Recommended Products
biological source
synthetic
Quality Level
reg. compliance
FDA 21 CFR 117
Assay
≥98%
optical activity
[α]21/D −19.7°, c = 4 in H2O
mp
88-92 °C (lit.)
application(s)
flavors and fragrances
Documentation
see Safety & Documentation for available documents
food allergen
no known allergens
Organoleptic
odorless
SMILES string
OC[C@@H](O)[C@@H](O)[C@@H](O)C([H])=O
InChI
1S/C5H10O5/c6-1-3(8)5(10)4(9)2-7/h1,3-5,7-10H,2H2/t3-,4+,5-/m0/s1
InChI key
PYMYPHUHKUWMLA-LMVFSUKVSA-N
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General description
D-(−)-Ribose has been in an in vitro study of the effect of non-enzymatic ribation in modifying bone collagen leading to bone fragility.
Application
- Protective effect of thymoquinone on glycation of human myoglobin induced by d-ribose.: This study investigates the protective effects of thymoquinone against d-ribose-induced glycation in human myoglobin, highlighting potential therapeutic applications in preventing protein glycation (Liu et al., 2023).
Disclaimer
For R&D or non-EU Food use. Not for retail sale.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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A series of peracetylated O-aryl α,β-d-ribofuranosides have been synthesized and an efficient biocatalytic methodology has been developed for the separation of their anomers which was otherwise almost impossible by column chromatographic or other techniques. The incubation of 2,3,5-tri-O-acetyl-1-O-aryl-α,β-d-ribofuranoside with Lipozyme®
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Non-enzymatic glycation (NEG) and advanced glycation endproducts (AGEs) may contribute to bone fragility in various diseases, ageing, and other conditions by modifying bone collagen and causing degraded mechanical properties. In this study, we sought to further understand how collagen modification
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Poly-ADP-ribose metabolism plays a mayor role in a wide range of biological processes, such as maintenance of genomic stability, transcriptional regulation, energy metabolism and cell death. Poly-ADP-ribose polymerases (PARPs) are an ancient family of enzymes, as evidenced by the poly-ADP-ribosylating
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