D3126
2-Deoxyribose 5-phosphate sodium salt
≥95% (ICP-AES)
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About This Item
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biological source
synthetic (inorganic)
Quality Level
assay
≥95% (ICP-AES)
form
powder
color
white to off-white
solubility
H2O: 100 mg/mL, clear, colorless to very faintly yellow
cation traces
Na: 14.0-19.0% (dry basis)
storage temp.
−20°C
SMILES string
[Na].OC(COP(O)(O)=O)C(O)CC=O
InChI
1S/C5H11O7P.Na.H/c6-2-1-4(7)5(8)3-12-13(9,10)11;;/h2,4-5,7-8H,1,3H2,(H2,9,10,11);;
InChI key
VKWGIGKPYXQSGV-UHFFFAOYSA-N
Application
2-Deoxyribose 5-phosphate is used as a substrate to identify, differentiate and characterize deoxyribose-phosphate aldolase(s). It is used for the synthesis of 2′-deoxyribonucleoside building blocks for the synthesis of antisense drugs and antiviral nucleosides.
Other Notes
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Faceshields, Gloves, type N95 (US)
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Journal of industrial microbiology & biotechnology, 40(1), 29-39 (2012-11-28)
A codon-optimized 2-deoxyribose-5-phosphate aldolase (DERA) gene was newly synthesized and expressed in Escherichia coli to investigate its biochemical properties and applications in synthesis of statin intermediates. The expressed DERA was purified and characterized using 2-deoxyribose-5-phosphate as the substrate. The specific
Bioprocess and biosystems engineering, 35(5), 857-863 (2012-02-10)
To improve the properties of the immobilised 2-deoxy-D-ribose-5-phosphate aldolase (DERA), unreacted functional groups on support surface were blocked with amino acids. The relative activities of the immobilised enzyme were 144.7 and 141.9% when the post-immobilisation modification was done with Arg
Protein expression and purification, 68(2), 196-200 (2009-06-10)
A new deoC gene encoding deoxyribose 5-phosphate aldolase (DERA) was identified in Yersinia sp. EA015 isolated from soil. The DERA gene had an open reading frame (ORF) of 672 base pairs encoding 223 amino acids to yield a protein of
Applied microbiology and biotechnology, 104(24), 10515-10529 (2020-11-05)
In this work, deoxyribose-5-phosphate aldolase (Ec DERA, EC 4.1.2.4) from Escherichia coli was chosen as the protein engineering target for improving the substrate preference towards smaller, non-phosphorylated aldehyde donor substrates, in particular towards acetaldehyde. The initial broad set of mutations
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