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F6625

Sigma-Aldrich

Flavin adenine dinucleotide disodium salt hydrate

≥95% (HPLC), powder

Sinonimo/i:

FAD, FAD-Na2, Riboflavin 5′-adenosine diphosphate disodium salt, FAD-Na2

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10 MG
CHF 85.70
25 MG
CHF 91.50
100 MG
CHF 121.00
250 MG
CHF 205.00
500 MG
CHF 370.00
1 G
CHF 670.00

CHF 85.70


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Cambia visualizzazione
10 MG
CHF 85.70
25 MG
CHF 91.50
100 MG
CHF 121.00
250 MG
CHF 205.00
500 MG
CHF 370.00
1 G
CHF 670.00

About This Item

Formula empirica (notazione di Hill):
C27H31N9Na2O15P2 · xH2O
Numero CAS:
Peso molecolare:
829.51 (anhydrous basis)
Beilstein:
5326842
Numero MDL:
Codice UNSPSC:
41106305
ID PubChem:
NACRES:
NA.51

CHF 85.70


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Origine biologica

microbial

Saggio

≥95% (HPLC)

Stato

powder

Colore

yellow to orange-brown

Solubilità

H2O: soluble-50 mg/mL, clear, slightly orang to deep orange

Temperatura di conservazione

−20°C

Stringa SMILE

[Na+].[Na+].[H]O[H].Cc1cc2N=C3C(=O)NC(=O)N=C3N(C[C@H](O)[C@H](O)[C@H](O)COP([O-])(=O)OP([O-])(=O)OC[C@H]4O[C@H]([C@H](O)[C@@H]4O)n5cnc6c(N)ncnc56)c2cc1C

InChI

1S/C27H33N9O15P2.2Na.H2O/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36;;;/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43);;;1H2/q;2*+1;/p-2/t14-,15+,16+,19-,20+,21+,26+;;;/m0.../s1
GXTPHHZYFMAGLX-UJXBNFGUSA-L

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Descrizione generale

Flavin adenine dinucleotide disodium salt hydrate (FAD-Na2) is an adenine-containing enzymatic redox cofactor[1]. Also known as flavin cofactors, FAD is critical electron transporter in living systems.[2] They catalyze several 1-2 electron redox reactions. e.g., β-oxidation of fatty acids occurs in the presence of FAD as a cofactor.[3] FAD is one of the two active coenzymes of vitamin B12(riboflavin).[4] FAD displays a significantly shorter excited state lifetime in aqueous solutions than its analog, flavin mononucleotide.[2]

Applicazioni

FAD is used to remove reactive oxygen species (ROS) from mammalian cells. The fluorescence mechanism of FAD is used to study energy-dependent intramitochondrial redox potential.[5] FAD is used as a predominant fluorophore to study unstained eosinophils, which exhibit autofluorescence compared to other leucocytes.[6]
Flavin adenine dinucleotide (FAD) is used as a redox cofactor (electron carrier) by flavoproteins including succinate dehydrogenase (complex), α-ketoglutarate dehydrogenase, apoptosis-inducing factor 2 (AIF-M2, AMID), folate/FAD-dependent tRNA methyltransferases, and N-hydroxylating flavoprotein monooxygenases. FAD is a component of the pyruvate dehydrogenase complex.

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 3

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, type N95 (US)


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I clienti hanno visto anche

A N Mayeno et al.
Journal of leukocyte biology, 51(2), 172-175 (1992-02-01)
Unstained human eosinophils exhibit marked autofluorescence in comparison to other leukocytes due to a granule-associated fluorescent substance. Fluorescence spectroscopy of granule extracts reveals excitation maxima at approximately 380 and approximately 450 nm with a single emission at approximately 520, characteristic
Martina Kieninger et al.
Biomolecules, 10(4) (2020-04-15)
Flavin cofactors, like flavin adenine dinucleotide (FAD), are important electron shuttles in living systems. They catalyze a wide range of one- or two-electron redox reactions. Experimental investigations include UV-vis as well as infrared spectroscopy. FAD in aqueous solution exhibits a
J Rösner et al.
Journal of microscopy, 264(2), 215-223 (2016-07-02)
Dynamic alterations in flavin adenine dinucleotide (FAD) fluorescence permit insight into energy metabolism-dependent changes of intramitochondrial redox potential. Monitoring FAD fluorescence in living tissue is impeded by photobleaching, restricting the length of microfluorimetric recordings. In addition, photodecomposition of these essential
Ruofan Cao et al.
Journal of biomedical optics, 25(1), 1-16 (2020-01-11)
Two-photon fluorescence lifetime imaging microscopy (FLIM) is widely used to capture autofluorescence signals from cellular components to investigate dynamic physiological changes in live cells and tissues. Among these intrinsic fluorophores, nicotinamide adenine dinucleotide (phosphate) (NAD(P)H) and flavin adenine dinucleotide (FAD)-essential
João L Lagarto et al.
Sensors (Basel, Switzerland), 19(12) (2019-06-16)
Single Photon Avalanche Diode (SPAD) arrays are increasingly exploited and have demonstrated potential in biochemical and biomedical research, both for imaging and single-point spectroscopy applications. In this study, we explore the application of SPADs together with fiber-optic-based delivery and collection

Articoli

Serotonin is stored in cells and metabolized by MAO, influencing CNS, GI, and platelet functions.

Cellular oxidative stress is countered by enzymatic scavengers and antioxidant modulators against reactive oxygen species damage.

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