Analytical Data
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Gene name
FAD
- Application
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Alternative Names
FAD；FAD synthase
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49768
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Expression Region
1-467aa
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AA Sequence
MTELPAPLSYFQNAQMSEDNHLSNTVRSQNDNRERQEHNDRRSLGHPEPLSNGRPQGNSRQVVEQDEEEDEELTLKYGAKHVIMLFVPVTLCMVVVVATIKSVSFYTRKDGQLIYTPFTEDTETVGQRALHSILNAAIMISVIVVMTILLVVLYKYRCYKVIHAWLIISSLLLLFFFSFIYLGEVFKTYNVAVDYITVALLIWNFGVVGMISIHWKGPLRLQQAYLIMISALMALVFIKYLPEWTAWLILAVISVYDLVAVLCPKGPLRMLVETAQERNETLFPALIYSSTMVWLVNMAEGDPEAQRRVSKNSKYNAESTERESQDTVAENDDGGFSEEWEAQRDSHLGPHRSTPESRAAVQELSSSILAGEDPEERGVKLGLGDFIFYSVLVGKASATASGDWNTTIACFVAILIGLCLTLLLLAIFKKALPALPISITFGLVFYFATDYLVQPFMDQLAFHQFYI
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Molecular Weight
52.6 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
FAD (Flavin Adenine Dinucleotide) is an essential cofactor involved in various biological processes, including redox reactions and metabolic pathways. Research on FAD recombinant proteins has gained significant attention due to their pivotal roles in enzymatic functions and cellular metabolism. These proteins are often crucial in the study of flavoproteins, which are a group of proteins that contain FAD as a prosthetic group, enabling them to participate in electron transfer reactions. The recombinant production of FAD-binding proteins allows for detailed investigations into their structures, functions, and mechanisms, facilitating a deeper understanding of their roles in biological systems. Furthermore, these proteins are of great interest in biotechnology and pharmaceutical industries, where engineered FAD-dependent enzymes can be utilized for various applications, including biocatalysis and drug development. Advances in genetic engineering and protein expression technologies have enhanced the ability to produce these proteins in significant quantities and with desired properties, leading to more effective studies on their biophysical and biochemical characteristics. Consequently, research into FAD recombinant proteins not only elucidates fundamental biochemical pathways but also opens up new avenues for industrial applications, highlighting their importance in both basic and applied sciences.
