Analytical Data
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Gene name
FMN2
- Application
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NZ56
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Expression Region
1284-1722aa
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AA Sequence
KQPIEPCRPMKPLYWTRIQLHSKRDSSTSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHGRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNGGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCLFPLPEPQDLFQASQMKFEDFQKDLRKLKKDLKACEVEAGKVYQVSSKEHMQPFKENMEQFIIQAKIDQEAEENSLTETHKCFLETTAYFFMKPKLGEKEVSPNAFFSIWHEFSSDFKDFWKKENKLLLQERVKEAEEVCRQKKGKSLYKIKPRHDSGIKAKISMKT
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Molecular Weight
57.7 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
FMN2 (flavin mononucleotide protein 2) is a member of the flavin-dependent enzyme family involved in various biological processes, including cellular redox regulation and electron transfer reactions. Recent research has highlighted its potential roles in fundamental cellular pathways such as metabolism, signaling, and gene expression. Mutations in the FMN2 gene have been associated with different diseases, including certain neurological disorders, making it a subject of increased interest in biomedical research. The recombinant production of FMN2 protein allows for in-depth characterization of its biochemical properties and functional mechanisms. By studying the structural and functional aspects of FMN2, researchers aim to elucidate its specific roles in cellular physiology and its implications in disease pathology. Furthermore, understanding FMN2's interactions with other cellular components can provide insights into its involvement in complex signaling networks. As a potential therapeutic target, elucidating the mechanisms of FMN2 could lead to innovative strategies for treating associated disorders and enhancing our knowledge of flavin-dependent enzymatic processes. The development of recombinant FMN2 not only facilitates these investigations but also advances techniques in protein engineering and synthetic biology.
