Plain beads
Plain beads are a type of beads that do not have a linker (spacer).
DNA and RNA are directly immobilized on the epoxy group on the surface and used for purification of transcription factors and complementary DNA and RNA.
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Magnetic beads
The lineup of this product is only regular FG beads.
Beads | FG beads |
---|---|
Code | TAS8848N1010 |
Price | Please contact us |
Storage conditions | 2-8 ℃ (no freezing), protect from light |
Storage buffer | Ultrapure water |
Magnetization | Superparamagnetism (≧10 emu/g) |
Size of beads | 180±30 nm |
Concentration | 20 mg/ml |
Functional groups | Epoxy groups |
Amounts of the functional groups | Approx. 1 μmol/mg of beads |
- Protocol
- SDS
- Papers /
Technical Information - Related Products
- FAQ
Technical Information
Papers
-
Itpr1 regulates the formation of anterior eye segment tissues derived from neural crest cells
Development (2021) 148 (16): dev188755 -
Design and Trial Production of Magnetic Filter for Medical Protein Screening System using High Gradient Magnetic Separation
Journal of Physics: Conf. Series 1293 (2019) 012081 -
Comparative analysis of type 2 diabetes-associated SNP alleles identifies allele-specific DNA-binding proteins for the KCNQ1 locus
Int J Mol Med. 2015 Jul;36(1):222-30. -
M. Golan-Mashiach et al. (2012)
Identification of CTCF as a master regulator of the clustered protocadherin genes
Nucl. Acids Res., 40, 3378 (2012). -
A general mechanism for transcription regulation by Oct1 and Oct4 in response to genotoxic and oxidative stress
Genes Dev., 23, 208 (2009). -
Embryonic Lethality, Decreased Erythropoiesis, and Defective Octamer-Dependent Promoter Activation in Oct-1-Deficient Mice
Mol. Cell. Biol., 24, 1022 (2004). -
Regulation of Immunoglobulin Promoter Activity by TFII-I Class Transcription Factors
J. Biol. Chem., 279, 5460 (2004). -
Total Analysis and Purification of Cellular Proteins Binding to Cisplatin-Damaged DNA Using Submicron Beads
Bioconjugate Chem., 13, 163 (2002). -
Selective isolation of DNA or RNA using single-stranded DNA affinity latex particles
J. Colloid Interface Sci., 177, 245 (1996). -
Copurification of casein kinase II with transcription factor ATF/E4TF3
Nucleic Acids Res., 24, 876 (1996). -
[40] DNA affinity chromatography
Methods in Enzymology, 254, 595 (1995). -
Application of cationic latex particles for protein separation
Coll. Surf. B., 2, 419 (1994). -
Preparation of DNA-carrying affinity latex and purification of transcription factors with the latex
J. Biomater. Sci. Polym. Ed., 5, 293 (1994). -
Direct purification of multiple ATF/E4TF3 polypeptides from HeLa cell crude nuclear extracts using DNA affinity latex particles
Anal. Biochem., 206, 109 (1992). -
A Common trans-Acting Factor, Ad4-binding Protein, to the Promoters of Steroidogenic P-450s
J. Biol. Chem., 267, 17913 (1992). -
Purification of DNA-binding transcription factors by their selective adsorption on the affinity latex particles
Nucleic Acids Res., 17, 6229 (1989).
- 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?
- 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 binding DNA?
- What method is used to bind RNA?
- 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?