Analytical Data
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Gene name
NDUFS4
- Application
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Alternative Names
NDUFS4;NADH dehydrogenase [ubiquinone] iron-sulfur Protein 4. mitochondrial
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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
O43181
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Expression Region
43-175aa
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AA Sequence
AQDQTQDT QLITVDEKLD ITTLTGVPEE HIKTRKVRIF VPARNNMQSG VNNTKKWKME FDTRERWENP LMGWASTADP LSNMVLTFST KEDAVSFAEK NGWSYDIEER KVPKPKSKSY GANFSWNKRT RVSTK
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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
NDUFS4, or NADH:ubiquinone oxidoreductase core subunit S4, is a critical component of the mitochondrial respiratory chain, specifically within Complex I. This multi-subunit enzyme plays a pivotal role in cellular energy metabolism by facilitating the transfer of electrons from NADH to ubiquinone, ultimately contributing to ATP production through oxidative phosphorylation. Mutations in the NDUFS4 gene have been associated with various mitochondrial disorders, which can lead to severe neurological and muscular dysfunctions in affected individuals. As a result, understanding the structure and function of NDUFS4 is essential for elucidating the pathophysiology of these diseases. The study of recombinant NDUFS4 proteins provides an opportunity to dissect the biochemical properties of this subunit, explore its interactions with other Complex I components, and assess the effects of specific mutations on its function. Advances in recombinant DNA technology and protein purification techniques have enabled researchers to produce and analyze NDUFS4 in vitro, which is crucial for developing potential therapeutic strategies aimed at restoring function in patients with NDUFS4-related disorders. Through these investigations, insights into the mechanisms of mitochondrial dysfunction can be gained, potentially leading to targeted interventions that could alleviate symptoms or improve quality of life for patients suffering from mitochondrial diseases linked to NDUFS4 mutations.
