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Thermo Scientific Chemicals
Flavin adenine dinucleotide disodium salt hydrate, 94% (dry wt.), water <10%
CAS: 1891059-93-0 | C27H31N9Na2O15P2 | 829.52 g/mol
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CAS1891059-93-0
規格
規格表
規格表Water Content (Karl Fischer Titration)<10.0%
pH5.5 - 6.5
FormPowder
Identification (FTIR)Conforms
Optical Rotation-23.2? ? 2.3? (c=2 in water)
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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.
This Thermo Scientific Chemicals brand product was originally part of the Alfa Aesar product portfolio. Some documentation and label information may refer to the legacy brand. The original Alfa Aesar product / item code or SKU reference has not changed as a part of the brand transition to Thermo Scientific Chemicals.
Applications
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.
Solubility
Soluble in water (50 mg/ml).
Notes
Store at 4°C. Store in cool, dry conditions in a well sealed container. Store away from oxidizing agents.
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.
Solubility
Soluble in water (50 mg/ml).
Notes
Store at 4°C. Store in cool, dry conditions in a well sealed container. Store away from oxidizing agents.
RUO – Research Use Only
General References:
- Enza M Torchetti; Francesco Bonomi; Michele Galluccio; Elisabetta Gianazza; Teresa A Giancaspero; Stefania Iametti; Cesare Indiveri; Maria Barile. Human FAD synthase (isoform 2): a component of the machinery that delivers FAD to apo-flavoproteins. FEBS Journal. 2011, 278 (22), 4434-4449.
- Djemel Hamdane; Manuela Argentini; David Cornu; Hannu Myllykallio; Stéphane Skouloubris; Gaston Hui-Bon-Hoa; Béatrice Golinelli-Pimpaneau. Insights into folate/FAD-dependent tRNA methyltransferase mechanism: role of two highly conserved cysteines in catalysis. Journal of Biological Chemistry. 2011, 286 (42), 36268-36280.