Analytical Data
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Gene name
SDH
- Application
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Alternative Names
SDH；C11orf79；PGL2；SDH5；Succinate dehydrogenase assembly factor 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
P20132
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Expression Region
1-328aa
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AA Sequence
MMSGEPLHVKTPIRDSMALSKMAGTSVYLKMDSAQPSGSFKIRGIGHFCKRWAKQGCAHFVCSSAGNAGMAAAYAARQLGVPATIVVPSTTPALTIERLKNEGATVKVVGELLDEAFELAKALAKNNPGWVYIPPFDDPLIWEGHASIVKELKETLWEKPGAIALSVGGGGLLCGVVQGLQEVGWGDVPVIAMETFGAHSFHAATTAGKLVSLPKITSVAKALGVKTVGAQALKLFQEHPIFSEVISDQEAVAAIEKFVDDEKILVEPACGAALAAVYSHVIQKLQLEGNLRTPLPSLVVIVCGGSNISLAQLRALKEQLGMTNRLPK
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Molecular Weight
42.1 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
SDH, or succinate dehydrogenase, is a crucial enzyme within the mitochondrial respiratory chain, playing a dual role in both the tricarboxylic acid cycle and oxidative phosphorylation. Dysfunctional SDH is implicated in various metabolic disorders and certain types of cancer, notably paragangliomas and pheochromocytomas. The enzyme consists of four subunits—SDHA, SDHB, SDHC, and SDHD—that work in tandem to facilitate the conversion of succinate to fumarate while simultaneously reducing ubiquinone to ubiquinol. Due to its pivotal role in energy metabolism and reactive oxygen species production, understanding the structure and function of SDH is essential for elucidating its biochemical pathways and regulatory mechanisms. Research into SDH has gained momentum with advances in structural biology techniques, leading to detailed insights into its assembly, stability, and interactions with other metabolic pathways. Moreover, the characterization of pathogenic mutations in SDH subunits has opened new avenues for targeted therapies and biomarker discovery, emphasizing SDH as a significant focus in cancer research and metabolic disease. Comprehensive studies on SDH not only enhance our understanding of its fundamental biological functions but also potentially contribute to the development of novel therapeutic strategies for diseases associated with SDH dysfunction. As such, the ongoing investigation of SDH and its recombinant proteins serves as a cornerstone for both basic and applied research in biochemistry, molecular biology, and medical science.
