SKU: 186004505
XBridge Protein BEH C4 Column, 300 Å, 3.5 µm, 4.6 mm x 250 mm, 1/pk

XBridge Protein BEH C4 Columns | 186004505


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

The XBridge Protein BEH C4, 300 Å, 3.5 µm, 4.6 mm x 250 mm column is QC tested and optimized to separate proteins based on size, hydrophobicity and isoelectric point. If you compare to traditional C18 phases, the C4 ligand is less retentive and will minimize protein carryover, increase protein recovery, and improve peak capacity.

Specifications

  • Chemistry

    C4

  • Separation Mode

    Reversed Phase

  • Particle Substrate

    Hybrid

  • pH Range Min

    2 pH

  • pH Range Max

    10 pH

  • Maximum Pressure

    6000 psi (415 Bar)

  • Endcapped

    No

  • Silanol Activity

    Low

  • Molecular Weight Range Max

    150000

  • Particle Shape

    Spherical

  • Particle Size

    3.5 µm

  • Endfitting Type

    Waters

  • Pore Size

    300 Å

  • QC Tested

    Protein

  • Format

    Column

  • Surface Area

    90

  • System

    HPLC

  • Particle Technology

    BEH

  • USP Classification

    L26

  • Inner Diameter

    4.6 mm

  • Length

    250 mm

  • Carbon Load

    8 %

  • UNSPSC

    41115709

  • Application

    Protein

  • Brand

    XBridge

  • Product Type

    Columns

  • Units per Package

    1 pk

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 C4 Column, 300Å, 3.5 µm, 4.6 mm X 250 mm, 10K - 500K, 1/pk

Benefit from the XBridge Protein BEH C4 Column’s Protein Separation Technology which incorporates BEH technology and uses synthetic particles that offer the highest quality combined with consistent performance.

The XBridge Protein BEH C4 Column is QC tested with a peptide map to ensure the stability of peptide separation methods. This is made possible using well-characterized, state-of-the-art bonding procedures for the C18 ligand. In addition to this, it guarantees predictable behavior with the variety of samples that are used in proteomics, protein characterization, and peptide synthesis. The resulting analytical column offers consistent batch-to-batch synthetic peptide and protein digest separations. The manufacturing techniques used for the lab equipment ensure stable particle structure and bonding chemistry from pH 1 to 12 and at elevated temperatures.

Get exceptional separation of a wide variety of peptides using the XBridge Protein BEH C4 Column. It also delivers narrow and symmetrical peaks for maximum resolution. For optimal chromatography, the XBridge Protein BEH C4 Column provides superior peak shape and retention in formic acid and trifluoroacetic acid.

To find more variants of the product listed here, products compatible with it, and to shop for lab equipment, browse through our catalog. It will also enable you to reach out to our offices worldwide and contact members of our staff should you have any queries regarding the products or the technology.

You may also be interested in LCGC Certified Clear Glass 12 x 32 mm Screw Neck Vial, with Cap and Preslit PTFE/Silicone Septum, 2 mL Volume, 100/pk that makes it possible for you to store your analytes, samples, and solutions in a chemically inert vial so that you get reliable and interference-free results from your analysis. All Waters LC/GC certified vials are also UV-tested by HPLC, the test used to detect trace levels of chemicals used in packaging and manufacturing processes.

What Happens When A Protein Precipitates?

Precipitation can occur due to a change in pH or if the hydrophobicity alters interactions between the protein and the aqueous environment. It can also happen through binding of salts or metals to protein functional groups such that intramolecular interactions are disrupted. As a result of this precipitation, the proteins denature, aggregate, and fall out of solution.