3′-Azido-2′,3′-ddTTP
Triphosphate for modifying of 3'END RNA or ssDNA
| Size | Catalog No. | Price |
|---|---|---|
| 1 µmol | BCT-28-S | € 250,00 |
| 5 µmol | BCT-28-L | € 850,00 |
Chemical Properties
-
Molecular Formula
C10H16N5O13P3
-
Shelf Life
12 months unopened after receipt
-
Storage Conditions
-20 °C
-
Molecular Weight
507.18 g/mol
-
Purity
≥ 95% (HPLC)
-
Physical State
100 mM clear aquaeous solution; colorless
-
CAS Number
149022-21-9 (sodium salt)
92586-35-1 (free acid)
-
Absorption (max)
λmax = 267 nm
-
Ɛ (max)
10,900 cm-1M-1
-
Additional name
3′-Azido-ddTTP, AZTTP, AZT-TP, Zidovudine
Triphosphate, Azidothymidine Triphosphate
Product Information
Azide modified nucleotide closely resemble natural nucleotides and are the basis of chemoenzymatic mRNA labeling. Due to the small size of the azide group, 3′-Azido-2′,3′-ddTTP is well accepted by T7 RNA polymerase and poly(A) polymerase and terminale deoxynucleotidyl transferase (Tdt) for enzymatic incorporation. This is highly beneficial, as labeling of mRNA with our approach is modular and not limited to enzymatic compatibility of bulky pre-labeled nucleotides. Moreover, only a very limited number of such pre-modified nucleotides, mainly dye-labeled ones, are commercially available. Internal and external studies successfully showed e.g. that the poly(A) polymerase adds specifically and sequence independently single azido terminator to the 3’-end of RNA.
The main advantage: Any mRNA can be site-specifically labeled without special requirements or altered production protocols at the 3’-end.
LITERATURE
Site-specific terminal and internal labeling of RNA by poly(A) polymerase tailing and copper-catalyzed or copper-free strain-promoted click chemistry, M. L. Winz et al., 2012, Nucleic Acids Res., Vol. 40, p. 1–13.
https://doi.org/10.1093/nar/gks062
Chemoenzymatic Preparation of Functional Click-Labeled Messenger RNA, S. Croce et al., 2020, ChemBioChem, Vol. 21, p. 1641-1646.
https://doi.org/10.1002/cbic.201900718
Application and design considerations for 3′-end sequencing using click-chemistry, M. K. Jensen et al., 2021, Methods in Enzymology, Vol. 655, p. 1-23.