MagReSyn® Protein A

High capacity Protein A for affinity purification of antibodies and immunoprecipitation

MagReSyn® Protein A microparticles contain covalently coupled Protein A for highly specific single-step purification of IgG to >95% purity from whole serum samples. Protein A is a ~56 kDa surface protein originally isolated from the cell wall of the bacterium Staphylococcus aureus and is widely used for highly specific purification of IgG antibodies and for immunoprecipitation experiments. Protein A has 5 immunoglobulin binding domains folded into a three-helix bundle and specifically binds the Fc region on the heavy chain of the IgG class of antibodies. More specifically, Protein A binds with high affinity to specific subclasses of human, rabbit, mouse, guinea pig, cat and pig IgG. It does not react with human IgG3, IgD or IgE, mouse IgM, IgA or IgE, or goat, koala and llama IgG. The high recombinant Protein A content of MagReSyn® ensures a high immunoglobulin capacity allowing for experimental miniaturization.

Support: Proprietary polymer microparticles containing iron oxide (magnetite) with immobilized Protein A
Binding capacity: > 2.4 (Rabbit IgG)
Bead size: ~5-10 µm
Formulation: 15 suspension in Tris buffer


MagReSyn® Protein A MAX

Ultra-capacity Protein A for the affinity purification of antibodies and immunoprecipitation

MagReSyn® Protein A MAX microparticles have been specially engineered for custom applications where maximum antibody binding is desired. This includes microplate applications where miniaturization and high-throughput automated analysis are required.

Binding capacity: > 4.8 (Rabbit IgG)
Bead size: ~5-10 µm
Formulation: 15 suspension in Tris buffer

* Please note that MagReSyn® Protein A MAX is a custom product and requires 2 weeks lead time from date of order *


Product Resources

MagReSyn® Protein A Performance Superiority

Superior binding capacity for IgG

  • Unparalleled miniaturization of experimentation
  • Sample concentration from dilute solutions to a minimal volume

Exceptional value

  • MagReSyn® Protein A binds over 4800 µg IgG per product compared to less than 3000 µg IgG for alternate products. MagReSyn® Protein A MAX binds over 9600 µg IgG per product

Exceptional stability

  • Obtain IgG purity of >95% in a single chromatography step from whole serum samples
  • Eliminates the need for additional purification steps

Vastly reduced Protein A leaching

  • Stable multipoint attachment of Protein A to the microparticles
  • Virtually no Protein A leaches during affinity capture and immunoglobulin elution

MagReSyn® Protein A microparticles provide superior binding capacity for IgG (over 160 µ compared to alternate suppliers. MagReSyn® Protein A MAX provides an unparalleled IgG binding capacity in excess of 320 µ for specialized applications. Green bars represent MagReSyn®, orange bars represent alternate suppliers

Protein A leaching was tested using a Protein A ELISA kit (GenScript) on comparative microparticle quantities required to purify 100 µg of rabbit IgG. Alternate products were evaluated using their recommended protocols.

Comparative assessment of IgG binding capacity of MagReSyn® Protein A (lane 8) against two leading alternate products (lanes 6 & 7). All samples were purified using equal quantities of microparticles (1 mg each) and the suppliers’ recommended purification protocols and buffers. MagReSyn® microparticles show superior IgG capacity and purity (arrows). Lane 1: molecular weight markers, Lane 2: whole serum sample, Lanes 3-5: pooled unbound and wash fractions for the two alternate products and MagReSyn® Protein A  respectively.

Specific enrichment of IgG from rabbit serum using MagReSyn® Protein A and alternate suppliers’ magnetic Protein A microparticles. The quantity of alternate suppliers’ microparticles was adjusted to equivalent binding capacity to compare the purity of the isolated IgG. Lane 1: molecular weight markers, Lane 2: whole rabbit serum, Lane 3: MagReSyn® Protein A-purified IgG, Lane 4: Alternate product 1, Lane 5: Alternate product 2. MagReSyn® microparticles show significantly higher specificity for the target protein. IgG heavy and light chain fragments appear as two distinct bands on the gel.

Products supplied by ReSyn Biosciences (Pty) Ltd are for research purposes only. ReSyn products are not to be used for diagnostic, therapeutic or commercial means any use resulting in monetary gain, including, but not limited to, incorporation in a kit, repackaging and re-formulation. Please enquire about sub-licenses for commercial use.

Citations and References

Plant-based production of highly potent anti-HIV antibodies with engineered posttranslational modifications

–  Advaita Acarya Singh et al.

Nature Scientific Reports (2020)

MagReSyn® Protein A

Immune genes are primed for robust transcription by proximal long noncoding RNAs located in nuclear compartments

–  Stephanie Fanucchi et al.

Nature Genetics (2018)

MagReSyn® Protein A, Protein G, & Streptavidin

REVERBa couples the circadian clock to hepatic glucocorticoid action

–   Giorgio Caratti et al.

Journal of Clinical Investigation (2018)

MagReSyn® Protein A & Protein G

LRP1 is required for novobiocin-mediated fibronectin turnover

–   Natasha Marie-Eraine Boel et al.

Scientific Reports 8 (2018)

MagReSyn® Protein A

Circadian clock component REV-ERBα controls homeostatic regulation of pulmonary inflammation.

–   Marie Pariollaud et al.

Journal of Clinical Investigation 128 (2018)

MagReSyn® Protein A

An Unbiased Mass Spectrometry Approach Identifies Glypican-3 as an Interactor of Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) and LDL Receptor in Hepatocellular Carcinoma Cells

–   Kévin Ly et al.

JBC 291 (2016)

MagReSyn® Protein A

Phosphoproteomic analysis of interacting tumor and endothelial cells identifies regulatory mechanisms of transendothelial migration

–   Marie Loucard-Paulet et al.

Science Signaling 9 (2016)

MagReSyn® Protein A