Protein A beads
Protein A beads can mainly immobilize antibodies (IgG) on beads by affinity purification.
It can be used for antibody purification and immunoprecipitation experiments using antigen-antibody reaction.
Protein A is a protein derived from the cell wall of Staphylococcus aureus (S. aureus).
Magnetic beads
The product lineup includes regular FG beads and highly magnetically responsive HM beads.
Beads | FG beads | HM beads (High Magnetic Response Type) |
---|---|---|
Code | TAS8848N1172 | TAB8848N3172 |
Price | Please contact us | |
Storage conditions | 2-8 ℃ (no freezing) | |
Storage buffer | 10 mM HEPES(pH7.9), 50 mM KCl, 1 mM EDTA, 10% glycerol |
10 mM HEPES(pH7.9) |
Magnetization | Superparamagnetism (≧10 emu/g) | Superparamagnetism (≧20 emu/g) |
Size of beads | 180±30 nm | 140±20 nm |
Concentration | 20 mg/ml | |
Functional groups | Protein A | |
Binding ability | ≧35 ug Human IgG/mg of beads |
Binding properties of Protein A and Protein G to IgG
※Please scroll horizontally.
Animal species | Human | Mouse | ||||||
---|---|---|---|---|---|---|---|---|
Subclass | IgG1 | IgG2 | IgG3 | IgG4 | IgG1 | IgG2a | IgG2b | IgG3 |
Protein A | ◎ | ◎ | △ | ◎ | △ | ◎ | ◎ | ◎ |
Protein G | ◎ | ◎ | ◎ | ◎ | ◎ | ◎ | ◎ | ◎ |
Animal species | Rat | Bovine | Chicken | Rabbit | Horse | |||||
---|---|---|---|---|---|---|---|---|---|---|
Subclass | IgG1 | IgG2a | IgG2b | IgG2c | IgG1 | IgG2 | IgG | IgY | IgG | IgG |
Protein A | 〇 | × | × | ◎ | × | ◎ | × | × | ◎ | △ |
Protein G | 〇 | ◎ | 〇 | ◎ | ◎ | ◎ | × | × | ◎ | ◎ |
Animal species | Goat | Guinea pig | Dog | Cat | Hamster | Sheep | Pig | ||
---|---|---|---|---|---|---|---|---|---|
Subclass | IgG1 | IgG2 | IgG | IgG | IgG | IgG | IgG1 | IgG2 | IgG |
Protein A | × | ◎ | ◎ | ◎ | ◎ | △ | × | ◎ | ◎ |
Protein G | ◎ | ◎ | 〇 | ◎ | 〇 | – | ◎ | ◎ | ◎ |
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Technical Information - Related Products
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Technical Information
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Immunoprecipitation(1)
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Immunoprecipitation(2)
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Immunoprecipitation (3)
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Immunoprecipitation (4)
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Chromatin immunoprecipitation 1
unichi Yamamoto, Tokyo Medical University
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Chromatin immunoprecipitation 2
obuo Horikoshi, Houston Methodist Research Institute Weill Cornell Medical College
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papers
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Tumor Suppressive Role of the PRELP Gene in Ovarian Clear Cell Carcinoma
J. Pers. Med. 2022, 12(12), 1999; https://doi.org/10.3390/jpm12121999 -
An oncogenic splice variant of PDGFRα in adult glioblastoma as a therapeutic target for selective CDK4/6 inhibitors
Scientifc Reports (2022) 12:1275 -
α1,4- Linked N- acetylglucosamine suppresses gastric cancer development by inhibiting Mucin-1-mediated signaling.
