Product nameAnti-HA Affinity Resin - Amintra®
DescriptionAnti-HA Affinity Resin - Amintra®
Anti-HA Affinity Resin - Amintra® (ab270603) is designed for simple, rapid HA-tagged recombinant protein purification and immunoprecipitation.
This product is manufactured by Expedeon, an Abcam company. Expedeon product code AHA0001 was previously called Amintra® Anti-HA Affinity Resin - 1ml Medium and is the same as the 1 mL size of this product. Expedeon product code AHA0005 was previously called Amintra® Anti-HA Affinity Resin - 5ml Medium and is the same as the 5 mL size.
The HA tag is derived from the human influenza virus HA protein corresponding to amino acids 98-106 (YPYDVPDYA). The HA tag does not appear to interfere with the bioactivity or the biodistribution of the recombinant HA-tagged protein, so it has been extensively used as a general epitope tag at the N-terminal or C-terminal of the fusion protein. Anti-HA Affinity Resin - Amintra® is based on a 4% agarose beads matrix, and non-specific binding is rare. It can be used for HA fusion protein purification and immunoprecipitation.
The characteristics of Anti-HA Affinity Beads are summarized below:
Item Description Matrix 4% agarose beads Ligand Anti-HA Antibody Binding capacity >1mg HA fusion protein/ml medium Particle Size (μm) 45–165 Max. Pressure 0.1 MPa, 1 bar Storage buffer 1 x PBS with 0.02% NaN3 Storage Temperature 2ºC – 8ºC
For the purification of your HA-tagged fusion proteins, Amintra® Anti-HA Affinity Beads can be used in column chromatography, batch format and immunoprecipitation.
For large volumes of sample, column chromatography or batch format are recommended to quickly capture the target protein from a large volume of extract.
When a small amount of sample is being purified, immunoprecipitation procedure is recommended.
- One step purification
- Binding capacity: > 1 mg HA fusion protein/mL medium
- Highly specific
Storage instructionsShipped at 4°C. Store at +4°C. Do Not Freeze.
Storage bufferPreservative: 0.02% Sodium azide
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ab270603 has not yet been referenced specifically in any publications.