Streptavidin beads
Streptavidin beads can immobilize biotin-labeled compounds and antibodies, DNA, etc. and can be used in a wide range of applications.
Since Streptavidin does not have sugar chains, there is no non-specific adsorption derived from sugar chains.
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 | TAS8848N1170 | TAB8848N3170 |
| 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 | 20mg/ml | |
| Functional groups | Streptavidin | |
| Binding ability | ≧ 3.0 ug Biotin labeled BSA / mg of beads | |
Fluorescent beads
Fluorescent beads contain fluorescent dyes, and there are FF beads with magnetic material and non-magnetic FS beads.
| Beads | FF beads （Magnetic type） |
FS beads （Non-magnetic type） |
||
|---|---|---|---|---|
| Code | Fluorescent dye | Europium | TAB8849N2170 | TAB5849N2170 |
| Cyanine 3 | TAB8850N2170 | TAB5850N2170 | ||
| Cyanine 5 | TAB8851N2170 | TAB5851N2170 | ||
| Price | Please contact us | |||
| Storage conditions | 2-8 ℃ (no freezing), protect from light | |||
| Storage buffer | 10 mM HEPES(pH7.9), 50 mM KCl, 1 mM EDTA, 10%glycerol | |||
| Magnetization | Superparamagnetism (≧10 emu/g) | No magnetization | ||
| Size of beads | 180±30 nm | 400±20 nm | ||
| Concentration | 10 mg/mL | |||
| Functional groups | Streptavidin | |||
| Binding ability | ≧ 2.0 ug Biotin labeled BSA / mg of beads | ≧ 1.0 ug Biotin labeled BSA / mg of beads | ||
- Protocol
- SDS
- Papers /
Technical Information - Related Products
- FAQ
- Screening by using ligand immobilized beads
- Competitive inhibition
- Drug elution
- Immobilization of biotinylated molecule on Streptavidin beads and NeutrAvidin beads
- Immunoprecipitation
- Direct Quantification of Immobilized Proteins (Antibodies)
- Preparation of cell extract (Large scale method)
- Preparation of cell extract (Small scale method)
SDS for FF Eu Streptavidin beads
SDS for FF Cyanine3 Streptavidin beads
SDS for FF Cyanine5 Streptavidin beads
SDS for FS Eu Streptavidin beads
Technical Information
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Cell separation
Learn More→ -
Isolation of drug target protein – Biotinylated MTX
Learn More→
Papers
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Histone deacetylation regulates nucleotide excision repair through an interaction with the XPC protein
iScience 25, 104040, April 15, 2022 -
Telomere-specific chromatin capture using a pyrrole–imidazole polyamide probe for the identification of proteins and non-coding RNAs
Epigenetics & Chromatin (2021) 14:46 -
Directed evolution of orthogonal RNA–RBP pairs through library-vs-library in vitro selection
Nucleic Acids Research, gkab527 (2021) -
Age-related dysfunction of p53-regulated phagocytic activity in macrophages
Biochemical and Biophysical Research Communications 529 (2020) 462 -
The SH3 domain in the fucosyltransferase FUT8 controls FUT8 activity and localization and is essential for core fucosylation
J. Biol. Chem. (2020) 295(23) 7992 -
Tag-Convertible Photocrosslinker with Click-On/Off N-Acylsulfonamide Linkage for Protein Identification
Chemistry—An Asian Journal Volume14, Issue18 September 16, 2019 Pages 3145-3148 -
Chemical Synthesis of Atomically Tailored SUMO E2 Conjugating Enzymes for the Formation of Covalently Linked SUMO–E2–E3 Ligase Ternary Complexes.
J. Am. Chem. Soc., 141, 37, 14742(2019) -
Wisteria floribunda agglutinin staining for the quantitative assessment of cardiac fibrogenic activity in a mouse model of dilated cardiomyopathy
Laboratory Investigation (2019) 99:1749–1765 -
Combinatorially Screened Peptide as Targeted Covalent Binder:Alteration of Bait-Conjugated Peptide to Reactive Modifier
Bioconjugate Chem., 29, 1866 (2018) -
Evaluation of protein-ligand interactions using the luminescent interaction assay FlimPIA with streptavidin-biotin linkage
Analytical Biochemistry 563 (2018) 61-66 -
Improved Liquid-Phase Detection of Biological Targets Based on Magnetic Markers and High-Critical-Temperature Superconducting Quantum Interference Device
IEICE TRANSACTIONS on Electronics Vol.E99-C No.6 pp.669-675 -
Generation of Immunity against Pathogens via Single-Domain Antibody–Antigen Constructs
J Immunol December 15, 2016, 197 (12) 4838-4847 -
Alteration of matrix metalloproteinase-3 O-glycan structure as a biomarker for disease activity of rheumatoid arthritis
Arthritis Research & Therapy, 18, 112 (2016). -
Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups
Nature Communications, 6:10216 (2015). -
A Peptide Derived from Tenascin-C Induces β1 Integrin Activation through Syndecan-4
J. Biol. Chem., 282, 34929 (2007).
- 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?
- What amount of the beads is required?
- What are the important points when designing a ligand?
- How are beads stored after the ligands are bound to them?
- Are there any methods other than HPLC for verifying whether or not ligand binding has been successful?
- How strong is the affinity for the proteins that are affinity purified?
- What is the purification efficiency?
- What is the optimal bead type for binding proteins?
- When binding proteins, what should be done if there is lysine residue at a location related to binding with the target substance?
- What is the efficiency when binding proteins?
- What is the optimal bead type for binding peptides?
- How is the cell extract prepared?
- Is there any problem with using frozen stock homogenate?
- How much protein supply is necessary?
- Can affinity purification be used with membrane proteins such as GPCRs and ion channels?
- 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?
- Why is it that both salt elution and boil elution are performed for elution?
- 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?
- Is the optimal binding reaction time of 4 hours?
- 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?
