94742
Vanadyl ribonucleoside complexes solution
BioReagent, Molecular Biology, 200 mM
Synonym(s):
Ribonucleoside vanadyl complexes
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About This Item
NACRES:
NA.52
UNSPSC Code:
12352200
Product Name
Vanadyl ribonucleoside complexes solution, BioReagent, Molecular Biology, 200 mM
grade
Molecular Biology
product line
BioReagent
form
liquid
concentration
200 mM
impurities
oxovanadium V
suitability
in accordance for ribonuclease inhibition test
shipped in
dry ice
storage temp.
−20°C
Quality Level
Application
Vanadyl ribonucleoside complexes (VDR) are transition state analogs that bind to active sites of many RNases, inhibiting their activity. Because the RNases are not covalently modified by the complexes, VDR must be used at every stage of RNA extraction and purification. However, VDR also inhibit RNA polymerases and in vitro translation and therefore must be removed from final preparation of RNA.
Vanadyl ribonucleoside complexes solution has been used:
- as a component of polysome lysis buffer and fluorescence in situ hybridization (FISH) buffer
- as a RNase inhibitor for the isolation of endogenous YTH domain-containing 2 protein (YTHDC2) from mouse testes
General description
Vanadyl ribonucleoside complexes are low molecular weight inhibitors of ribonucleases.
Vanadyl ribonucleoside complexes solution is an inhibitor for ribonuclease (RNase). Use of vanadyl ribonucleoside complexes exhibits protection from degradation by RNase in tissue, genomic, RNA and protein samples.
Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Wei Wang et al.
Nucleic acids research, 36(15), 4913-4928 (2008-07-26)
The mechanisms of influenza A virus mRNA intracellular transport are still not clearly understood. Here, we visualized the distribution and transport of influenza A virus mRNA in living cells using molecular beacon (MB) technology. Confocal-FRAP measurements determined that the transport
CARM1 and Paraspeckles Regulate Pre-implantation Mouse Embryo Development
Hupalowska A, et al.
Cell, 175(7), 1902-1916 (2018)
Immunoprecipitation of mRNA-protein complexes
Peritz T, et al.
Nature Protocols, 1(2), 577-577 (2006)
Regulation of m 6 A Transcripts by the 3?? 5? RNA Helicase YTHDC2 Is Essential for a Successful Meiotic Program in the Mammalian Germline
Wojtas MN, et al.
Molecular Cell, 68(2), 374-387 (2017)
Single-molecule Fluorescence in situ Hybridization (smFISH) for RNA Detection in Adherent Animal Cells
Haimovich G and Gerst JE
Proceedings of the National Academy of Sciences of the USA, 8(21) (2018)
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