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Magnetic Beads

Magnetic Beads

Immunoprecipitation assays are fundamental for studying complex protein interactions that regulate cell physiology, gene expression and drive various types of disease. While agarose A/G beads have been the prevailing choice for quite some time, many labs have recently made the switch to Magnetic Beads after seeing results that are cleaner, more consistent and require less time. Just like agarose beads, magnetic beads bind to the Fc region of IgG as a means to isolate specific proteins and protein complexes from cell lysate. The advantage of magnetic beads is that they aggregate without the stress of centrifugation, which can significantly increase the yield of delicately attached protein complexes. Additionally, magnetic beads are easy to separate from supernatant by simply using a magnetic source close to your tube. This will allow the removal of unwanted supernatant without disturbing your protein pellet. Magnetic beads are also smaller and nonporous compared to agarose beads, so nonspecific binding and background signal is minimized.

Magnetic beads provide the same ability to isolate protein complexes as agarose beads with fewer steps and easier separation of pellet from the supernatant. Together, this translates to less experimental variability, reproducible data and confidence in your results. GenScript MagBeads are optimally designed for high capacity/Fc-specific IgG binding for immunoprecipiatation assays and small scale protein purification. Choose from our Protein A, Protein G, Protein A/G, or specially tagged magnetic beads and experience cleaner results in a shorter amount of time.

Key Features

  • Quick,easy and convenient magnetic separation procedures
  • Extremely gentle sample handling with no loss of your target
  • High binding capacity and reproducible results
  • Ideal for immunoprecipitation and micro-scale protein and antibody purification


  • Immunoprecipitation and micro-scale antibody purification
  • Micro-scale purification of His and GST tagged protein
  • Fast and flexible isolation of antibody and target protein

  • Product Details
  • Selection Guide
  • Customer Citations

Protein A, G and A/G MagBeads

Cat. No.
Product Name
L00273 Protein A MagBeads
4 ml
L00672-4 Protein A MagBeads MX
4 ml
L00274 Protein G MagBeads
2 ml
L00673-4 Protein G MagBeads MX
4 ml
L00277 Protein A/G MagBeads
2 ml

Tagged Protein Purification MagBeads

Cat. No.
Product Name
L00295 Ni-charged MagBeads
8 ml
L00327 Glutathione MagBeads
8 ml
L00424 Streptavidin MagBeads
2 ml

Application Product Technology Binding capacity Size Cat.No.
Immunoprecipitation and micro-scale antibody purification Protein A MagBeads Protein/peptide capture through primary antibody >10 mg rabbit IgG/ml settled beads 4 ml L00273
Protein A MagBeads MX >30 mg human IgG /ml settled beads 4 ml L00672
Protein G MagBeads > 10 mg goat IgG/ml settled beads 2 ml L00274
Protein G MagBeads MX > 25 mg Human IgG per 1 ml settled beads 4 ml L00673
Protein A/G MagBeads > 10 mg goat IgG/ml settled beads 2 ml L00277
Micro-scale purification of His-tagged proteins Ni-charged MagBeads His-tagged protein capture through pre-charged nickel ion 5 - 20 mg 6×His-tagged protein (27kD)/ml settled beads 8 ml L00295
Micro-scale purification of GST fusion proteins Glutathione MagBeads GST fusion protein capture through reduced glutathione 20 - 30 mg GST/ml settled beads 8 ml L00327
Immunoprecipitation and purification of biotinylated molecules Streptavidin MagBeads Biotinylated molecule capture through pre-coupled streptavidin > 60 nmol free biotin /ml settled beads 2 ml L00424
* Each size includes 75% Storage Buffer.

  • Y Kuroda., et al. Improved capillary electrophoresis method for the analysis of carbohydrate-deficient transferrin in human serum, avoiding interference by complement C3. J Pharm Biomed Anal. 2013 Mar 25;76:81-6.
  • Hsieh YH., et al. Histone deacetylase inhibitor suberoylanilide hydroxamic acid suppresses the pro-oncogenic effects induced by hepatitis B virus pre-S2 mutant oncoprotein and represents a potential chemopreventive agent in high-risk chronic HBV patients. Carcinogenesis.. 2013 Feb;34(2):475-85.
  • Ferreira E., et al. Protein Interaction Studies Point To New Functions For Escherichia Coli Glyceraldehyde-3-Phosphate Dehydrogenase.Res Microbiol. 2013 Feb-Mar;164(2):145-54.
  • Tyler RE., et al. Unassembled CD147 is an endogenous endoplasmic reticulum-associated degradation substrate. Mol Biol Cell. 2012 Dec;23(24):4668-78.
  • Wiltrout E., et al. Misacylation Of Trna With Methionine In Saccharomyces Cerevisiae. Nucleic Acids Res. 2012 Nov 1;40(20):10494-506.
  • Priyanka Sivadas, et al. A Flagellar A-Kinase Anchoring Protein With Two Amphipathic Helices Forms A Structural Scaffold In The Radial Spoke Complex. J Cell Biol. 2012 Nov 12;199(4):639-51.
  • Dai C., et al.Loss Of Tumor Suppressor Nf1 Activates Hsf1 To Promote Carcinogenesis. J Clin Invest. 2012Oct 1;122(10):3742-54.
  • Leyme A., et al. Identification Of Ilk As A New Partner Of The Adam12 Disintegrin And Metalloprotease In Cell Adhesion And Survival. Mol Biol Cell. 2012 Sep;23(17):3461-72.
  • Dai MS., et al. Physical and functional interaction between ribosomal protein L11 and the tumor suppressor ARF.
    J Biol Chem. 2012 May 18;287(21):17120-9.
  • Tang X., et al. A High-Throughput Screening Method for Small-Molecule Inhibitors of the Aberrant Mutant SOD1 and Dynein Complex Interaction. J Biomol Screen. 2012 Mar;17(3):314-26.
  • An J., et al. CHCM1/CHCHD6, Novel Mitochondrial Protein Linked to Regulation of Mitofilin and Mitochondrial Cristae Morphology. J Biol Chem. 2012 Mar 2;287(10):7411-26.
  • Kazuhiro Ishiguro, et al. Cutting Edge: Tubulin α Functions as an Adaptor in NFAT-importin β Interaction. J Immunol. 2011Mar 1;186(5):2710-3.
  • Luo MH., et al. Human Cytomegalovirus Infection Causes Premature and Abnormal Differentiation of Human Neural Progenitor Cells. J Virol. 2010 Apr;84(7):3528-41.
  • Dongzhu Ma, et al.Rheb GTPase Controls Apoptosis by Regulating Interaction of FKBP38 with Bcl-2 and Bcl-XL. J Biol Chem. 2010 Mar 19;285(12):8621-7.
  • Crystal Morales, et al. Drosophila Glycoprotein 93 Is an Ortholog of Mammalian Heat Shock Protein gp96 (grp94, HSP90b1, HSPC4) and Retains Disulfide Bond-Independent Chaperone Function for TLRs and Integrins. J Immunol. 2009 Oct 15;183(8):5121-8.
  • Cross BC., et al. Dissecting the physiological role of selective transmembrane-segment retention at the ER translocon.
    J Cell Sci. 2009 Jun 1;122(Pt 11):1768-77.