your cart

Navigate to the Shopping Cart

Select Request a Quote to get your quote instantly


Product Description

XBridge Protein BEH SEC, 125 Å Columns, containing 3.5um particles are based on the same Waters Ethylene Bridged Hybrid (BEH)-based particle technology and diol-bonded surface coating as used in our successful line of HPLC-based SEC columns.   They are best suited to separate proteins ranging from 1,000 – 80,000 Daltons.  Note: P/N 176003593 contains an XBridge Protein BEH SEC, 125 Å, 3.5um  7.8 x 300 Column with one vial the BEH125 SEC Protein Std (P/N 186006519)

Specifications

  • Chemistry

    SEC

  • Separation Mode

    SEC

  • Particle Substrate

    Hybrid

  • pH Range Min

    2 pH

  • pH Range Max

    8 pH

  • Endcapped

    No

  • Bonding Technology

    SEC

  • Silanol Activity

    Low

  • Particle Shape

    Spherical

  • Particle Size

    3.5 µm

  • Endfitting Type

    Waters

  • Pore Size

    125 Å

  • QC Tested

    Protein

  • Format

    Column

  • Surface Area

    395

  • System

    HPLC

  • Particle Technology

    BEH

  • USP Classification

    L33

  • Inner Diameter

    7.8 mm

  • Length

    300 mm

  • Carbon Load

    12 %

  • UNSPSC

    41115709

  • Application

    Protein

  • Brand

    XBridge

  • Product Type

    Columns

  • Units per Package

    1 pk

Hazaradous Material This product contains hazardous material which requires special freight handling. Additional charges may apply.

Product Support

Documents

Documents



What do you want to do?

What do you want to do?

Related Products

Back To Top Back To Top

XBridge Protein BEH SEC Column, 125Å, 3.5 µm, 7.8 mm X 300 mm

Easily develop and transfer SEC methods based on laboratory instrumentation with the XBridge Protein BEH SEC Column. The column enables you to also develop methods based on required protein component resolution, and sample throughput requirements.

Developed especially for the chromatography of size-exclusion chromatography of proteins, the XBridge Protein BEH SEC Columns complement Waters existing line of smaller particle size, UPLC-based SEC columns.

Get exceptional column life with the XBridge Protein BEH SEC Column that offers less non-desired, protein and column interactions compared to silica-based SEC columns. It offers HPLC-based SEC resolution of proteins from 10-1,500K Daltons with higher throughput capability. These diol-bonded XBridge Protein BEH SEC Columns offer flow and pressure tolerance for increased sample throughput on HPLC systems. They combine BEH base particle technology with innovative diol bonding processes to deliver column stability, performance, and lifetime.

You may also be interested in the XBridge Protein BEH SEC Guard Column, 125Å, 3.5 µm, 7.8 mm X 30 mm. The column guard is designed to extend the lifespan of your analytical column by eliminating any chemical or particulate contaminants from the mobile phase, and thus, preserving the column and ensuring you get the most accurate and precise results.

Check our complete range of available products, browse through our online inventory, and shop for lab equipment.

How Does SEC Work?

Size exclusion chromatography (SEC) is a Liquid Chromatography technique that is commonly used to monitor protein aggregates throughout the commercialization process of a biotherapeutic protein. This includes monoclonal antibodies. The technique, also known as molecular sieve chromatography, separates molecules based on their size, and in some cases molecular weight. It is usually applied to large molecules or macromolecular complexes such as proteins and industrial polymers. Usually, HPLC-based SEC methods use columns packed with >3 µm particles of an appropriate pore size for the separation of proteins of different hydrodynamic radii. The proteins are ideally separated solely on their relative size in solution, with larger aggregate species eluting prior to the desired monomer drug.