Analytical Data
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Gene name
SFXN1
- Application
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Alternative Names
SFXN1；Sideroflexin-1
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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
Q9H9B4
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Expression Region
1-322aa
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AA Sequence
MSGELPPNINIKEPRWDQSTFIGRANHFFTVTDPRNILLTNEQLESARKIVHDYRQGIVPPGLTENELWRAKYIYDSAFHPDTGEKMILIGRMSAQVPMNMTITGCMMTFYRTTPAVLFWQWINQSFNAVVNYTNRSGDAPLTVNELGTAYVSATTGAVATALGLNALTKHVSPLIGRFVPFAAVAAANCINIPLMRQRELKVGIPVTDENGNRLGESANAAKQAITQVVVSRILMAAPGMAIPPFIMNTLEKKAFLKRFPWMSAPIQVGLVGFCLVFATPLCCALFPQKSSMSVTSLEAELQAKIQESHPELRRVYFNKGL
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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
SFXN1, or sideroflexin 1, is a mitochondrial protein that has garnered increasing attention in the field of molecular biology due to its potential roles in iron metabolism and mitochondrial function. As an essential component of the mitochondrial inner membrane, SFXN1 is believed to be involved in the transport of metabolites and may play a crucial role in maintaining cellular iron homeostasis. Dysregulation of iron levels within mitochondria can lead to various pathologies, including neurodegenerative diseases and metabolic disorders. Recent studies have indicated that mutations or altered expression of SFXN1 could contribute to iron-related diseases, highlighting the need for further investigation. The recombinant production of SFXN1 protein allows for in-depth studies of its biochemical properties, interaction with other cellular components, and its functional implications in iron-sulfur cluster biogenesis. By utilizing advanced techniques such as protein purification and structural analysis, researchers aim to elucidate the precise mechanisms by which SFXN1 operates within mitochondrial pathways. This understanding could potentially open new avenues for therapeutic interventions in diseases associated with iron dysregulation. Overall, the study of SFXN1 and its recombinant protein provides a promising direction for unraveling the complexities of mitochondrial biology and iron metabolism.
