5-Ethynyl-2'-deoxyuridine (5-EdU)
For research use only.
Description:
5-EdU (5-Ethynyl-2'-deoxyuridine) can be used as a replacement for BrdU (5-Bromo-2'-deoxyuridine) to measure de novo DNA synthesis during the S-phase of the cell cycle. 5-EdU is cell permeable and incorporates into replicating DNA instead of its natural analog thymidine. The resulting ethynyl-functionalized DNA can subsequently be detected via Cu(I)-catalyzed click chemistry that offers the choice to introduce a Biotin group (via Azides of Biotin) for subsequent purification tasks or a fluorescent group (via Azides of fluorescent dyes) for subsequent microscopic imaging [1-5].
Presolski et al.[6] and Hong et al.[7] provide a general protocol for Cu(I)-catalyzed click chemistry reactions that may be used as a starting point for the set up and optimization of individual assays.
Shipping: shipped at ambient temperature
Storage Conditions: store at -20 °C
store dry and under inert gas
Short term exposure (up to 1 week cumulative) to ambient temperature possible.
Shelf Life: 12 months after date of delivery
Molecular Formula: C11H12N2O5
Molecular Weight: 252.23 g/mol
Exact Mass: 252.07 g/mol
CAS#: 61135-33-9
Purity: ≥ 98 % (HPLC)
Form: solid
Color: white to off-white
Solubility: DMSO, up to 200 mM (at room temperature) in 1 x PBS or water by heating the obtained suspension for 1 minute by 70 °C
Spectroscopic Properties: λmax 288 nm, ε 12.0 L mmol-1 cm-1 (Tris-HCl pH 7.5)
Applications:
DNA synthesis monitoring[1-5]
Related products:
- 5-Ethynyl-deoxycytidine (5-EdC), #CLK-N003
- Copper (II)-Sulphate (CuSO4), #CLK-MI004
- Tris(3-hydroxypropyltriazolylmethyl)amine (THPTA), #CLK-1010
- Sodium Ascorbate (Na-Ascorbate), #CLK-MI005
Selected References:
[1] Salic et al. (2008) A chemical method for fast and sensitive detection of DNA synthesis in vivo. Proc. Natl. Acad. Sci. USA 105 (7):2415.
[2] Li et al. (2010) Fluorogenic click reaction for labeling and detection of DNA in proliferating cells. Biotechniques 49 (1):525.
[3] Chehrehasa et al. (2009) EdU, a new thymidine analogue for labelling proliferating cells in the nervous system. J. Neurosci. Methods 177:122.
[4] Limsirichaikul et al. (2009) A rapid non-radioactive technique for measurement of repair synthesis in primary human fibroblasts by incorporation of ethynyl deoxyuridine (EdU). Nucleic Acids Res. 37 (4):e31.
[5] Buck et al. (2008) Detection of S-phase cell cycle progression using 5-ethynyl-2'-deoxyuridine incorporation with click chemistry, an alternative to using 5-bromo-2'-deoxyuridine antibodies. Biotechniques 44 (7):927.
[6] Presolski et al. (2011) Copper-Catalyzed Azide-Alkyne Click Chemistry for Bioconjugation. Current Protocols in Chemical Biology 3:153.
[7] Hong et al. (2011) Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation. Angew. Chem. Int. Ed. 48:9879.
| Cat. No. | Amount | Price |
|---|---|---|
| CLK-N001-25 | 25 mg | 70,40 € |
| CLK-N001-100 | 100 mg | 204,40 € |
| CLK-N001-500 | 500 mg | 648,70 € |
| CLK-N001-5000 | 5 g | 3.405,40 € |
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Scientific citations for Jena Bioscience clk-n001
66 scientific citations and 6 citation images found by Bioz.
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TRRAP enables MMB-dependent mitotic transcription and determines sensitivity to CHK1 inhibition.
Cell Reports, 2026-09-11 · PMID:42731029
.. ..Cat# I9278 Recombinant human EGF Sigma-Aldrich Cat# E9644
5-Ethynyl-2′-deoxyuridine (EdU)Jena Bioscience Cat#CLK-N001 RO-3306 (CDK1 inhibitor) Sigma-Aldrich Cat#.. .. -
High-resolution single-molecule replication profiling of the human genome
bioRxiv, 2026-07-20 · DOI:10.64898/2026.07.15.738623
PrePrint: Exponentially growing, untreated cells or cells pulse-labelled 24 times with BrdU or PBS as described above were incubated with 10 μM
5-ethynyl-2’-deoxyuridine (EdU,Jena Bioscience #CLK-N001 -100) for 1 h and fixed in ethanol.. Fixed cells were pelleted, incubated in PBS-0.2% Triton X-100 for 20 min at room .. -
Identification of ribosomal protein eL21 as a novel externalized protein and a target in triple-negative breast cancer.
Cancer gene therapy, 2026-07-01 · PMID:41957522
Abstract: Proteins normally localized in the intracellular compartments of healthy cells have been observed at the surface of cancer cells, despite lacking a transmembrane domain or secretion signals. This unexpected localization likely reflects yet-unknown functions and presents a unique opportunity to develop cancer cell-specific antibody- or peptide-based therapeutic strategies. While ribosomal proteins (RPs) are primarily involved in translation, several display moonlighting functions in the cytoplasm and nucleus
