Analytical Data
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Gene name
SDHD
- Application
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Alternative Names
PGL; PGL1; QPs3; Succinate-ubiquinone reductase membrane anchor subunit; Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9CXV1
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Expression Region
Met1~Leu159
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Molecular Weight
20kDa
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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
SDHD (succinate dehydrogenase subunit D) is a crucial component of the mitochondrial enzyme complex II, playing a vital role in the metabolism of succinate during the tricarboxylic acid (TCA) cycle. Research on SDHD has garnered attention due to its association with hereditary paragangliomas and pheochromocytomas, which are rare neuroendocrine tumors linked to mutations in succinate dehydrogenase (SDH) subunits. Mutations in the SDHD gene disrupt normal enzyme function, leading to increased succinate levels and altered cellular energy metabolism, which can drive tumorigenesis. Additionally, altered expression and activity of SDHD have been implicated in various other cancers, making it a potential biomarker and therapeutic target. Studies on recombinant SDHD proteins aim to elucidate the molecular mechanisms underlying these pathology developments, exploring enzyme kinetics, interaction with other metabolic pathways, and the effects of specific mutations. Understanding the structure-function relationship of SDHD through recombinant protein studies can provide insights into its regulatory roles in cellular metabolism and cancer biology, ultimately contributing to the development of targeted therapies for related malignancies. Such research is crucial for advancing our knowledge of tumor biology and improving clinical outcomes for patients with SDH-related tumors.
