Overview

  • Product name

    Protein A/G Sepharose®
  • Product overview

    High binding capacity Protein A/G Sepharose (>20 mg IgG/mL). Minimal leaching of ligand. Suitable for column or batch purification of IgG, immunoprecipitation & ChIP.


    Contents:


    Supplied as a 50% slurry in 20% Ethanol; > 5mg Protein A/G per mL Sepharose® beads.


     


    Features:


    Binding capacity greater than 20 mg/mL of wet gel; high flow rate; low falling off of rProtein A/G; pH stability 2-10.


    These beads are for use in column purification. If used in batch purification, we recommend not exceeding 150 x g when centrifuging.


    Store beads at 4°C.


    The beads may be damaged above 40°C.


    DO NOT FREEZE.


    Wash beads 3 times with 3x bead volume of desired buffer before use.


     


    Applications:


    Purification of monoclonal and polyclonal antibodies.


     


    Sepharose is a registered trademark of GE Healthcare

  • Notes

    Protein A/G Sepharose® is prepared by covalently coupling recombinant Protein A/G (contains five Ig-binding regions of protein A and three Ig-binding regions of protein G) to 6% cross-linked Sepharose® beads. The coupling was optimized to give a high binding capacity for IgG. The capacity of IgG binding could be greater than 10 mg of rabbit IgG per ml of wet gel.

  • Tested applications

    Suitable for: Purificationmore details

Properties

Applications

Our Abpromise guarantee covers the use of ab193262 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

Application Abreviews Notes
Purification Use at an assay dependent concentration.

Purification of monoclonal and polyclonal antibodies.

References

This product has been referenced in:

  • Le-Bel G  et al. Analysis of the proteasome activity and the turnover of the serotonin receptor 2B (HTR2B) in human uveal melanoma. Exp Eye Res 184:72-77 (2019). Read more (PubMed: 31002821) »
  • Albrecht LV  et al. Arginine methylation is required for canonical Wnt signaling and endolysosomal trafficking. Proc Natl Acad Sci U S A 115:E5317-E5325 (2018). Read more (PubMed: 29773710) »
See all 2 Publications for this product

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