FAD
CAS 84366-81-4
Purity≥96.0%
Flavin cofactor material for enzyme and assay development
Flavin Adenine Dinucleotide Disodium Salt Powder (CAS 84366-81-4), specification ≥96.0%. Orange-yellow flavin coenzyme powder for biochemical reagent and enzyme-reaction evaluation. Batch COA and evaluation samples are available. MOQ: 10 g. NAD+ ingredients
Quote / sample & delivery
Key Specifications
| Product Positioning | Flavin cofactor material for enzyme and assay development |
| Application Scenarios | flavoprotein enzyme assays · oxidoreductase research · diagnostic reagent development |
| CAS Number | 84366-81-4 |
| Purity | ≥96.0% |
| Molecular Formula | C₂₇H₃₁N₉O₁₅P₂·2Na |
| Molecular Weight | 829.53 g/mol |
| Appearance | Orange-yellow powder |
| Solubility | Soluble in water |
| Storage | ≤-20°C, protect from light |
| Shelf Life | 18 months |
Procurement & delivery
Supply details confirmed by intended use, volume and target market
Flavin adenine dinucleotide disodium salt (FAD disodium salt, CAS 84366-81-4) is the sodium-stabilized form of FAD, a dinucleotide redox coenzyme built from a flavin mononucleotide (riboflavin phosphate) unit joined to adenosine monophosphate through a pyrophosphate bridge. Its molecular formula is C27H31N9O15P2·2Na (MW 829.53 g/mol), and it appears as an orange-yellow powder with ≥96.0% purity. FAD occurs naturally in every living cell as the prosthetic group of flavoenzymes and is biosynthesized from vitamin B2 (riboflavin). Commercial bulk material is typically produced through a biosynthetic route: riboflavin generated by microbial fermentation is enzymatically phosphorylated to FMN and then adenylylated to FAD using ATP-dependent kinase and FAD-synthetase activity, after which the product is purified, converted to its disodium salt, crystallized, and dried into powder.
High-Purity Redox Coenzyme
Assayed at ≥96.0% by HPLC, meeting the purity level required for enzymology research, flavoenzyme reconstitution, and biocatalysis applications.
Biosynthetic Production Control
Manufactured via a controlled microbial fermentation and enzymatic conversion platform rather than uncontrolled extraction, giving batch-to-batch consistency in identity and purity.
Stable Orange-Yellow Powder Form
Supplied as a free-flowing orange-yellow powder, water-soluble and convenient for accurate weighing, dissolution, and downstream formulation.
Verified Contaminant Testing
Each batch is screened for heavy metals (Pb, Hg, Cd, As) and microbial limits, with full certificates of analysis available on request.
Flexible Bulk & OEM Supply
Available from gram-scale research quantities to industrial bulk packaging, with OEM/private-label and customized packaging options for B2B partners.
Test items, specifications and results for the listed batch are shown here. View or request a COA in the quality documents section.
Batch No.
PGFAD-260515
Test date
2026-05-16
Specification
In-house
Pack size
1 g, 5 g/bottle
Storage
≤-20°C, protect from light
Conclusion
Conforms
| Test Item | Specification | Result |
|---|---|---|
| Appearance | Orange yellowish powder | Complies |
| Identification | HPLC main peak retention time consistent with reference | Complies |
| State of solution | Orange yellow and clear | Complies |
| Purity | ≥93.0% | 97.4% |
| Specific rotation (at 20℃) | −25.5 to 21.0° | −22.9° |
| Water (KF) | ≤10% | 4.5% |
| pH | 5.5–6.5 | 6.2 |
| Lead (Pb) | ≤10 ppm | Complies |
| Arsenic (As) | ≤1 ppm | Complies |
| Free phosphoric acid | ≤0.25% | 0.13% |
| Related compounds | ≤0.1% | Complies |
View an available COA in the quality documents section. Check the document for its product form and batch; request a signed COA for your purchasing or shipment batch separately.
Enzyme catalysis
Diagnostic reagent raw materials
FAD disodium is not interchangeable with riboflavin or FMN; design against enzyme-binding requirements.
97.4%
Purity
4.5%
Water (KF)
PGFAD-260515 · Results apply to this lot; interpret purity, assay and water on their respective bases.
