Recombinant Protein A/G & Immobilized Protein A/G (5 Citations)
Catalog
Description
Size
Price(USD)
Qty
Catalog
786-836
786-836
Description
Immobilized Protein A/G Resin
Immobilized Protein A/G Resin
Size
3ml
3ml
$400.00
$400.00
Catalog
786-837
786-837
Description
Immobilized Protein A/G Resin
Immobilized Protein A/G Resin
Size
15ml
15ml
$1,450.00
$1,450.00
Catalog
786-838
786-838
Description
Immobilized Protein A/G Resin
Immobilized Protein A/G Resin
Size
5 x 1ml columns
5 x 1ml columns
$583.00
$583.00
Catalog
786-839
786-839
Description
Protein A/G Resin
Protein A/G Resin
Size
5 column kit
5 column kit
$778.00
$778.00
Catalog
786-840
786-840
Description
Immobilized Protein A/G Resin
Immobilized Protein A/G Resin
Size
10 x 0.2ml columns
10 x 0.2ml columns
$331.00
$331.00
Catalog
786-841
786-841
Description
Protein A/G Resin
Protein A/G Resin
Size
10 column kit
10 column kit
$427.00
$427.00
Catalog
786-2012
786-2012
Description
Recombinant Protein A/G
Recombinant Protein A/G
Size
1 mg
1 mg
$78.00
$78.00
Catalog
786-2013
786-2013
Description
Recombinant Protein A/G
Recombinant Protein A/G
Size
5 mg
5 mg
$208.00
$208.00
Recombinant Protein A/G contains four Fc-binding domains from Protein A and two from Protein G but lacks the albumin binding sites.
Immobilized Protein A/G consists of recombinant protein A/G ligand covalently immobilized onto 6% highly cross-linked agarose. The dynamic binding capacity will vary depending on several factors such as target antibody, flow rate etc.
Protein A/G binds well to IgG subclasses but does not bind IgA, IgM or serum albumin. This makes Protein A/G an excellent tool for purification and detection of monoclonal antibodies from IgG subclasses, without interference from IgA, IgM and serum albumin. Individual subclasses of monoclonals are likely to have a stronger affinity to the chimeric Protein A/G than to either Protein A or Protein G.
The Immobilized Protein A/G 1ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples. Each 1ml column enables purification of 1-13mg IgG from 0.5-2ml of serum or other sample.
The Immobilized Protein A/G 0.2ml spin column kit is ideal for the small scale affinity purification of antibodies form a variety of samples. Each 0.2ml column enables purification of 0.1-1mg IgG from 25-500µl of serum or other sample.
Specific binding and elution buffers are also available.
Click here to request bulk or custom sizes.
Features
- High binding capacity: 38mg human IgG/ml resin; >20mg sheep IgG/ml resin
- Ligand: Recombinant Streptococcal protein A/G lacking the albumin binding sites expressed in E. coli
- Bead size: 50-165μm
- Bead Structure: 6% highly cross-linked agarose
Applications
- Suitable for immunoaffinity chromatography and immunoprecipitation.
Protocol | |
786-836 | |
786-837 | |
786-838 | |
786-839 | |
786-840 | |
786-841 |
Material Safety Data Sheet | |
786-836 | |
786-837 | |
786-838 | |
786-839 | |
786-840 | |
786-841 | |
786-2012 | |
786-2013 |
Technical Literature | |
Protein A, Protein G, Protein A/G and Protein L Binding Affinity | A table highlighting the binding affinities of protein A, protein G, protein A/G and Protein L. Designed to help in the choice of Well-Coated™ plates. |
- Paul, Sangita et al (2022) Cyclin dependent kinsase 5 regulates cPLA2 activity and neuroinflammation in Parkinson's disease. ENEURO. https://doi.org/10.1523/ENEURO.0180-22.2022
- Paul, Sangita et al (2022) Cyclin dependent kinsase 5 regulates cPLA2 activity and neuroinflammation in Parkinson's disease. ENEURO. https://doi.org/10.1523/ENEURO.0180-22.2022
- Ahmed, S. et al (2017) Stabilization of a soluble, native-like trimeric form of an efficiently cleaved Indian HIV-1 clade C envelope glycoprotein. J Biol Chem.doi: 10.1074/jbc.M117.776419
- Das, S. et al (2017) Identification and characterization of a naturally occurring, efficiently cleaved, membrane-bound, clade A HIV-1 Env, suitable for immunogen design, with properties comparable to membrane-bound BG505. Virology 510:22
- McCabe, K. E. et al (2014) Cell Death Dis. DOI: 10.1038/cddis.2014.448