Pierce™ Protein A/G Magnetic Beads
Pierce™ Protein A/G Magnetic Beads
Thermo Scientific™

Pierce™ Protein A/G Magnetic Beads

Immunoprecipitate or affinity purify antibodies (IgG) using Protein A/G coated magnetic particles for manual or robotic magnetic separation.
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Catalog NumberQuantity
888021 mL
888035 mL
Catalog number 88802
Price (EUR)
240,65
Online Exclusive
268,00
Save 27,35 (10%)
Each
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Quantity:
1 mL
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Price (EUR)
240,65
Online Exclusive
268,00
Save 27,35 (10%)
Each
Add to cart
Ask our AI about this Product

Thermo Scientific Pierce Protein A/G Magnetic Beads are high-performance affinity particles for antibody purification and immunoprecipitation methods using manual or robotic magnetic separators.

Features of Protein A/G Magnetic Beads:

  • High capacity—nearly four times higher binding capacity than typical magnetic beads from other suppliers, allowing the use of smaller amounts per experiment
  • Low non-specific binding—stable, pre-blocked beads provide clean purification products (e.g., antigen eluted in IP with antibody is devoid of contaminating proteins from complex IP matrix)
  • Flexibility—convenience of IgG binding domains of both Protein A and Protein G on one bead
  • Compatibility—beads are compatible with manual and automated applications (e.g., Thermo Scientific KingFisher Instruments)
  • Assay consistency—magnetic beads eliminate resin loss and provide for more efficient separation of solutions than traditional IP methods that use only microcentrifuge tubes

These magnetic beads are coated with genetically engineered Pierce Protein A/G, a recombinant fusion protein which combines the IgG binding domains of both Protein A and Protein G. This enables capture of antibodies from a wider range of species and isotypes than either protein alone. Using our crosslinker chemistry, you can immobilize an antibody onto the magnetic particle and prevent IgG contamination in your immunoprecipitated sample. These beads can be used both manually with a magnetic stand as well as with automated platforms such as the Thermo Scientific KingFisher Instruments.

Applications:

  • IP and Co-IP experiments (see complete kit)
  • Immunoprecipitation for analysis in non-reducing conditions
  • Antibody purification

The recombinant Protein A/G that is immobilized onto the Pierce Magnetic Beads is a fusion of the IgG binding domains of both Protein A and Protein G. Protein A/G contains four Fc-binding domains from Protein A and two from Protein G, making it a convenient tool for investigating and purifying immunoglobulins. Thus, Pierce Magnetic Particles are not simply a mixed immobilization of separate Protein A and Protein G polypeptides, nor are they a mixture of Protein A magnetic beads and Protein G magnetic beads.

For Research Use Only. Not for use in diagnostic procedures.
Specifications
ConcentrationSlurry: 10mg/mL, 1% solids
Ligand TypeProtein A/G
Protein FormRecombinant
Quantity1 mL
TargetAntibody
Capacity (Metric)1 mL
FormLiquid
Particle Size1 μm
Product LinePierce™
TypeMagnetic Affinity Bead
Unit SizeEach
Contents & Storage
Upon receipt store at 4°C. Product shipped with an ice pack.
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Certificates

Lot #Certificate TypeDateCatalog Number(s)
AB407884Certificate of AnalysisJun 17, 202588802
ZL403214Certificate of AnalysisJun 17, 202588802TS, 88802
3216868Certificate of AnalysisJun 17, 202588802
3215640Certificate of AnalysisJun 03, 202588803
3212675Certificate of AnalysisJun 02, 202588802
5 results displayed, search above for a specific certificate

Safety Data Sheets

Frequently asked questions (FAQs)

Pierce Protein A/G Magnetic Beads are intended for single use only. Therefore, we do not recommend reusing them.

