R3380
Ribonucleoside vanadyl complexes
liquid
Synonym(s):
vanadyl ribonucleoside complexes
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.52
Product Name
Ribonucleoside vanadyl complexes, 200 mM
biological source
non-animal source
form
liquid
concentration
200 mM
solubility
H2O: soluble
shipped in
dry ice
storage temp.
−20°C
Quality Level
Related Categories
Application
Ribonucleoside vanadyl complexes are used as ribonuclease inhibitors during cell lysis and mRNA purification, to protect mRNA during cDNA production, and to protect RNA during digestion of DNA by DNaseI.
Ribonucleoside vanadyl complexes has been used:
- as a component of lysis buffer for cell lines prior to Poly(U) pull down assay
- to inhibit nucleases prior to immunoprecipitation (IP) of m6A-containing RNA fragment
- as a component of hybridization buffer for human retinal slices
Biochem/physiol Actions
Ribonucleoside vanadyl complexes (RVC) elicits antimicrobial functionality by inhibiting ribosomal subunit formation and suppressing the growth of Staphylococcus aureus and Escherichia coli. It is also used as a preservative solution for tissues.
General description
Ribonucleoside vanadyl complexes are stable complexes formed between ribonucleotides. They are low molecular weight inhibitors of cellular ribonucleases (RNases) that are used for the isolation of RNA from cells.
hcodes
pcodes
Hazard Classifications
Aquatic Chronic 3
Storage Class
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
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Transcriptome-wide mapping of N6-methyladenosine by m6A-Seq
Dominissini D, et al.
Test, 560, 131-147 (2015)
SIRT1 functions as a negative regulator of eukaryotic poly (A) RNA transport
Shan P, et al.
Current Biology, 27(15), 2271-2284 (2017)
Neuroinflammatory processes, A1 astrocyte activation, and protein aggregation in the retina of Alzheimer's Disease patients, possible biomarkers for early diagnosis.
Grimaldi A, et al.
Frontiers in Neuroscience, 13, 925-925 (2019)
DNA damage induces p21 protein expression by inhibiting ubiquitination in ML-1 cells.
Fukuchi K
Biochimica et Biophysica Acta, 1404(3), 405-411 (1998)
Hyone-Myong Eun
Enzymology Primer for Recombinant DNA Technology (1996)
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