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ReadiPrep™ Protein G Magnetic Agarose Beads

Protein G magnetic agarose beads are used extensively for immunoprecipitation (IP) studies and purification of immunoglobulins (IgGs).
  • High capacity — binds greater than 10 mg of rabbit IgG per 1 mL of beads
  • Exceptional performance — improve sample throughput and recovery while minimizing loss
  • Flexible application — purify antibodies from serum, tissue extracts and other complex samples
Protein G magnetic agarose beads are provided as a 25% (250 mg / mL) suspension and are capable of binding greater than 10 mg / mL of antibody depending on the species. High quality manufacturing ensures consistent batch-to-batch performance.

To use, beads are first added to the sample, capturing antibodies of interest. Then the beads are washed while held in place by a magnet. Finally, the target is eluted using a low pH elution buffer. This process eliminates the need for centrifugation, reducing hands-on time, while maximizing sample recovery.

Protein G is a streptococcal bacteria derived protein that specifically targets the Fab and Fc regions of immunoglobulins (IgGs). The table below shows the binding affinity of protein G and protein A for IgGs of different species [1,2].

SpeciesImmunoglobulin (IgG)Protein G bindingProtein A binding
HumanIgG++++++++
IgG1++++++++
IgG2++++++++
IgG3++++-
IgG4++++++++
MouseIgG1+++++
IgG2a++++++++
IgG2b++++++
IgG3+++++
RatIgG1+-
IgG2a++++-
IgG2b++-
IgG2c+++
RabbitIgG+++++++
SheepIgG++-
GoatIgG++-

[1] Akerström, B., Brodin, T. H. O. M. A. S., Reis, K. A. T. H. L. E. E. N., & Björck, L. A. R. S. (1985). Protein G: a powerful tool for binding and detection of monoclonal and polyclonal antibodies. Journal of immunology (Baltimore, Md.: 1950), 135(4), 2589-2592.

[2] Björck, L., & Kronvall, G. (1984). Purification and some properties of streptococcal protein G, a novel IgG-binding reagent. Journal of Immunology (Baltimore, Md.: 1950), 133(2), 969-974.

References

View all 17 references: Citation Explorer
Stability, enrichment, and quantification of total and HPV16-specific IgG present in first-void urine.
Authors: Téblick, Laura and Lipovac, Marijana and Bell, Margo and De Smet, Annemie and De Meester, Ingrid and Delputte, Peter and Vorsters, Alex
Journal: Scientific reports (2024): 14441
Bioprospection and Selection of Peptides by Phage Display as Novel Epitope-Based Diagnostic Probes for Serological Detection of HTLV-1 and Use in Future Vaccines.
Authors: Machado, Luiz Fernando Almeida and Filho, Luiz Ricardo Goulart and Santos, Fabiana Almeida Araújo and Siravenha, Leonardo Quintão and Silva, Andrea Nazaré Monteiro Rangel and Queiroz, Maria Alice Freitas and Vallinoto, Antonio Carlos Rosário and Ishak, Marluísa Oliveira Guimarães and Ishak, Ricardo
Journal: Frontiers in medicine (2022): 884738
Analytical methods of antibody surface coverage and orientation on bio-functionalized magnetic beads: application to immunocapture of TNF-α.
Authors: Laborie, Etienne and Le-Minh, Victor and Mai, Thanh Duc and Ammar, Mehdi and Taverna, Myriam and Smadja, Claire
Journal: Analytical and bioanalytical chemistry (2021): 6425-6434
Data on antigen recognition hindrance by antibodies covalently immobilized to Protein G magnetic beads by dimethyl pimelimidate (DMP) cross-linking.
Authors: Caminha, Marcelle A and de Lorena, Virginia Maria B and de Oliveira Júnior, Wilson and Perales, Jonas and Carvalho, Paulo C and Lima, Diogo B and Cavalcanti, Maria da Glória A M and Martins, Sílvia M and Valente, Richard H and Menna-Barreto, Rubem F S
Journal: Data in brief (2019): 516-521
A proteome-wide immuno-mass spectrometric identification of serum autoantibodies.
Authors: Music, Milena and Soosaipillai, Antoninus and Batruch, Ihor and Prassas, Ioannis and Bogdanos, Dimitrios P and Diamandis, Eleftherios P
Journal: Clinical proteomics (2019): 25
Page updated on September 11, 2024

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Physical properties

Solvent

N/A

Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22

Storage

Refrigerated (2-8 °C)
UNSPSC12352200