Cancer Science. 2022;00:1–12 -
Stabilization of CDK6 by ribosomal protein uS7, a target protein of the natural product fucoxanthinol
COMMUNICATIONS BIOLOGY (2022) 5:564 -
Downregulation of METTL6 mitigates cell progression, migration, invasion and adhesion in hepatocellular carcinoma by inhibiting cell adhesion molecules
INTERNATIONAL JOURNAL OF ONCOLOGY 60: 4, 2022 -
Identification of the mutation signature of the cancer genome caused by irradiation
Radiotherapy and Oncology 155 (2021) 10 -
Exploiting ubiquitin ligase cereblon as a target for small-molecule compounds in medicine and chemical biology
Cell Chemical Biology 28, July 15, 2021 -
N-glycosylation of Rim21 at an unconventional site fine-tunes its behavior in the plasma membrane
Cell Structure and Function 2020, https://doi.org/10.1247/csf.19021 -
Artificial switching of the metabolic processing pathway of an etiologic factor, β2-microglobulin, by a “navigator” molecule
Journal of Controlled Release 327 (2020) 8–18 -
Mismatch repair dependence of replication stress-associated DSB recognition and repair
Heliyon 5 (2019) e03057 -
ISGF3 with reduced phosphorylation is associated with constitutive expression of interferon-induced genes in aging cells
npj Aging and Mechanisms of Disease (2018)4:11 -
A Novel Autoantibody against Plexin D1 in Patients with Neuropathic Pain
Ann. Neurol., 84, 200 (2018). -
Transport Granules Bound with Nuclear Cap Binding Protein and Exon Junction Complex Are Associated with Microtubules and Spatially Separated from eIF4E Granules and P Bodies in Human Neuronal Processes
Front. Mol. Biosci. 4:93. doi: 10.3389/fmolb.2017.00093 -
A proteomics method using immunoaffinity fluorogenic derivatization-liquid chromatography/tandem mass spectrometry (FD‐LC‐MS/MS) to identify a set of interacting proteins.
Biomedical Chromatography, DOI: 10.1002/bmc.4063 (2017). -
Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3
Genes to Cells (2017) 22, 310–327 -
TLR7 mediated viral recognition results in focal type I interferon secretion by dendritic cells
NATURE COMMUNICATIONS 8: 1592 -
N-Myristoylation of the Rpt2 subunit of the yeast 26S proteasome is implicated in the subcellular compartment?specific protein quality control system
Journal of Proteomics, 130, 33 (2016) -
Development of an efficient entire-capsid-coding-region amplification method for direct detection of poliovirus from stool extracts
J. Clin. Microbiol., 53, 73 (2015). -
Opt2 mediates the exposure of phospholipids during cellular adaptation to altered lipid asymmetry
J Cell Sci (2015) 128 (1): 61–69. -
Identification of the Specific Interactors of the Human Lariat RNA Debranching Enzyme 1 Protein
Int. J. Mol. Sci., 16, 3705 (2015). -
DNA Methylation Restricts Lineage-specific Functions of Transcription Factor Gata4 during Embryonic Stem Cell Differentiation
PLOS Genetics, 9, e1003574 (2013). -
Development of poliovirus extraction method from the stool extracts by using magnetic nanoparticles sensitized with soluble poliovirus receptor.
J. Clin. Microbiol. DOI:10.1128 (2013).
- Please tell me how to separate FG beads (magnetic separation and centrifugation).
- Please tell me how to disperse FG beads (ultrasonic method and manual method).
- I mistakenly frozen some beads that were supposed to be stored in the refrigerator. Is it available?
- How is the cell extract prepared?
- Is there any problem with using frozen stock homogenate?
- How much protein supply is necessary?
- There are many background bands. how can i reduce it?
- What should be done when a large number of bound protein bands are detected?
- Is it necessary to use the recommended buffer as the binding buffer?
- Does it happen that the band of bound protein becomes thin when the concentration of ligand is increased?
- Why can’t I see any bands of bound proteins?
- How long is the stable period of the ligand-immobilized beads?
- What is the optimal bead type for immobiliding antibodies?
- Can I quantify the immobilization amount of the antibodies on the beads?
- What is the efficiency when immobiliding antibodies?
- Is there a way to increase the antibody immobilization efficiency (immobilization amount)?
- Can I disperse antibody-immobilized beads by ultrasonic device?
- When immobilizing antibodies to beads, the beads may adhere to the wall of the tube. Is there a way to suppress this?
- How can I improve dispersibility of antibodies immobilized beads?
- I want to analyze bound proteins with MS, but what should I do if the target protein band is thin?
- How much protein can be analyzed by MS?