Analytical Data
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Gene name
SFXN3
- Application
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Alternative Names
SFXN3；Sideroflexin-3
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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
Q9BWM7
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Expression Region
1-321aa
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AA Sequence
MGELPLDINIQEPRWDQSTFLGRARHFFTVTDPRNLLLSGAQLEASRNIVQNYRAGVVTPGITEDQLWRAKYVYDSAFHPDTGEKVVLIGRMSAQVPMNMTITGCMLTFYRKTPTVVFWQWVNQSFNAIVNYSNRSGDTPITVRQLGTAYVSATTGAVATALGLKSLTKHLPPLVGRFVPFAAVAAANCINIPLMRQRELQVGIPVADEAGQRLGYSVTAAKQGIFQVVISRICMAIPAMAIPPLIMDTLEKKDFLKRRPWLGAPLQVGLVGFCLVFATPLCCALFPQKSSIHISNLEPELRAQIHEQNPSVEVVYYNKGL
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Molecular Weight
35 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
SFXN3 (Sideroflexin 3) is a relatively less studied member of the sideroflexin family, which is pivotal in cellular iron metabolism. Recent research has highlighted its potential role in mitochondrial function and iron homeostasis. SFXN3 is believed to facilitate the transport of specific metabolites and might have implications in various physiological and pathological processes, including neurodegenerative diseases where iron accumulation is a common feature. Understanding the molecular mechanisms by which SFXN3 operates can provide insights into its function in cellular metabolism and its contribution to diseases linked with iron dysregulation. The expression and activity of SFXN3 are modulated by several factors, including cellular iron levels and oxidative stress, suggesting that its role may be context-dependent. Additionally, the recombinant protein SFXN3 is utilized in studies to elucidate its structural characteristics and functional properties. As research progresses, the exploration of SFXN3 not only aids in unraveling its biological significance but also has the potential to inform therapeutic strategies aimed at alleviating conditions associated with iron mismanagement. Thus, the study of SFXN3 and its recombinant forms is a promising avenue for understanding the intricate balance of iron metabolism and mitochondrial health in both normal and diseased states.
