Analytical Data
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Gene name
FLAD1
- Application
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Alternative Names
FLAD1；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
Q8NFF5
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Expression Region
1-490aa
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AA Sequence
MTSRASELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQPFRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEAQAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVEQASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
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Molecular Weight
58.3 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
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Protein Description
FLAD1, or flavin adenine dinucleotide biosynthesis enzyme 1, has garnered significant attention in recent years due to its crucial role in cellular metabolism and maintenance of redox homeostasis. This enzyme is vital for the synthesis of flavin adenine dinucleotide (FAD), a cofactor that is integral to numerous biological processes, including oxidative phosphorylation, flavoprotein-mediated reactions, and enzymatic activity related to amino acid and lipid metabolism. Dysregulation of FLAD1 has been associated with various pathological conditions, including metabolic disorders and some forms of cancer, highlighting its potential as a therapeutic target. Furthermore, the recombinant expression of FLAD1 provides a valuable tool for studying its biochemical properties, functional mechanisms, and interactions with other cellular components. By utilizing techniques such as molecular cloning and protein purification, researchers aim to better understand the structure-function relationships of FLAD1 and explore its applications in biotechnology and medicine. The development of FLAD1-based therapies could lead to novel intervention strategies for diseases linked to metabolic dysregulation, making it a promising candidate for further study and exploration in the field of metabolic engineering and therapeutic development.
