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Citations & References (8)
Thermo Scientific™
Pierce™ Anti-HA Magnetic Beads
Perform immunoprecipitation of recombinant HA-tagged proteins expressed in bacterial or mammalian cells or in vitro systems, using manual or robotic magnetic separators.
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| Catalog Number | Quantity |
|---|---|
| 88836 | 1 mL |
| 88837 | 5 mL |
Catalog number 88836
Price (CNY)
2,148.00
Online Exclusive
Ends: 27-Dec-2025
3,460.00Save 1,312.00 (38%)
Each
Quantity:
1 mL
Price (CNY)
2,148.00
Online Exclusive
Ends: 27-Dec-2025
3,460.00Save 1,312.00 (38%)
Each
Thermo Scientific Pierce Anti-HA Magnetic Beads are affinity particles for immunoprecipitation of recombinant HA-tagged proteins expressed in bacterial or mammalian cells or in vitro systems, using manual or robotic magnetic separators.
Features of Anti-HA Magnetic Beads:
- Specific—highly specific anti-HA monoclonal antibody (clone 2-2.2.14) enables high yield and high purity immunoprecipitation
- Convenient and fast—product instructions provide an easy-to-follow, optimized protocol for immunoprecipitation in approximately one hour
- Low non-specific binding—stable, pre-blocked beads and specific antibody minimize off-target binding for HA-tag IP or co-IP experiments
- Versatile—beads are compatible with manual and automated workflows (e.g., Thermo Scientific KingFisher Instruments)
The blocked magnetic bead surface is coated with anti-HA antibody, a highly specific mouse IgG1 monoclonal antibody that recognizes the HA-epitope tag (YPYDVPDYA) derived from the human influenza hemagglutinin (HA) protein. The Pierce Anti-HA Magnetic Beads can be used manually with a magnetic stand, as well as with automated platforms, such as the Thermo Scientific KingFisher Instruments, for high-throughput workflows.
Specifications:
Product Details:
Pierce Anti-HA Magnetic Beads are convenient for the immunoprecipitation (IP) of recombinant HA-tagged proteins and the co-immunoprecipitation (co-IP) of their interacting proteins. The beads are incubated with a cell lysate containing HA-tagged protein and the fusion protein is captured. The beads are subsequently washed and then the target proteins are eluted using 0.1M glycine, pH 2.0, 50 mM NaOH, or SDS-PAGE sample buffer. If gentler elution conditions are desired, 2 mg/mL Pierce HA peptide can be used. The protocol has been optimized for each of these conditions. Anti-HA antibody can be used to detect HA-tagged protein by Western blot analysis.
For Research Use Only. Not for use in diagnostic procedures.
Thermo Scientific™ Pierce Anti-HA Magnetic Beads are convenient for the immunoprecipitation (IP) of recombinant HA–tagged proteins and the co–immunoprecipitation (co–IP) of their interacting proteins. The beads are incubated with a cell lysate containing HA–tagged protein and the fusion protein is captured. The beads are subsequently washed and then the target proteins are eluted using 0.1M glycine, pH 2.0, 50mM NaOH, or SDS–PAGE sample buffer. If gentler elution conditions are desired, 2mg/mL Pierce HA peptide can be used. The protocol has been optimized for each of these conditions. Anti-HA antibody can be used to detect HA–tagged protein by Western blot analysis.
Specifications
ConcentrationSlurry: 10mg/mL, 1% solids
Ligand TypeAntibody
Protein FormRecombinant
Quantity1 mL
TargetHA
Capacity (Metric)1 mL
FormLiquid
Particle Size1 μm
Product LinePierce
TypeMagnetic Affinity Bead
Unit SizeEach
Contents & Storage
Store at 4°C.
Frequently asked questions (FAQs)
Are the Pierce Anti-HA Magnetic Beads (Cat. No. 88836, 88837) compatible with sodium dodecyl sulfate? If yes, up to which concentration?
Citations & References (8)
Citations & References
Abstract
MT4-MMP promotes invadopodia formation and cell motility in FaDu head and neck cancer cells.
Journal:Biochemical and biophysical research communications
PubMed ID:31813546
Hypoxia-inducible factor-1α (HIF-1α) induces cancer metastasis. We previously demonstrated that HIF-1α-induced membrane-type 4 matrix metalloproteinase (MT4-MMP) is involved in hypoxia-mediated metastasis in head and neck squamous cell carcinoma (HNSCC). However, the functions and detailed mechanisms of MT4-MMP in cancer metastasis are not well understood. In this study, we investigated whether
A bead-based GPCR phosphorylation immunoassay for high-throughput ligand profiling and GRK inhibitor screening.
Journal:Communications biology
PubMed ID:36352263
Analysis of agonist-driven phosphorylation of G protein-coupled receptors (GPCRs) can provide valuable insights into the receptor activation state and ligand pharmacology. However, to date, assessment of GPCR phosphorylation using high-throughput applications has been challenging. We have developed and validated a bead-based immunoassay for the quantitative assessment of agonist-induced GPCR phosphorylation
Labeling and isolating cell specific neuronal mitochondria and their functional analysis in mice post stroke.
Journal:Experimental neurology
PubMed ID:39719208
Dendritic and axonal plasticity, which mediates neurobiological recovery after a stroke, critically depends on the mitochondrial function of neurons. To investigate, in vivo, neuronal mitochondrial function at the stroke recovery stage, we employed Mito-tag mice combined with cerebral cortical infection of AAV9 produced from plasmids carrying Cre-recombinase controlled by two
Bi-allelic LAMP3 variants in childhood interstitial lung disease: a surfactant-related disease.
Journal:EBioMedicine
PubMed ID:40023045
BACKGROUND: LAMP3 encodes a lysosomal membrane protein associated with lamellar bodies and has recently been proposed as a candidate gene for childhood interstitial lung diseases (chILD). Here, we identified two LAMP3 variants in a proband with chILD and performed functional validation of these variants as well as the previously reported
A novel interaction between RNA m(6)A methyltransferase METTL3 and RREB1.
Journal:Biochemical and biophysical research communications
PubMed ID:39278095
Regulation of gene expression is achieved through the modulation of regulatory inputs both pre- and post-transcriptionally. Methyltransferase-like 3 (METTL3) is a key player in pre-mRNA processing, actively catalyzing N6-methyladenosine (m6A). Among the most enriched mRNA targets of METTL3 is the Ras Responsive Element Binding Protein 1 (RREB1), a transcription factor