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Protein A Sepharose

Reusable Protein A conjugated Sepharose beads with ≥16 mg/ml binding capacity & 2.07 ml/min flow rate for antibody purification from multiple sources
Catalog #: 6501

Availability: In stock

SKU-Size Size Price Qty
6501-1 1 ml
$80.00
6501-5 5 ml
$235.00
6501-25 25 ml
$795.00
6501-100 100 ml
$2,295.00

Product Details

Highlights • CONTENTS
- Supplied as a 50% slurry in 20 % Ethanol/H2O.
- HIGH BINDING CAPACITY: Binding of IgG ≥16 mg human or rabbit IgG/ml Protein A-Sepharose.
- MINIMAL LEACHING OF THE LIGAND.
- FLOW RATE TESTED*: 2.07 ml/min.
*Test condition: Calculations based on the time required to pass 18 ml of water through 2 ml settled beads (column diameter 1.5 cm).
- USAGE: Reusable for up to 10 times without significant loss of binding capacity.
• APPLICATIONS
- Purification of monoclonal and polyclonal antibodies from culture media, serum, ascites fluid or hybridoma supernatants.
- Isolation of antibody/antigen complexes in immunoprecipitation experiments, since only the Fc region is involved in antibody binding and the Fab region is available for binding antigen.
Storage Conditions 4°C
USAGE For Research Use Only! Not For Use in Humans.

Details

Protein A-Sepharose beads are prepared by covalently coupling recombinant Protein A to 6% cross-linked Sepharose beads. BioVision Protein A (Cat. # 6500, Cat. # 6500B) is a genetically engineered protein containing five IgG-binding regions of native Protein A. The cell wall binding region, albumin binding region and other non-specific regions have been eliminated from the recombinant Protein A to ensure the maximum specific IgG binding. The coupling technique is optimized to give a higher binding capacity for IgG & minimum leaching of recombinant Protein A. The IgG binding capacity of Protein A-Sepharose is ≥ 16 mg human or rabbit IgG per ml of wet beads. Protein A-Sepharose beads display high chemical & physical stability as well as high flow rate, hydrophilicity & high gel strength. It can be used for IgG purification and immunoprecipitation.


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