R0630000

Riboflavin sodium phosphate

Name: Riboflavin sodium phosphate
Brand: SIAL

European Pharmacopoeia (EP) Reference Standard

Synonym(s):

Riboflavin 5′-monophosphate sodium salt, Riboflavin Sodium phosphate

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About This Item

Empirical Formula (Hill Notation):

C₁₇H₂₀N₄NaO₉P

CAS Number:

130-40-5

Molecular Weight:

478.33

UNSPSC Code:

41116107

NACRES:

NA.24

PubChem Substance ID:

329823989

EC Number:

204-988-6

Beilstein/REAXYS Number:

4106529

MDL number:

MFCD00065362

Key Documents

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InChI

1S/C17H21N4O9P.Na/c1-7-3-9-10(4-8(7)2)21(15-13(18-9)16(25)20-17(26)19-15)5-11(22)14(24)12(23)6-30-31(27,28)29;/h3-4,11-12,14,22-24H,5-6H2,1-2H3,(H,20,25,26)(H2,27,28,29);/q;+1/p-1/t11-,12+,14-;/m0./s1

SMILES string

[Na+].Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)COP(O)([O-])=O)c2cc1C

InChI key

OHSHFZJLPYLRIP-BMZHGHOISA-M

biological source

synthetic

grade

pharmaceutical primary standard

agency

API family

riboflavin

form

solid

manufacturer/tradename

EDQM

technique(s)

gas chromatography (GC): suitable, liquid chromatography (LC): suitable

application(s)

pharmaceutical (small molecule)

format

neat

storage temp.

2-8°C

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Related Categories

Analytical Chemistry

Analytical Reference Materials for Pharma QC

Pharmacopeia & Metrological Institute Standards

Phosphates

Reference Materials

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Show Differences

1 of 4

This Item	BP459	Y0002362	77623
R0630000 Riboflavin sodium phosphate	BP459 Riboflavin sodium phosphate	Supelco Y0002362 Riboflavin sodium phosphate for peak identification	Sigma-Aldrich 77623 Riboflavin Sodium Phosphate Hydrate
application(s) pharmaceutical (small molecule)	application(s) pharmaceutical (small molecule)	application(s) pharmaceutical	application(s) pharmaceutical (small molecule)
technique(s) gas chromatography (GC): suitable, liquid chromatography (LC): suitable	technique(s) gas chromatography (GC): suitable, liquid chromatography (LC): suitable	technique(s) -	technique(s) -
form solid	form solid	form -	form powder
grade pharmaceutical primary standard	grade pharmaceutical primary standard	grade pharmaceutical primary standard	grade -
storage temp. 2-8°C	storage temp. 2-8°C	storage temp. 2-8°C	storage temp. 2-8°C
manufacturer/tradename EDQM	manufacturer/tradename BP	manufacturer/tradename EDQM	manufacturer/tradename -

Application

Riboflavin sodium phosphate EP Reference standard, intended for use in laboratory tests only as specifically prescribed in the European Pharmacopoeia.

General description

This product is provided as delivered and specified by the issuing Pharmacopoeia. All information provided in support of this product, including SDS and any product information leaflets have been developed and issued under the Authority of the Issuing Pharmacopoeia. For further information and support please go to the website of the issuing Pharmacopoeia.

Other Notes

Sales restrictions may apply.

Packaging

The product is delivered as supplied by the issuing Pharmacopoeia. For the current unit quantity, please visit the EDQM reference substance catalogue.

related product

Product No.

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Pricing

PHR1054

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Riboflavin, United States Pharmacopeia (USP) Reference Standard

R0600000

Riboflavin, European Pharmacopoeia (EP) Reference Standard

Y0000757

Riboflavin for peak identification, European Pharmacopoeia (EP) Reference Standard

1535700

Phosphated Riboflavin, United States Pharmacopeia (USP) Reference Standard

PHR1936

Riboflavin Impurity A, Pharmaceutical Secondary Standard; Certified Reference Material

BP459

Riboflavin sodium phosphate, British Pharmacopoeia (BP) Reference Standard

PHR2570

Riboflavin Impurity B, Pharmaceutical Secondary Standard; Certified Reference Material

Storage Class

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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Nitric oxide synthase domain interfaces regulate electron transfer and calmodulin activation.

Brian C Smith et al.

Proceedings of the National Academy of Sciences of the United States of America, 110(38), E3577-E3586 (2013-09-05)

Nitric oxide (NO) produced by NO synthase (NOS) participates in diverse physiological processes such as vasodilation, neurotransmission, and the innate immune response. Mammalian NOS isoforms are homodimers composed of two domains connected by an intervening calmodulin-binding region. The N-terminal oxidase

Detection of a quaternary organization into dimer of trimers of Corynebacterium ammoniagenes FAD synthetase at the single-molecule level and at the in cell level.

Carlos Marcuello et al.

Biochimica et biophysica acta, 1834(3), 665-676 (2013-01-08)

Biochemical characterization of Corynebacterium ammoniagenes FADS (CaFADS) pointed to certain confusion about the stoichiometry of this bifunctional enzyme involved in the production of FMN and FAD in prokaryotes. Resolution of its crystal structure suggested that it might produce a hexameric

Alternative pyrimidine biosynthesis protein ApbE is a flavin transferase catalyzing covalent attachment of FMN to a threonine residue in bacterial flavoproteins.

Yulia V Bertsova et al.

The Journal of biological chemistry, 288(20), 14276-14286 (2013-04-06)

Na(+)-translocating NADH:quinone oxidoreductase (Na(+)-NQR) contains two flavin residues as redox-active prosthetic groups attached by a phosphoester bond to threonine residues in subunits NqrB and NqrC. We demonstrate here that flavinylation of truncated Vibrio harveyi NqrC at Thr-229 in Escherichia coli

The transfer of reduced flavin mononucleotide from LuxG oxidoreductase to luciferase occurs via free diffusion.

Ruchanok Tinikul et al.

Biochemistry, 52(39), 6834-6843 (2013-09-06)

Bacterial luciferase (LuxAB) is a two-component flavin mononucleotide (FMN)-dependent monooxygenase that catalyzes the oxidation of reduced FMN (FMNH(-)) and a long-chain aliphatic aldehyde by molecular oxygen to generate oxidized FMN, the corresponding aliphatic carboxylic acid, and concomitant emission of light.

Gene regulation by riboswitches with and without negative feedback loop.

Jong-Chin Lin et al.

Biophysical journal, 103(11), 2320-2330 (2013-01-04)

Riboswitches, structured elements in the untranslated regions of messenger RNAs, regulate gene expression by binding specific metabolites. We introduce a kinetic network model that describes the functions of riboswitches at the systems level. Using experimental data for flavin mononucleotide riboswitch

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