Composition candidates, processing sequences and tests support pilot design. Confirm candidate excipients and processes using this material in the actual finished formulation.
Application examples follow the materials, formats and findings actually studied. Combination studies, single-ingredient studies, commercial precedents and development candidates are distinguished.
FAD-GDH contains FAD; its name alone does not imply that every finished enzyme needs added free FAD powder.
Show research and formulation insights +Hide details −Combination / selection rationale: FAD-GDH contains FAD; its name alone does not imply that every finished enzyme needs added free FAD powder.
Published evidence / source details: A 2020 review distinguishes fungal and bacterial multi-subunit FAD-GDH, mediators, direct electron transfer and engineering—not a diagnostic-strip recipe for free FAD.
Development insights: Document enzyme cofactor occupancy and activity first. For reconstitution/supplementation work, compare FAD levels against no-addition controls and measure activity, free-FAD background, mediator and immobilization effects.
Evidence scope: Sensor review and development guidance, not a universal FAD-supplementation requirement.
2020 · FAD-GDH sensor review · DOI 10.1016/j.bioelechem.2019.107414 ↗StyB uses NADH to reduce FAD for StyA-catalysed epoxidation; cofactor loading and enzyme balance affect coupling.
Show research and formulation insights +Hide details −Combination / selection rationale: StyB uses NADH to reduce FAD for StyA-catalysed epoxidation; cofactor loading and enzyme balance affect coupling.
Published evidence / source details: A 2017 study engineered reductase–epoxidase fusions, examined FAD-dependent kinetic behaviour and demonstrated indigoid-dye biocatalysis.
Development insights: Screen FAD, NADH, substrate and enzyme ratios and compare separate/fused enzymes. Measure product, NADH use and peroxide background to assess uncoupling and oxygen supply; convert salt mass to molarity.
Evidence scope: A specific biocatalytic study, not automatic cascade activity or scale-up performance from the powder alone.
2017 · Styrene monooxygenase fusions · DOI 10.1007/s12010-016-2304-4 ↗Literature-Supported Research Directions
FAD is a cofactor for many flavoproteins involved in dehydrogenation, oxidation and monooxygenation, supporting oxidoreductase mechanism, substrate-conversion and enzyme-engineering research.
Citation: Fitzpatrick et al. Substrate dehydrogenation by flavoproteins. Accounts of chemical research (2001). PMID: 11308304.View source
FAD-dependent glucose dehydrogenases are used in electrochemical glucose sensors and enzyme assays, with research focusing on electron transfer, substrate selectivity and signal response.
Citation: Okuda-Shimazaki et al. FAD dependent glucose dehydrogenases - Discovery and engineering of representative glucose sensing enzymes. Bioelectrochemistry (Amsterdam, Netherlands) (2020). PMID: 31838457.View source
FAD-dependent oxidases and monooxygenases support selective oxidation and biomanufacturing. Cofactor purity, photostability and enzyme–cofactor compatibility are key process-development variables.
Citation: Daniel et al. The family of berberine bridge enzyme-like enzymes: A treasure-trove of oxidative reactions. Archives of biochemistry and biophysics (2017). PMID: 28676375.View source
Note: For ingredient R&D and scientific information; findings depend on model, dose, formulation and population and do not constitute a treatment claim or efficacy guarantee.
Lead Time
3–5business days
Standard products are generally in stock; confirm the exact lead time with us.
Minimum Order
10 g
Samples, pilot trials, and commercial volumes are supported.
Foil Pouch
Sealed, moisture-protective inner packaging
Insulated Box + Carton
For products requiring temperature-controlled transport
Bulk Shipping
Palletized and stretch-wrapped for protection
Ambient storage: foil pouch + fiber drum; temperature controlled: foil pouch + insulated box/carton. Confirm by product.
Custom packaging: Custom foil bags or HDPE drums, GMP label printing, and export documentation are available. Contact us for a quote.Images are packaging illustrations.
Certifications
Riboflavin Fermentation
An engineered high-yield microbial strain (e.g., Bacillus subtilis or Ashbya gossypii-type production strains) is fermented to accumulate riboflavin (vitamin B2), the biosynthetic precursor of FAD.
