Analytical Data
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Gene name
SDHA
- Application
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Alternative Names
Flavoprotein subunit of complex II ;Fp
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31040
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Expression Region
44-293aa
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Molecular Weight
54.1 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
Related Products
Protein Description
Succinate dehydrogenase (SDH) is a crucial enzyme that plays a dual role in both the tricarboxylic acid (TCA) cycle and the electron transport chain, making it integral to cellular respiration and energy production. Research into SDH has gained significant traction due to its association with metabolic disorders and certain types of cancer, notably familial paraganglioma and pheochromocytoma, which are linked to mutations in its subunit genes. Moreover, the enzyme's regulation and function are implicated in the broader context of metabolic reprogramming, especially under hypoxic conditions prevalent in tumors. The recombinant expression of SDH proteins allows for in-depth studies of their structural and functional properties, facilitating investigations into how mutations affect enzyme activity and stability. This approach not only enhances our understanding of the enzyme's role in normal physiology and disease but also aids in the development of potential therapeutic strategies targeting SDH-related pathways. Ongoing research is also directed at exploring the enzyme's regulatory mechanisms and its interactions with other metabolic pathways, highlighting its significance in the intricate balance of energy metabolism within cells. Overall, the study of recombinant SDHA (the gene encoding for the A subunit of SDH) proteins is pivotal for advancing our comprehension of both basic biochemistry and its relevance to human health and disease.
