Product nameProtein G Resin - Amintra®
DescriptionProtein G Resin - Amintra®
Protein G Resin - Amintra® (ab270309) is an affinity chromatography medium designed for easy, one-step purification of classes, subclasses and fragments of immunoglobulins from biological fluids and from cell culture media. The recombinant protein G ligand is coupled to highly cross-linked 4% agarose. The binding capacity of Protein G Resin - Amintra® is greater than 30mg human lgG/mL medium. With the high binding capacity and chemical stability, very high batch-to-batch reproducibility, which ensures excellent performance on isolation of immune complexes.
This product is manufactured by Expedeon, an Abcam company. Expedeon product code APG0005 was previously called Amintra Protein G - 5 ml medium (10 ml in 50% slurry) and is the same as the 5 mL size of this product. Expedeon product code APG0025 was previously called Amintra Protein G - 25 ml medium (50 ml in 50% slurry) and is the same as the 25 mL size. Expedeon product code APG0100 was previously called Amintra Protein G - 100 ml medium (200 ml in 50% slurry) and is the same as the 100 mL size.
- Supporting matrix: Highly crosslinked 4% agarose supplied as a 50% slurry
- Ligand: Recombinant Protein G
- Bead size range: 45-165 µm
- pH stability: long term: pH 3 – 9 –short term: pH 2 – 10
- Typical binding capacity: >30 mg Human IgG /ml resin
- Maximum pressure: 0.3MPa (3 bar)
- Chemical stability: High. The IgG binding capacity and recovery was maintained after storage for:
- 7 days at 37° in:
- 1 M acetic acid pH 2.0, 20 mM sodium phosphate, 1% SDS, pH 7.0
- 6 M Guandine-HCl, pH 7.0
- 70% ethanol
- 2 hours at room temperature in:
- 0.1 M HCl, pH 1.0
- 8 M urea, pH 10.5
- 0.1 M Glycine-NaOH, pH 11.0
- 7 days at 37° in:
- Solubility in water: Insoluble
Protein A and Protein G Antibody binding affinity:
Storage instructionsShipped at 4°C. Store at +4°C. Please see notes section.
Storage bufferConstituent: 20% Ethanol
Concentration information loading...
ab270309 has not yet been referenced specifically in any publications.