Pierce Magentic Agarose Beads have a much higher binding capacity.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

No, centrifuging causes the formation of irreversible aggregates which greatly reduces binding capacity.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Adding 50-350 mM of NaCl to the Binding/Wash and Elution Buffers can help reduce non-specific bands. Also, use a low-pH elution for single-use applications. The optimal time for low-pH elution is 10 minutes; exceeding 10 minutes may result in non-specific binding and yield reduction.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Avoid bead-boil elutions when using rabbit antibodies (primary or secondary) in downstream Western blot applications. Instead, perform elution in SDS-PAGE sample buffer at room temperature. For all other antibody species, boiling the beads in SDS-PAGE sample buffer is acceptable for single-use applications. Boiling could cause bead aggregation and loss of binding activity.

Find additional tips, troubleshooting help, and resources within our Protein Assays and Analysis Support Center.

Citations & References (11)

Citations & References
Abstract
The Thyroid Hormone Analog GC-1 Mitigates Acute Lung Injury by Inhibiting M1 Macrophage Polarization.
Authors:Li B,Xia C,He W,Liu J,Duan R,Ji Z,Pan X,Zhou Y,Yu G,Wang L
Journal:Advanced science (Weinheim, Baden-Wurttemberg, Germany)
PubMed ID:39373388
Acute lung injury (ALI)/acute respiratory distress syndrome (ARDS) is a life-threatening condition with a high mortality rate of ≈40%. Thyroid hormones (THs) play crucial roles in maintaining homeostasis of the cellular microenvironment under stress. The previous studies confirmed that the clinical-stage TH analog GC-1 significantly alleviates pulmonary fibrosis by improving ... More
E3 ubiquitination ligase XIAP lightens diabetes-induced cognitive impairment by inactivating TXNIP-ERS-mediated neuronal injury.
Authors:Zhang Q,Huang HJ,Zhang JL,Tian Y,Hu Y
Journal:The Kaohsiung journal of medical sciences
PubMed ID:39629879
Diabetes-induced cognitive dysfunction (DCD) is a neurological disorder associated with diabetes, characterized by cognitive impairment driven by neuronal injury from chronic high glucose (HG) exposure. This study aims to elucidate the role and mechanisms of the X-linked inhibitor of apoptosis protein (XIAP)/thioredoxin-interacting protein (TXNIP) in hippocampal neuron cell death and ... More
Interplay Between Phosphorylation and O-GlcNAcylation of Sarcomeric Proteins in Ischemic Heart Failure.
Authors:Mercier T,Bouvet M,Dubois-Deruy E,Dechaumes A,Beseme O,Richard V,Mulder P,Pinet F
Journal:Frontiers in endocrinology
PubMed ID:30344511
Post-translational modifications (PTMs) of sarcomeric proteins could participate to left ventricular (LV) remodeling and contractile dysfunction leading in advanced heart failure (HF) with altered ejection fraction. Using an experimental rat model of HF (ligation of left coronary artery) and phosphoproteomic analysis, we identified an increase of desmin phosphorylation and a ... More
Extracellular matrix stiffness regulates degradation of MST2 via SCF (βTrCP).
Authors:Fiore APZP,Rodrigues AM,Ribeiro-Filho HV,Manucci AC,de Freitas Ribeiro P,Botelho MCS,Vogel C,Lopes-de-Oliveira PS,Pagano M,Bruni-Cardoso A
Journal:Biochimica et biophysica acta. General subjects
PubMed ID:36044955
The Hippo pathway plays central roles in relaying mechanical signals during development and tumorigenesis, but how the proteostasis of the Hippo kinase MST2 is regulated remains unknown. Here, we found that chemical inhibition of proteasomal proteolysis resulted in increased levels of MST2 in human breast epithelial cells. MST2 binds SCF(βTrCP) ... More
Interaction of cochlin and mechanosensitive channel TREK-1 in trabecular meshwork cells influences the regulation of intraocular pressure.
Authors:Carreon TA,Castellanos A,Gasull X,Bhattacharya SK
Journal:Scientific reports
PubMed ID:28352076
In the eye, intraocular pressure (IOP) is tightly regulated and its persistent increase leads to ocular hypertension and glaucoma. We have previously shown that trabecular meshwork (TM) cells might detect aqueous humor fluid shear stress via interaction of the extracellular matrix (ECM) protein cochlin with the cell surface bound and ... More
11 total citations

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