Enzymatic Phosphorylation to FMN
Riboflavin is converted to flavin mononucleotide (FMN) via ATP-dependent riboflavin kinase, either as a purified enzyme step or whole-cell biocatalysis.
Enzymatic Adenylylation to FAD
FMN is further coupled with ATP via FAD synthetase (FMN adenylyltransferase activity) to form flavin adenine dinucleotide (FAD).
Bioconversion Broth Clarification
The bioconversion mixture is clarified by centrifugation and/or membrane filtration to remove cell mass and insoluble debris, yielding a clear FAD-containing solution.
Chromatographic Purification
The clarified solution is purified using ion-exchange and/or adsorption chromatography to separate FAD from residual FMN, riboflavin, salts, and other fermentation by-products.
Sodium Salt Formation & Crystallization
Purified FAD is converted to its disodium salt form under controlled pH and ionic strength, then crystallized to improve stability and handling.
Concentration & Drying
The crystallized product is concentrated and dried, typically by vacuum or spray drying at controlled, moderate temperature to protect the light- and heat-sensitive flavin ring.
Milling, Blending & Quality Release
Dried FAD disodium salt is milled to uniform particle size, blended for lot homogeneity, and released only after passing purity, heavy metal, and microbial testing.
Purity is determined by reverse-phase HPLC with UV detection, typically referenced against a certified FAD standard and monitored at the characteristic flavin absorbance wavelengths (~260 nm and ~450 nm) to distinguish FAD from residual FMN, riboflavin, or ADP/AMP-related impurities. Buyers should confirm the reference standard used, the water/moisture correction applied to the assay result, and request the batch-specific certificate of analysis (COA) before large-scale use.
FAD disodium salt is readily soluble in water, forming a clear light-to-deep orange solution suitable for direct use in enzyme assay buffers, cell culture supplements, or biocatalytic reaction systems. Because the flavin ring is light- and, to a lesser extent, heat-sensitive, aqueous solutions should be freshly prepared where possible, stored cold and protected from light, and used in neutral-pH buffers to minimize degradation; the solid powder itself should be stored sealed, dry, and away from direct light for long-term stability.
Each production batch is tested by HPLC against a reference standard, and results are documented in a batch-specific certificate of analysis (COA), which we provide with every order and can send in advance for review.
It is produced through a biosynthetic route: riboflavin is generated by microbial fermentation, then enzymatically converted to FMN and subsequently to FAD via ATP-dependent kinase and FAD-synthetase activity, followed by purification and salt formation — not through uncontrolled botanical extraction.
It is readily soluble in water, forming a clear orange solution. We recommend preparing solutions fresh, keeping them cold and protected from light, and using a neutral-pH buffer, since the flavin ring is light-sensitive.
Yes, small evaluation samples are available on request so your team can verify purity, appearance, and solubility against your own specifications before committing to a bulk purchase order.
Yes, we supply a batch-specific COA with every shipment, and we support independent third-party testing at accredited labs; retained samples can be provided for buyers who wish to verify results themselves.
Yes, we offer OEM/private-label manufacturing, including customized specifications, labeling, and documentation, for B2B partners looking to market this ingredient under their own brand.
FAD disodium powder pack options are 10 g, 50 g, 100 g. Special inner-packaging, labeling and transport requirements are agreed separately for the order.
The raw-material MOQ for FAD disodium powder is 10 g, with pack options of 10 g, 50 g, 100 g. Enzyme-assay projects should match the disodium identity and assay basis.
No. Some supplied enzymes already contain bound FAD. Document the cofactor-binding state and intended reconstitution or recycling design first. Where supplementation is relevant, compare FAD levels with a no-addition control, testing enzyme activity, free-FAD background, mediators and storage. FAD, FMN and riboflavin are different materials.
Documents are subject to product and batch availability; third-party reports are provided only when applicable.
Quality documents
The specification sheet defines acceptance limits. The COA shows actual batch results, which may vary by batch. Third-party reports are provided only for products or batches that have been independently tested.
Stable acceptance criteria · Available on request
Actual test data · Check the COA for the applicable batch
Technical Resources
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