MagReSyn® Protein G
High capacity Protein G for affinity purification of antibodies and immunoprecipitation
MagReSyn® Protein G is a proprietary magnetic polymeric microparticle support that provides a simple and convenient method for highly specific capture of various immunoglobulins from biological samples. Recombinant Streptococcal Protein G (lacking the albumin binding region for increased immunoglobulin specificity) is covalently linked to the magnetic microparticles reducing leaching during your experimentation, and potentially stabilizing the Protein G for applications in non-standard conditions. Protein G binds to most mammalian immunoglobulins with greater affinity than Protein A, including human IgG3 and rat IgG2a. It does not react with human IgM, IgD or IgA.
The high recombinant Protein G content of MagReSyn® ensures a high immunoglobulin capacity allowing for experimental miniaturization. MagReSyn® Protein G microparticles have been engineered to be highly specific, providing single step purification of IgG to >95% from whole serum samples.
Support: Proprietary polymer microparticles containing iron oxide (magnetite) with immobilized Protein G
Binding capacity: > 2.4 mg.ml-1 (Rabbit IgG)
Bead size: ~5-10 µm
Formulation: 15 mg.ml-1 suspension in Tris buffer
MagReSyn® Protein G Performance Superiority
MagReSyn® Protein G microparticles provide superior binding capacity for IgG (over 160 µg.mg-1) compared to alternate suppliers.
Green bars represent MagReSyn®, orange bars represent alternate products.
TERMS AND CONDITIONS
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
Hypoxia regulates GR function through multiple mechanisms involving microRNAs 103 and 107
– Nan Yang et al.
Molecular and Cellular Endocrinology (2020)
p38α MAPK proximity assay reveals a regulatory mechanism of alternative splicing in cardiomyocytes
– Audrey-Ann Dumont et al.
BBA – Molecular Cell Research 1866 (2019)
An improved method of quantitative ChIP studies of nuclear receptor function
– Ann Louise Hunter et al.
Journal of Molecular Endocrinology 62 (2019)
Immune genes are primed for robust transcription by proximal long noncoding RNAs located in nuclear compartments
– Stephanie Fanucchi et al.
Nature Genetics (2018)
REVERBa couples the circadian clock to hepatic glucocorticoid action
– Giorgio Caratti et al.
Journal of Clinical Investigation (2018)