Analytical Data
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Gene name
NDUFS2
- Application
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Alternative Names
NDUFS2;NADH dehydrogenase [ubiquinone] iron-sulfur Protein 2. 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
O75306
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Expression Region
1-463aa
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AA Sequence
MAALRALCGFRGVAAQVLRPGAGVRLPIQPSRGVRQWQPDVEWAQQFGGA VMYPSKETAHWKPPPWNDVDPPKDTIVKNITLNFGPQHPAAHGVLRLVME LSGEMVRKCDPHIGLLHRGTEKLIEYKTYLQALPYFDRLDYVSMMCNEQA YSLAVEKLLNIRPPPRAQWIRVLFGEITRLLNHIMAVTTHALDLGAMTPF FWLFEEREKMFEFYERVSGARMHAAYIRPGGVHQDLPLGLMDDIYQFSKN FSLRLDELEELLTNNRIWRNRTIDIGVVTAEEALNYGFSGVMLRGSGIQW DLRKTQPYDVYDQVEFDVPVGSRGDCYDRYLCRVEEMRQSLRIIAQCLNK MPPGEIKVDDAKVSPPKRAEMKTSMESLIHHFKLYTEGYQVPPGATYTAI EAPKGEFGVYLVSDGSSRPYRCKIKAPGFAHLAGLDKMSKGHMLADVVAI IGTQDIVFGEVDR
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Molecular Weight
79 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
NDUFS2, or NADH:ubiquinone oxidoreductase (Complex I) subunit S2, is a critical component of the mitochondrial respiratory chain, playing an essential role in cellular energy metabolism. Mutations in the NDUFS2 gene are linked to various mitochondrial diseases, particularly affecting energy production, leading to conditions such as Leigh syndrome, which manifests in neurological deficits and multi-organ dysfunction. Given the pivotal role of Complex I in oxidative phosphorylation, the study of NDUFS2 is crucial for understanding disease mechanisms and developing potential therapies targeting mitochondrial dysfunction. Research has focused on characterizing the structural and functional aspects of the NDUFS2 protein, investigating how specific mutations impair its activity and contribute to clinical phenotypes. Additionally, the generation of recombinant NDUFS2 protein allows for detailed biochemical studies, enabling scientists to explore its interactions within the mitochondrial complex and assess the efficacy of small molecules aimed at restoring its function. As mitochondrial diseases often result in severe clinical outcomes and limited treatment options, understanding the biology of NDUFS2 can pave the way for innovative therapeutic strategies, making it a significant focus in the field of translational medicine.
