Analytical Data
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Gene name
NDUFV2
- Application
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Alternative Names
NDUFV2;NADH dehydrogenase [ubiquinone] flavoProtein 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
P19404
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Expression Region
33-249aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSGAGGALF VHRDTPENNP DTPFDFTPEN YKRIEAIVKN YPEGHKAAAV LPVLDLAQRQ NGWLPISAMN KVAEVLQVPP MRVYEVATFY TMYNRKPVGK YHIQVCTTTP CMLRNSDSIL EAIQKKLGIK VGETTPDKLF TLIEVECLGA CVNAPMVQIN DNYYEDLTAK DIEEIIDELK AGKIPKPGPR SGRFSCEPAG GLTSLTEPPK GPGFGVQAGL
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Molecular Weight
26 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
NDUFV2, or NADH:ubiquinone oxidoreductase core subunit, is a crucial component of complex I in the mitochondrial electron transport chain, which plays a vital role in cellular respiration and energy production. Dysfunction or mutations in the NDUFV2 gene have been linked to various mitochondrial diseases, characterized by impaired energy metabolism and a range of clinical symptoms affecting multiple organ systems. Recent studies have highlighted the significance of NDUFV2 in maintaining mitochondrial integrity and function, as well as its involvement in oxidative stress responses. Understanding the structure, function, and dynamics of NDUFV2 can provide insights into the mechanisms underlying mitochondrial pathologies and offer potential therapeutic targets for intervention. Research on recombinant NDUFV2 proteins has gained traction, aiming to elucidate the protein’s functional characteristics, interactions with other mitochondrial components, and the molecular basis of its role in complex I. By employing techniques such as X-ray crystallography, cryo-electron microscopy, and biochemical assays, scientists strive to uncover the intricate details of NDUFV2's structure-function relationship, paving the way for advancements in treating mitochondrial disorders and enhancing our comprehension of mitochondrial bioenergetics. Moreover, elucidating the biology of NDUFV2 may also contribute to the broader understanding of aging and metabolic diseases, reinforcing its importance in both basic and applied research.
